https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Douglas+Read 2026-09-14T18:33:13Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox341&diff=1225392 2011-04-05T04:21:55Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE='Sandbox341/Active_site_one/3'}}<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225391 2011-04-05T04:20:59Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE='Sandbox341/Active_site_one/3'}}<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225390 2011-04-05T04:18:31Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE='Sandbox341/Active_site_one/3'}}<br /> <br /> <br /> &lt;scene name='Sandbox341/Active_site_one/3'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' scene name='Sandbox341/Active_site_one/3'/&gt;<br /> <br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225389 2011-04-05T04:16:23Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=active site one}}<br /> <br /> &lt;scene name='Sandbox341/Active_site_one/3'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' scene name='Sandbox341/Active_site_one/3'&gt;TextToBeDisplayed&lt;/scene&gt; /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225388 2011-04-05T04:10:35Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=active site one}}<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225387 2011-04-05T04:08:16Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=active site one}}<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Active Site One/1}}<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225386 2011-04-05T04:05:24Z

<p>Douglas Read: </p> <hr /> <div>&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Isopentenyl Diphosphate Isomerase' scene='Active Site One' /&gt;<br /> <br /> <br /> <br /> {{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Active Site One/1}}<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225385 2011-04-05T04:03:18Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Active Site One/1}}<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225384 2011-04-05T04:02:00Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Active Site One/1}}<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Active Site One' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225383 2011-04-05T04:00:09Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_1vhh | PDB=1vhh | SCENE=Sandbox_191/Scenedefault/4}}<br /> <br /> <br /> <br /> {{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Active Site One/1}}<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Active Site One' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225382 2011-04-05T03:57:04Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_1vhh | PDB=1vhh | SCENE=Sandbox_191/Scenedefault/4}}<br /> <br /> <br /> <br /> {{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341}}<br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=File:My_protein.png&diff=1225381 2011-04-05T03:41:22Z

<p>Douglas Read: </p> <hr /> <div>Isopentyl Diphosphate Isomerase</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225380 2011-04-05T03:40:18Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341}}<br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> <br /> <br /> <br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png |thumb]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225379 2011-04-05T03:39:00Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341}}<br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225378 2011-04-05T03:36:06Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Mynewscene/1 }}<br /> <br /> [[Image: MY_PROTEIN.png|thumb|Isopentyl Diphosphate Isomerase ]]<br /> <br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image: My_protein.png ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225377 2011-04-05T03:35:21Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Mynewscene/1 }}<br /> <br /> [[Image: MY_PROTEIN.png|thumb|Isopentyl Diphosphate Isomerase ]]<br /> <br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225374 2011-04-05T03:34:02Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Mynewscene/1 }}<br /> <br /> [[Image: MY PROTEIN.png|thumb|Isopentyl Diphosphate Isomerase ]]<br /> <br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png<br /> ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225369 2011-04-05T03:31:55Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Mynewscene/1 }}<br /> <br /> [[Image:MY PROTEIN.png|thumb|Isopentyl Diphosphate Isomerase ]]<br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png<br /> ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225368 2011-04-05T03:21:12Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq | PDB=3hyq | SCENE=Sandbox_341/Mynewscene/1 }}<br /> <br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png<br /> ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225367 2011-04-05T03:18:03Z

<p>Douglas Read: </p> <hr /> <div>{{STRUCTURE_3hyq| PDB=3hyq | SCENE=Sandbox_341/Mynewscene/1 }}<br /> <br /> <br /> <br /> ----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png<br /> ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225360 2011-04-04T23:00:50Z

<p>Douglas Read: </p> <hr /> <div>----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png<br /> ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> '''REFRENCES'''<br /> <br /> 1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602.<br /> <br /> 2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.<br /> <br /> 3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696.<br /> <br /> 4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093.<br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225348 2011-04-04T21:12:15Z

<p>Douglas Read: </p> <hr /> <div>----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png<br /> ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2). <br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1225347 2011-04-04T20:41:51Z

<p>Douglas Read: </p> <hr /> <div>----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> This is a image of 3hq[[Image:Image:My_protein.png<br /> ]]<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).<br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> As stated above the enzyme requires metal co-factors in the active site; which consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=File:My_protein.png&diff=1224609 2011-04-04T01:02:45Z

<p>Douglas Read: </p> <hr /> <div></div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224287 2011-04-03T06:36:27Z

<p>Douglas Read: </p> <hr /> <div>----&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).<br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> As stated above the enzyme requires metal co-factors in the active site; which consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224280 2011-04-03T05:45:57Z

<p>Douglas Read: </p> <hr /> <div>----<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).<br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> As stated above the enzyme requires metal co-factors in the active site; which consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)<br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224279 2011-04-03T05:40:15Z

<p>Douglas Read: </p> <hr /> <div>----<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).<br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> As stated above the enzyme requires metal co-factors in the active site; which consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).<br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224246 2011-04-03T04:00:56Z

<p>Douglas Read: </p> <hr /> <div>----<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).<br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224240 2011-04-03T03:49:39Z

<p>Douglas Read: </p> <hr /> <div>----<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).<br /> <br /> '''STRUCTURE'''<br /> <br /> ----<br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224229 2011-04-03T03:35:42Z

<p>Douglas Read: </p> <hr /> <div>----<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).<br /> <br /> '''MECHANISM'''<br /> <br /> ----<br /> The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).<br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224221 2011-04-03T03:06:35Z

<p>Douglas Read: </p> <hr /> <div>----<br /> '''INTRODUCTION'''<br /> <br /> ----<br /> <br /> Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).<br /> <br /> <br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224171 2011-04-03T01:23:39Z

<p>Douglas Read: I</p> <hr /> <div>'''INTRODUCTION'''<br /> <br /> <br /> <br /> <br /> &lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224074 2011-04-02T22:09:54Z

<p>Douglas Read: </p> <hr /> <div>&lt;Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Sandbox341&diff=1224060 2011-04-02T21:49:57Z

<p>Douglas Read: New page: &lt;Structure load=&#039;3hyq&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Insert caption here&#039; scene=&#039;Insert optional scene name here&#039; /&gt;==This is a placeholder== This is a placeholder text to...</p> <hr /> <div>&lt;Structure load='3hyq' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=3cin | SCENE= }}</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064848 2010-04-01T04:49:45Z

<p>Douglas Read: </p> <hr /> <div>&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_2r3d| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> <br /> &lt;scene name='Sandbox_180/Act1/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis<br /> <br /> REFRENCES<br /> ----<br /> ----<br /> <br /> 1. Lord, Michael J., Roberts, Lynne M., Robertus, Jon D. Ricin: structure, mode of action, and some current applications. The FSEB journal. Vol 8. 1994.<br /> 2. Ernst, Stephen R., Hamlin, Ron., Katsen, Betsy., Montfort, William., Monzingo, Arthur F., Robertus, Jon D., Rutenbur, Earl., Villafranca, Jesus E., Xuong, Nuyhen H. The Three Dimensional Structure of Ricin at 2.8 Angstrom. The Journal of Biological Chemistry. Vol 262, No 11, pp. 5398-5403.1987.<br /> 3. Falnes, Pal., Olsnes, Sjur., Rapak, Andrzej. Retrograde Transport of Mutant Ricin to the Endoplasmic Recticulum with subsequent translocation to Cytosol. Cell Biology, Vol 94, pp. 3783-3788. 1997.</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064845 2010-04-01T04:47:29Z

<p>Douglas Read: </p> <hr /> <div>&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_2r3d| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> <br /> &lt;scene name='Sandbox_180/Act1/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis<br /> <br /> REFRENCES<br /> <br /> 1. Lord, Michael J., Roberts, Lynne M., Robertus, Jon D. Ricin: structure, mode of action, and some current applications. The FSEB journal. Vol 8. 1994.<br /> 2. Ernst, Stephen R., Hamlin, Ron., Katsen, Betsy., Montfort, William., Monzingo, Arthur F., Robertus, Jon D., Rutenbur, Earl., Villafranca, Jesus E., Xuong, Nuyhen H. The Three Dimensional Structure of Ricin at 2.8 Angstrom. The Journal of Biological Chemistry. Vol 262, No 11, pp. 5398-5403.1987.<br /> 3. Falnes, Pal., Olsnes, Sjur., Rapak, Andrzej. Retrograde Transport of Mutant Ricin to the Endoplasmic Recticulum with subsequent translocation to Cytosol. Cell Biology, Vol 94, pp. 3783-3788. 1997.</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064841 2010-04-01T04:45:03Z

<p>Douglas Read: </p> <hr /> <div><br /> &lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_2r3d| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> <br /> &lt;scene name='Sandbox_180/Act1/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064830 2010-04-01T04:39:29Z

<p>Douglas Read: </p> <hr /> <div><br /> {{STRUCTURE_2r3d| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> &lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_2r3d| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> <br /> &lt;scene name='Sandbox_180/Act1/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064814 2010-04-01T04:30:23Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_2r3d| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> <br /> &lt;scene name='Sandbox_180/Act1/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064736 2010-04-01T03:15:20Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_2r3d| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064725 2010-04-01T03:08:54Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> {{STRUCTURE_1cza| PDB=2r3d | SCENE=Sandbox_180/Mynewscene/1 }}<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064550 2010-03-31T21:42:53Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> ----<br /> ----<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> ----<br /> ----<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> ----<br /> ----<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064544 2010-03-31T21:27:54Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> INTRODUCTION<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> <br /> STRUCTURE<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> <br /> PHYSIOLOGY<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064542 2010-03-31T21:23:08Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> INTRODUCTION<br /> <br /> Ricin is a potent cytotoxin that is synthesized in the edosperm cells<br /> of maturing Riccinus seeds(1). Ricin belongs to a small multi-gene family<br /> (2) that is composed of eight members. It is also important to mention<br /> that Ricin is classified as a Type II heterodimeric Ribosome Inactivating<br /> protein(1).<br /> <br /> <br /> STRUCTURE<br /> <br /> Ricin is a heterodimer that consists of a 32,000 dalton A chain <br /> glycoprotein linked by a disulfide bond to a 32,000 dalton B chain<br /> glycoprotein(2). The A chain enzyme is a globular protein with extensive<br /> secondary structure and a predominate active site(2), where the B chain<br /> is a lectin(2) that binds to galactose-containing surface receptors(3).<br /> <br /> <br /> FUNCTION<br /> <br /> The mechanism employed by Ricin to gain entry to a host cell involves <br /> the heterodimeric properties of the toxin. Firstly the toxin arranges<br /> itself in such a way where its B chain can easily interact with the host<br /> cells receptors and once this happens the B chain can fascilitate the <br /> transfer of the A chain into the Cytoplasm(2). This association between <br /> A and B chain is essential for toxicity(2) without it the Ricin would not be<br /> able to gain access to the cells organelles. Once the A chain gains entry into<br /> the cytosol its target of attack is the ribosome, and its mechanism involves<br /> depurination of a single endenosine residue in 28S ribosome RNA(3); which <br /> inhibits ribosome function, thus stopping protein synthesis.</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064527 2010-03-31T20:59:30Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1064521 2010-03-31T20:38:54Z

<p>Douglas Read: </p> <hr /> <div>&lt;applet load='2r3d' size='300' frame='true' align='right' caption='Insert caption here' /&gt;&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> INTRODUCTION<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> STRUCTURE<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> PHYSIOLOGY<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis.<br /> <br /> <br /> 1. Lord, Michael J., Roberts, Lynne M., Robertus, Jon D. Ricin: structure, mode of action, and some current applications. The FSEB journal. Vol 8. 1994.<br /> 2. Ernst, Stephen R., Hamlin, Ron., Katsen, Betsy., Montfort, William., Monzingo, Arthur F., Robertus, Jon D., Rutenbur, Earl., Villafranca, Jesus E., Xuong, Nuyhen H. The Three Dimensional Structure of Ricin at 2.8 Angstrom. The Journal of Biological Chemistry. Vol 262, No 11, pp. 5398-5403.1987.<br /> 3. Falnes, Pal., Olsnes, Sjur., Rapak, Andrzej. Retrograde Transport of Mutant Ricin to the Endoplasmic Recticulum with subsequent sol. Cell Biology, Vol 94, pp. 3783-3788. 1997.</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1062624 2010-03-31T03:13:57Z

<p>Douglas Read: </p> <hr /> <div>&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/t<br /> <br /> RICIN<br /> <br /> <br /> INTRODUCTION<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> STRUCTURE<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> PHYSIOLOGY<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis.<br /> <br /> <br /> 1. Lord, Michael J., Roberts, Lynne M., Robertus, Jon D. Ricin: structure, mode of action, and some current applications. The FSEB journal. Vol 8. 1994.<br /> 2. Ernst, Stephen R., Hamlin, Ron., Katsen, Betsy., Montfort, William., Monzingo, Arthur F., Robertus, Jon D., Rutenbur, Earl., Villafranca, Jesus E., Xuong, Nuyhen H. The Three Dimensional Structure of Ricin at 2.8 Angstrom. The Journal of Biological Chemistry. Vol 262, No 11, pp. 5398-5403.1987.<br /> 3. Falnes, Pal., Olsnes, Sjur., Rapak, Andrzej. Retrograde Transport of Mutant Ricin to the Endoplasmic Recticulum with subsequent sol. Cell Biology, Vol 94, pp. 3783-3788. 1997.</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1062619 2010-03-31T03:09:14Z

<p>Douglas Read: </p> <hr /> <div>&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/tr&gt;<br /> Douglas Reed<br /> <br /> <br /> INTRODUCTION<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> STRUCTURE<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> PHYSIOLOGY<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis.<br /> <br /> <br /> 1. Lord, Michael J., Roberts, Lynne M., Robertus, Jon D. Ricin: structure, mode of action, and some current applications. The FSEB journal. Vol 8. 1994.<br /> 2. Ernst, Stephen R., Hamlin, Ron., Katsen, Betsy., Montfort, William., Monzingo, Arthur F., Robertus, Jon D., Rutenbur, Earl., Villafranca, Jesus E., Xuong, Nuyhen H. The Three Dimensional Structure of Ricin at 2.8 Angstrom. The Journal of Biological Chemistry. Vol 262, No 11, pp. 5398-5403.1987.<br /> 3. Falnes, Pal., Olsnes, Sjur., Rapak, Andrzej. Retrograde Transport of Mutant Ricin to the Endoplasmic Recticulum with subsequent sol. Cell Biology, Vol 94, pp. 3783-3788. 1997.</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1062615 2010-03-31T03:06:34Z

<p>Douglas Read: </p> <hr /> <div>&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/tr&gt;<br /> Douglas Reed<br /> <br /> <br /> INTRODUCTION<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> STRUCTURE<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> PHYSIOLOGY<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis.</div>

Douglas Read https://proteopedia.org/index.php?title=Ricin&diff=1062614 2010-03-31T03:05:56Z

<p>Douglas Read: </p> <hr /> <div>&lt;table style=&quot;background-color:#ffffc0&quot; cellpadding=&quot;8&quot; width=&quot;95%&quot; border=&quot;0&quot;&gt;&lt;tr&gt;&lt;td&gt;Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].&lt;/td&gt;&lt;/tr&gt;<br /> Douglas Reed<br /> INTRODUCTION<br /> <br /> Ricin is a potent cytotoxi that is synthesized in the endosperm cells of maturing Riccinus seeds(1). Ricin belongs to a small multi gene family(2) that is composed of eight members. It is also important to mention that Ricin is classified as a type II heterodimeric Ribosome Inactivatiing protein(1). <br /> <br /> STRUCTURE<br /> <br /> Ricin is a heterodimer that consists of a 32,000 Dalton A chain glycoprotein linked by a disulfide bond to a 32,000 Dalton B chain glycoprotein(2). The A chain enzyme is a globular protein with extensive secondary structure and a predominate active site(2); where the B chain is a lectin(2) that binds to galactose-containing surface receptors(3). <br /> <br /> PHYSIOLOGY<br /> <br /> The mechanism deployed by Ricin to gain entry to a host cell uses the heterogenic properties given to the toxin. Firstly the toxin arranges itself in such a way where its B chain can easily interact with the host cells receptors, and once acknowledgement happens, the B chain can fascilitate transport of the A chain into the cytoplasm(2). This association between the A and B chain is essential for toxicity(2) without it the Ricin would not be able to gain access to the cells organelles rendering it useless. Once the A chain gains entry into the cytosol its mechanism for attack of the ribosome is depurination of a single endenosine residue in 28S Ribosomal RNA(3) and this inhibits protein synthesis.</div>

Douglas Read