https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Whitney+SmithProteopedia - User contributions [en]2026-09-15T21:35:05ZUser contributionsMediaWiki 1.43.8https://proteopedia.org/index.php?title=Aromatase&diff=1329754Aromatase2011-12-08T15:47:15Z<p>Whitney Smith: </p>
<hr />
<div><br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome P450 family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.<ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.<ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring<ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol.<ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, alcohol and smoking.<ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian CYP enzymes, the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino acid residues.<ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site.<ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> docks in a region adjacent to the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of aromatase includes twelve major α-helices and ten β-strands.<ref name="structure" /> An androstenedione molecule is bound in the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of aromatase stop estrogen production in post-menopausal women. This action is done by blocking the aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen.<ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three aromatase inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase inhibitors are unable to stop ovaries from producing estrogen; therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase deficiency is rare in humans; however, if aromatase is nonfunctional due to a mutation, estrogen synthesis cannot occur. Affected females are diagnosed at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation, epiphyseal closure, bone pain, and excess adiposy.<ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.<ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Aromatase&diff=1329753Aromatase2011-12-08T15:45:48Z<p>Whitney Smith: New page: = Aromatase = <Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB...</p>
<hr />
<div><br />
= Aromatase =<br />
<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome P450 family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.<ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.<ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring<ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol.<ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, alcohol and smoking.<ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian CYP enzymes, the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino acid residues.<ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site.<ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> docks in a region adjacent to the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of aromatase includes twelve major α-helices and ten β-strands.<ref name="structure" /> An androstenedione molecule is bound in the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of aromatase stop estrogen production in post-menopausal women. This action is done by blocking the aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen.<ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three aromatase inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase inhibitors are unable to stop ovaries from producing estrogen; therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase deficiency is rare in humans; however, if aromatase is nonfunctional due to a mutation, estrogen synthesis cannot occur. Affected females are diagnosed at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation, epiphyseal closure, bone pain, and excess adiposy.<ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.<ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1329752Sandbox Reserved 3822011-12-08T15:42:55Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome P450 family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.<ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.<ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring<ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol.<ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, alcohol and smoking.<ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian CYP enzymes, the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino acid residues.<ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site.<ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> docks in a region adjacent to the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of aromatase includes twelve major α-helices and ten β-strands.<ref name="structure" /> An androstenedione molecule is bound in the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of aromatase stop estrogen production in post-menopausal women. This action is done by blocking the aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen.<ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three aromatase inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase inhibitors are unable to stop ovaries from producing estrogen; therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase deficiency is rare in humans; however, if aromatase is nonfunctional due to a mutation, estrogen synthesis cannot occur. Affected females are diagnosed at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation, epiphyseal closure, bone pain, and excess adiposy.<ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.<ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1329728Sandbox Reserved 3822011-12-08T00:41:02Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome P450 family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.<ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.<ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring<ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol.<ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-M/illerian hormone, alcohol and smoking.<ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian CYP enzymes, the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino acid residues.<ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site.<ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> docks in a region adjacent to the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of aromatase includes twelve major α-helices and ten β-strands.<ref name="structure" /> An androstenedione molecule is bound in the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of aromatase stop estrogen production in post-menopausal women. This action is done by blocking the aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen.<ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three aromatase inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase inhibitors are unable to stop ovaries from producing estrogen; therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase deficiency is rare in humans; however, if aromatase is nonfunctional due to a mutation, estrogen synthesis cannot occur. Affected females are diagnosed at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation, epiphyseal closure, bone pain, and excess adiposy.<ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.<ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1329727Sandbox Reserved 3822011-12-08T00:37:13Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome P450 family (CYP). During aromatization reactions, aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome P450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell, and tissue specific promoters regulate its activity.<ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue.<ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring<ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" ''Journal of Steroid Biochemistry and Molecular Biology''. [Online] '''2010''',Vol. 118, Issue 4-5, p197-202. [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol.<ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce the female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking.<ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian CYP enzymes, the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino acid residues.<ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site.<ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> docks in a region adjacent to the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of aromatase includes twelve major α-helices and ten β-strands.<ref name="structure" /> An androstenedione molecule is bound in the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of aromatase stop estrogen production in post-menopausal women. This action is done by blocking the aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen.<ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three aromatase inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase inhibitors are unable to stop ovaries from producing estrogen; therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase deficiency is rare in humans; however, if aromatase is nonfunctional due to a mutation, estrogen synthesis cannot occur. Affected females are diagnosed at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation, epiphyseal closure, bone pain, and excess adiposy.<ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia.<ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327544Sandbox Reserved 3822011-12-02T19:55:15Z<p>Whitney Smith: /* Disorders */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site. <ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> is the region attached to the the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation, epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited in an autosomal dominant manner, affecting females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327543Sandbox Reserved 3822011-12-02T19:54:24Z<p>Whitney Smith: /* Disorders */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site. <ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> is the region attached to the the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation, epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327542Sandbox Reserved 3822011-12-02T19:52:18Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site. <ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> is the region attached to the the porphyrin. Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327541Sandbox Reserved 3822011-12-02T19:52:05Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site. <ref> PMID: 16395678 </ref> The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> is the region attached to the the porphyrin.<br />
Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. '''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327540Sandbox Reserved 3822011-12-02T19:50:59Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing <scene name='Sandbox_Reserved_382/Porphyrin/1'>porphyrin</scene> group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327539Sandbox Reserved 3822011-12-02T19:45:18Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> <br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer. <br />
There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327538Sandbox Reserved 3822011-12-02T19:41:38Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
<br />
<br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/3'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327489Sandbox Reserved 3822011-12-01T16:38:54Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/]</ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/2'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327488Sandbox Reserved 3822011-12-01T16:37:00Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"> PMID:2826573 </ref>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/2'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327487Sandbox Reserved 3822011-12-01T16:31:35Z<p>Whitney Smith: /* Function */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase is the only known enzyme in vertebrates capable of catalyzing the aromatization of a six-membered ring <ref name="structure"/>. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/2'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327486Sandbox Reserved 3822011-12-01T16:28:52Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left| Ribbon diagram displaying the overall structure of human placental aromatase. <ref name="structure"/>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/2'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327325Sandbox Reserved 3822011-11-30T23:56:02Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref name="structure">Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/3'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/2'>ligand</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327318Sandbox Reserved 3822011-11-30T23:39:06Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. <ref> PMID:21125383 </ref> In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref name="structure">Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327316Sandbox Reserved 3822011-11-30T23:36:40Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref name="structure">Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref name="structure" />. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327314Sandbox Reserved 3822011-11-30T23:35:15Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref name="products" /> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref name="structure">Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] name="structure"</ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327313Sandbox Reserved 3822011-11-30T23:34:13Z<p>Whitney Smith: /* Introduction */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref name="products"> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
<br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref name="structure">Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] name="structure"</ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327312Sandbox Reserved 3822011-11-30T23:32:33Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref name="structure">Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref name="structure" /> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] name="structure"</ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327311Sandbox Reserved 3822011-11-30T23:28:41Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] name="structure"</ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref name="structure" /><br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327310Sandbox Reserved 3822011-11-30T23:26:13Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] name"structure"</ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein. <ref> "structure"</ref><br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327309Sandbox Reserved 3822011-11-30T23:24:46Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
'''A ribbon diagram displaying the overall structure of the human placental aromatase is shown to the left.''' The amino terminus starts at residue 45 and is shown in dark blue. The carboxyl terminus ending at residue 496 is shown in red. The helices are labeled A-L and the sheets are labeled 1-10 accordingly. The heme group and the bound ligand are shown in the center of the protein.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327308Sandbox Reserved 3822011-11-30T23:19:08Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand (Cys437)</scene> is the region attached to the the porphyrin.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327307Sandbox Reserved 3822011-11-30T23:09:43Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is within the porphyrin and is considered the reaction center of the enzyme. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand</scene> is the region attached to the the porphyrin.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327306Sandbox Reserved 3822011-11-30T23:05:31Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The reaction center of the enzyme is within the porphyrin, where the <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene>. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand</scene> is the region attached to the the porphyrin.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327285Sandbox Reserved 3822011-11-30T20:27:13Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The reaction center of the enzyme is where the <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is located within the porphyrin. The porphyrin is attached to the <scene name='Sandbox_Reserved_382/Ligand/1'>ligand</scene>.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327284Sandbox Reserved 3822011-11-30T20:25:50Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The reaction center of the enzyme is where the <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is located within the porphyrin. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand</scene> is attached to the porphyrin.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327283Sandbox Reserved 3822011-11-30T20:24:31Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The reaction center of the enzyme is where the <scene name='Sandbox_Reserved_382/Heme_iron/2'>heme iron</scene> is located within the porphorin. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand</scene> is attached to the porphorin.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327281Sandbox Reserved 3822011-11-30T20:11:30Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The reaction center of the enzyme is where the <scene name='Sandbox_Reserved_382/Heme_iron/1'>heme iron</scene> is located within the porphorin. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand</scene> is attached to the porphorin/heme group.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327280Sandbox Reserved 3822011-11-30T20:05:25Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The reaction center of the enzyme is where the <scene name='Sandbox_Reserved_382/Heme_iron/1'>heme iron</scene> is located within the porphorin.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1327279Sandbox Reserved 3822011-11-30T20:04:12Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket and the reaction center of the enzyme is where the <scene name='Sandbox_Reserved_382/Heme_iron/1'>heme iron</scene> is located.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1326273Sandbox Reserved 3822011-11-30T06:15:08Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket and the reaction center of the enzyme is where the heme iron is located.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1326236Sandbox Reserved 3822011-11-30T06:14:24Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>[5]</ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket and the reaction center of the enzyme is where the heme iron is located.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1326179Sandbox Reserved 3822011-11-30T06:13:14Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket and the reaction center of the enzyme is where the heme iron is located.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1326145Sandbox Reserved 3822011-11-30T06:12:31Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands . An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket and the reaction center of the enzyme is where the heme iron is located.<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1326066Sandbox Reserved 3822011-11-30T06:05:54Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|Ribbon diagram displaying the overall structure of human placental aromatase| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1326064Sandbox Reserved 3822011-11-30T06:04:50Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|thumb|260px|left|'The ribbon diagram displaying the overall structure of human placental aromatase'| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1326061Sandbox Reserved 3822011-11-30T06:02:41Z<p>Whitney Smith: /* Function */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|260px|left|'The ribbon diagram displaying the overall structure of human placental aromatase'| <ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325988Sandbox Reserved 3822011-11-30T06:00:06Z<p>Whitney Smith: /* Function */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|260px|left|'The ribbon diagram displaying the overall structure of human placental aromatase'|]]<br />
<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325978Sandbox Reserved 3822011-11-30T05:59:38Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|260px|left|The ribbon diagram displaying the overall structure of human placental aromatase|]]<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325938Sandbox Reserved 3822011-11-30T05:57:49Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|260px|left|]]<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325921Sandbox Reserved 3822011-11-30T05:57:18Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
[[Image:Aromatase_Structure.jpg|300px|left|]]<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325867Sandbox Reserved 3822011-11-30T05:56:29Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
[[Image:Aromatase_Structure.jpg|200px|left|]]<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325784Sandbox Reserved 3822011-11-30T05:55:14Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
[[Image:Aromatase_Structure.jpg]]<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325625Sandbox Reserved 3822011-11-30T05:51:42Z<p>Whitney Smith: /* Structure */</p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
[[Image:Aromatase_Structure.jpg|350px|left|<ref> Ghosh, D. "X-ray Structure". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325612Sandbox Reserved 3822011-11-30T05:51:09Z<p>Whitney Smith: </p>
<hr />
<div><!-- PLEASE DO NOT DELETE THIS TEMPLATE --><br />
{{Sandbox_Reserved_JMeans}}<br />
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
[[Image:Aromatase_Structure.jpg|thumb|350px|right|<ref> Ghosh, D. "X-ray Structure". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smithhttps://proteopedia.org/index.php?title=Sandbox_Reserved_382&diff=1325589Sandbox Reserved 3822011-11-30T05:48:32Z<p>Whitney Smith: /* Structure */</p>
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= Aromatase =<br />
<Structure load='3EQM' size='400' frame='true' align='right' caption='Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione (PDB entry [http://www.pdb.org/pdb/explore/explore.do?structureId=3EQM])' scene='Insert optional scene name here' /><br />
== Introduction ==<br />
Aromatase belongs to the cytochrome p450 family. During aromatization reactions, Aromatase forms an electron-transfer complex with its partner, NADPH-cytochrome p450 reductase. This enzyme is localized in the endoplasmic reticulum of the cell and tissue specific promoters regulate its activity. In a number of species, including humans, aromatase can be found throughout the body in places such as the brain, gonads, blood vessels, endometrium, skin, bone and tissues including the placenta and adipose tissue. <ref> PMID: 11427156 </ref> There are many environmental factors that affect the activity of the aromatase enzyme and disrupt its function. Factors that increase the activity of the enzyme include age, obesity, gonadotropins, insulin, anti-m llerian hormone, alcohol and smoking. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref><br />
== Function ==<br />
The primary function of Aromatase is to produce estrogens by aromatizing androgens. Aromatase converts androstenedione to estrogen and testosterone to estradiol. <ref> "Aromatase Products" [http://www.novusbio.com/aromatase#13225047480835&ga_enabled%3B0] </ref> Aromatase is also a key enzyme in the biosynthesis of estrogens through a process called steroidogenesis. This enzyme helps produce this female sex hormone, estrogen, that helps to fuel the growth of hormone receptor-positive breast cancer.<br />
== Structure==<br />
Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. <br />
[[Image:Aromatase Structure.jpg|thumb|350px|right|<ref> Ghosh, D. "X-ray Structure". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>]<br />
<br />
== Aromatase Inhibitors ==<br />
Inhibitors of Aromatase stop the estrogen production in post-menopausal women. This action is done by blocking the Aromatase enzyme by turning the hormone, androgen, into small amounts of estrogen. <ref> "Aromatase Inhibitors" [http://www.breastcancer.org/treatment/hormonal/aromatase_inhibitors/] </ref><br />
There are three Aromatase Inhibitors that are often used in the treatment of breast cancer:<br />
*Arimidex (Anastrozole)<br />
*Aromasin (Exemestane)<br />
*Femara (Letrozole)<br />
Aromatase Inhibitors are unable to stop ovaries from producing estrogen, therefore, these inhibitors only work in post-menopausal women. <br />
== Disorders ==<br />
*'''Aromatase Enzyme Deficiency'''<br />
Aromatase Dificiency is rare in humans, however, if aromatase is nonfunctional due to a mutation estrogen synthesis cannot occur. Affected females are diagnoses at birth because of the obvious characteristics of pseudohermaphroditism. During the childhood of these girls, delayed bone maturation can occur along with cystic ovaries. However, affected males are diagnosed later in life because there are not obvious birth defects. Clincal symptoms such as a tall physique, delayed bone maturation and epiphyseal closure, bone pain, and excess adiposy. <ref> PMID: 17452968 </ref><br />
*'''Aromatase Excess Syndrome'''<br />
Research shows a rare disorder caused by excessive aromatase activity that can cause familial gynecomastia and feminization of both sexes. This can be inherited by an autosomal dominant manner, affected females and males differently. Females with this disorder showed signs of isosexual precocity and/or macromastia. Males showed characteristics of heterosexual precocity and/or gynecomastia. <ref> PMID: 9543166 </ref><br />
<br />
== References ==<br />
<references/></div>Whitney Smith