Proteopedia - User contributions [en]

Enolase

2010-05-04T16:51:44Z

Cory Tiedeman: New page: 200px {{STRUCTURE_1one | PDB=1one | SCENE= }} <scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycoly...

[[Image:1one.png|left|200px]]
{{STRUCTURE_1one | PDB=1one | SCENE= }}

<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref> Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis: it is a reversible dehydration reaction.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>. Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>.

==Structure==
The <scene name='Cory_Tiedeman_Sandbox_1/Secondary_structure/1'>secondary structure</scene> of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain). Enolase consists of two domains.

'''Structural Clasification of Proteins (SCOP)<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>'''

Enolase is in the alpha and beta proteins class and has a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is in the enolase family.

==Mechanism==
[[Image:mechanism.png|left|400px|The mechanism of 2PG to PEP using enolase.]]<ref>{{website2}}</ref>
The
<scene name='Cory_Tiedeman_Sandbox_1/Active_site/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with two
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>Mg 2+'s</scene> at its active site.
The substrate, 2PG, binds to the two <scene name='Cory_Tiedeman_Sandbox_1/Mechanism/4'>Mg2+'s, Glu 211, and Lys 345</scene>. The Mg 2+ then forms a bond at the deprotonated carboxylic acid on the 1'C to connect it with enolase. It also is connects to Glu 211 and Lys 345. Glu 211 makes a hydrogen bond with the alcohol group on the 3'C. Lys 345 deprotonates the 2'C and then the 2'C forms an alkene with the 1'C which then moves the electrons forming the ketone onto the oxygen making it have a negative charge. The other oxygen, which already has a negative charge, then moves its electron to form a ketone with the 1'C. The electrons that made up the alkene between the 1'C adn 2'C then moves to form an alkene between the 2'C and 3'C. This breaks the bond with the alcohol on the 3'C which deprotonates Glu 211 on enolase to form H2O. Then the new molecule is released from enolase as PEP. PEP then goes on through another step in glycolysis to create pyruvate.

Fluoride ions inhibits glycolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>

==Kinetics==
[[Image:enolase kinetics.jpeg|left|150px|V vs. [PGA]; PGA is 2PG, the top curve has [Mg2+] of 10^-3 M and the bottom curve has [Mg2+] of 106-2 M]]<ref>{{journal2}}</ref>
Since Mg2+ is essential for binding the substrate, 2-PG, it is also needed at a specific quality in order to have a good rate, or velocity. The graph shows the V vs. [PGA], in which PGA is 2-PG, with two different concentrations of Mg2+. The upper curve, which also has greater Vmax, has an Mg2+ concentration of 10^-3 M while the lower curve, which has a lower Vmax, has an Mg2+ concentration of 10^-2 M<ref>{{journal2}}</ref>. The Km is also larger the upper curve making the higher [Mg2+] more desirable.

==Regulation==
Enolase is found on the surface of a variety of eukaryotic cells as a strong plamingoen-binding receptor and on the surface of hematopietic celss such as monocytes, T cells and B cells, neuronal celss and endothelial cells. Enolase in muscle can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that they make a functional glycolytic segment in the muscle where ATP production is required in order for the muscle to contract. Myc-binding protein (MBP-1) is similar to the a-enolse structure and is found in the nucleus as a DNA-binding protein<ref>{{journal}}</ref>.
Enolase is regulated by the concentration of Mg2+ and the previous steps of glycolysis.

==References==
<references/>

2010-03-23T21:11:47Z

Cory Tiedeman: Shows the V vs. [S] graph of enolase with two different concentrations of Mg2+. The substrate, PGA, is actually 2-PG. The upper curve has an Mg2+ concentration of 10^-3 M and the lower curve has an Mg2+ concentration of 10^-2 M.

Cory Tiedeman Sandbox 1

2010-03-23T21:07:36Z

Cory Tiedeman:

[[Image:1one.png|left|200px]]
{{STRUCTURE_1one | PDB=1one | SCENE= }}

<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref> Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref> Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>.

==Structure==
The <scene name='Cory_Tiedeman_Sandbox_1/Secondary_structure/1'>secondary structure</scene> of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain).

'''Structural Clasification of Proteins (SCOP)<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>'''

Enolase is in the alpha and beta proteins class and has a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is in the enolase family. This specific enolase is found in the species: Saccharomyces cerevisiae, which is baker's yeast.

==Mechanism==
[[Image:mechanism.png|left|400px]]<ref>{{website2}}</ref>
The
<scene name='Cory_Tiedeman_Sandbox_1/Active_site/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>Mg 2+</scene> at its active site. The Mg 2+ then forms a bond with 2PG at the deprotonated carboxylic acid on the 1'C to connect it with enolase. It also is connects to Glu 211 and Lys 345. Glu 211 makes a hydrogen bond with the alcohol group on the 3'C. Lys 345 deprotonates the 2'C and then the 2'C forms an alkene with the 1'C which then moves the electrons forming the ketone onto the oxygen making it have a negative charge. The other oxygen, which already has a negative charge, then moves its electron to form a ketone with the 1'C. The electrons that made up the alkene between the 1'C adn 2'C then moves to form an alkene between the 2'C and 3'C. This breaks the bond with the alcohol on the 3'C which deprotonates Glu 211 on enolase to form H2O. Then the new molecule is released from enolase as PEP. PEP then goes on through another step in glycolysis to create pyruvate.

Fluoride ions inhibits glycolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>

==Kinetics==
[[Image:enolase kinetics.jpeg|left|400px]]<ref>{{journal2}}</ref>

==Regulation==
Enolase is found on the surface of a variety of eukaryotic cells as a strong plamingoen-binding receptor and on the surface of hematopietic celss such as monocytes, T cells and B cells, neuronal celss and endothelial cells. Enolase in muscle can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that they make a functional glycolytic segment in the muscle where ATP production is required in order for the muscle to contract. Myc-binding protein (MBP-1) is similar to the a-enolse structure and is found in the nucleus as a DNA-binding protein<ref>{{journal}}</ref>.

==References==
<references/>

Cory Tiedeman Sandbox 1

2010-03-23T20:56:41Z

Cory Tiedeman:

[[Image:1one.png|left|200px]]
{{STRUCTURE_1one | PDB=1one | SCENE= }}

<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref> Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref> Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>.

==Structure==
The <scene name='Cory_Tiedeman_Sandbox_1/Secondary_structure/1'>secondary structure</scene> of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain).

'''Structural Clasification of Proteins (SCOP)<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>'''

Enolase is in the alpha and beta proteins class and has a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is in the enolase family. This specific enolase is found in the species: Saccharomyces cerevisiae, which is baker's yeast.

==Mechanism==
[[Image:mechanism.png|left|400px]]<ref>{{website2}}</ref>
The
<scene name='Cory_Tiedeman_Sandbox_1/Active_site/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>Mg 2+</scene> at its active site. The Mg 2+ then forms a bond with 2PG at the deprotonated carboxylic acid on the 1'C to connect it with enolase. It also is connects to Glu 211 and Lys 345. Glu 211 makes a hydrogen bond with the alcohol group on the 3'C. Lys 345 deprotonates the 2'C and then the 2'C forms an alkene with the 1'C which then moves the electrons forming the ketone onto the oxygen making it have a negative charge. The other oxygen, which already has a negative charge, then moves its electron to form a ketone with the 1'C. The electrons that made up the alkene between the 1'C adn 2'C then moves to form an alkene between the 2'C and 3'C. This breaks the bond with the alcohol on the 3'C which deprotonates Glu 211 on enolase to form H2O. Then the new molecule is released from enolase as PEP. PEP then goes on through another step in glycolysis to create pyruvate.

Fluoride ions inhibits glycolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>

==Kinetics==

==Regulation==
Enolase is found on the surface of a variety of eukaryotic cells as a strong plamingoen-binding receptor and on the surface of hematopietic celss such as monocytes, T cells and B cells, neuronal celss and endothelial cells. Enolase in muscle can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that they make a functional glycolytic segment in the muscle where ATP production is required in order for the muscle to contract. Myc-binding protein (MBP-1) is similar to the a-enolse structure and is found in the nucleus as a DNA-binding protein<ref>{{journal}}</ref>.

==References==
<references/>

Template:Journal

2010-03-23T20:53:55Z

Cory Tiedeman: New page: Pancholi, V. "Multifunctional a-Enolase: Its Role in Diseases." CMLS, Cellular and Molecular Life Sciences 58 (2001): 902-20.

Pancholi, V. "Multifunctional a-Enolase: Its Role in Diseases." CMLS, Cellular and Molecular Life Sciences 58 (2001): 902-20.

Cory Tiedeman Sandbox 1

2010-03-23T20:45:16Z

Cory Tiedeman:

[[Image:1one.png|left|200px]]
{{STRUCTURE_1one | PDB=1one | SCENE= }}

<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref> Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>

==Structure==
The <scene name='Cory_Tiedeman_Sandbox_1/Secondary_structure/1'>secondary structure</scene> of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain).

'''Structural Clasification of Proteins (SCOP)<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>'''

Enolase is in the alpha and beta proteins class and has a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is in the enolase family. This specific enolase is found in the species: Saccharomyces cerevisiae, which is baker's yeast.

==Mechanism==
[[Image:mechanism.png|left|400px]]<ref>{{website2}}</ref>
The
<scene name='Cory_Tiedeman_Sandbox_1/Active_site/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>Mg 2+</scene> at its active site. The Mg 2+ then forms a bond with 2PG at the deprotonated carboxylic acid on the 1'C to connect it with enolase. It also is connects to Glu 211 and Lys 345. Glu 211 makes a hydrogen bond with the alcohol group on the 3'C. Lys 345 deprotonates the 2'C and then the 2'C forms an alkene with the 1'C which then moves the electrons forming the ketone onto the oxygen making it have a negative charge. The other oxygen, which already has a negative charge, then moves its electron to form a ketone with the 1'C. The electrons that made up the alkene between the 1'C adn 2'C then moves to form an alkene between the 2'C and 3'C. This breaks the bond with the alcohol on the 3'C which deprotonates Glu 211 on enolase to form H2O. Then the new molecule is released from enolase as PEP. PEP then goes on through another step in glycolysis to create pyruvate.

Fluoride ions inhibits glycolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>

==Kinetics==

==Regulation==
Enolase is found on the surface of a variety of eukaryotic cells as a strong plamingoen-binding receptor and on the surface of hematopietic celss such as monocytes, T cells and B cells, neuronal celss and endothelial cells. Enolase in muscle can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that they make a functional glycolytic segment in the muscle where ATP production is required in order for the muscle to contract. Myc-binding protein (MBP-1) is similar to the a-enolse structure and is found in the nucleus as a DNA-binding protein<ref>{{journal}}</ref>.

==References==
<references/>

Cory Tiedeman Sandbox 1

2010-03-21T19:58:52Z

Cory Tiedeman:

Template:Website2

2010-03-20T19:09:18Z

2010-03-18T20:01:23Z

Cory Tiedeman:

Cory Tiedeman Sandbox 1

2010-03-18T19:40:19Z

Cory Tiedeman:

Cory Tiedeman Sandbox 1

2010-03-18T19:26:13Z

Cory Tiedeman:

2010-03-01T18:52:07Z

Cory Tiedeman:

[[Image:1one.png|left|200px]]
{{STRUCTURE_1one | PDB=1one | SCENE= }}

Enolase is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyrubate. The energy released during glycolysis is used to make ATP.<ref>{{text book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=486|}}</ref> Enolase is used to convert2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis.<ref>{{text book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>

==Structure==
The <scene name='Cory_Tiedeman_Sandbox_1/Secondary_structure/1'>secondary structure</scene> of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parellel<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>. As shown in the figure, enolase has about 36 alpha helixes and 22 beta sheets (18 alpha helices and 11 beta sheets per domain).

'''Structural Clasification of Proteins (SCOP)<ref>{{web site| title=SCOP: Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae)|url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html|}}</ref>'''

Class: alpha and beta proteins (a/b)

Fold: TIM beta/alpha-barrel

Superfamily: Enolase C-terminal domain-like

Family: Enolase

Species: Baker's yeast (Saccharomyces cerevisiae)

==Mechanism==
[[Image:mechanism.png|left|300px]]
The
<scene name='Cory_Tiedeman_Sandbox_1/Active_sice/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>Mg 2+</scene> at its active site. The Mg 2+ then forms a bond with 2PG to connect it with enolase. Fluoride ions inhibits glcolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.<ref>{{text book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>

==References==
{{Reflist}}