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2011-04-03T20:01:26Z

Craig Murray:

=Chorismate synthase=
{{STRUCTURE_1ztb | PDB=1ztb | SCENE=Index.php/Sandbox_Reserved_337/Aroc/1 }}
__TOC__
Chorismate Synthase is the last enzyme present in the shikimate pathway<ref name= "planta"> PMID:9951731</ref>, a process which converts phosphoenolpyruvate, and erythrose 4-phosphate to chorismate in a series of seven steps.<ref name= "review"> PMID:15012217</ref> The shikimate pathway is essential in the production of the amino acids phenylalanine, tryptophan and tyrosine, all essential amino acids.<ref name= "main"> PMID:16459102</ref>

=Structure=
This protein is in a unique form containing four subunits, and forming a homotetramer.<ref name= "pizza"> PMID:15095868</ref> The protein also contains a unique <scene name='Index.php/Sandbox_Reserved_337/Aroc2/1'>β-α-β sandwich fold</scene>.<ref name = "pizza"/>
<structure load= 1um0 size=250 frame =’1’ align=’left’ caption= 'Fig. 1. Chorismate synthase complexed with FMN, from PDB 1um0' scene= />
The protein also has a cofactor bound within each monomer of the protein. This cofactor is FMN which is located within the <scene name='Index.php/Sandbox_Reserved_337/Fmn_cofactor1/1'>active site</scene> of the protein.<ref name = "pizza"/> Each of these cofactors are bound non-covalently within the protein in the reduced form.<ref name = "pizza"/>

==Function==
The purpose of chorismate synthase is to convert 5-enolpyruvylshikimate 3-phosphate to chorismate, an essential step in the formation of indole rings used in the essential amino acids phenylalanine, tyrosine, and tryptophan.<ref name = "planta" /> The reduced flavin is believed to have one of a couple functions. It either has a structural role helping with formation of the structure, or reduces a sulfhydryl group in the protein residue, either aiding with binding or with having a catalytic effect.<ref name ="planta" /> The enzyme is monofunctional, requiring another enzyme to reduce the flavin cofactor, or addition of extra reduced flavin to add to the enzyme.<ref name = "review" />
=Mechanism=
In this reaction the 5-enolpyruvylshikimate 3-phosphate, is reduced forming a second double bond in the benzene ring attached to the phosphate.<ref name = "review" /> It appears that the phosphate group is reduced allowing the benzene ring to have a free electron pair to form a double bond with.<ref name = "review" /> As well the double bond which originally existed, experiences a hydrogen shift and the second double bond occurs to form resonance.<ref name = "review" />
=References=
<references />

Index.php/Sandbox Reserved 337

2011-04-03T19:41:36Z

Craig Murray:

=Chorismate synthase=
{{STRUCTURE_1ztb | PDB=1ztb | SCENE=Index.php/Sandbox_Reserved_337/Aroc/1 }}
__TOC__
Chorismate Synthase is the last enzyme present in the shikimate pathway<ref name= "planta"> PMID:9951731</ref>, a process which converts phosphoenolpyruvate, and erythrose 4-phosphate to chorismate in a series of seven steps.<ref name= "review"> PMID:15012217</ref> The shikimate pathway is essential in the production of the amino acids phenylalanine, tryptophan and tyrosine, all essential amino acids.<ref name= "main"> PMID:16459102</ref>

=Structure=
This protein is in a unique form containing four subunits, and forming a homotetramer.<ref name= "pizza"> PMID:15095868</ref> The protein also contains a unique <scene name='Index.php/Sandbox_Reserved_337/Aroc2/1'>β-α-β sandwich fold</scene>.<ref name = "pizza"/>
<structure load= 1um0 size=250 frame =’1’ align=’left’ caption= 'Fig. 1. Chorismate synthase complexed with FMN, from PDB 1um0' scene= />
The protein also has a cofactor bound within each monomer of the protein. This cofactor is FMN which is located within the active site of the protein.<ref name = "pizza"/> Each of these cofactors are bound non-covalently within the protein in the reduced form.<ref name = "pizza"/>

==Function==
The purpose of chorismate synthase is to convert 5-enolpyruvylshikimate 3-phosphate to chorismate, an essential step in the formation of indole rings used in the essential amino acids phenylalanine, tyrosine, and tryptophan.<ref name = "planta" /> The reduced flavin is believed to have one of a couple functions. It either has a structural role helping with formation of the structure, or reduces a sulfhydryl group in the protein residue, either aiding with binding or with having a catalytic effect.<ref name ="planta" /> The enzyme is monofunctional, requiring another enzyme to reduce the flavin cofactor, or addition of extra reduced flavin to add to the enzyme.<ref name = "review" />
=Mechanism=
In this reaction the 5-enolpyruvylshikimate 3-phosphate, is reduced forming a second double bond in the benzene ring attached to the phosphate.<ref name = "review" /> It appears that the phosphate group is reduced allowing the benzene ring to have a free electron pair to form a double bond with.<ref name = "review" /> As well the double bond which originally existed, experiences a hydrogen shift and the second double bond occurs to form resonance.<ref name = "review" />
=References=
<references />

Index.php/Sandbox Reserved 337

2011-04-03T05:32:14Z

Craig Murray:

=Chorismate synthase=
{{STRUCTURE_1ztb | PDB=1ztb | SCENE=Index.php/Sandbox_Reserved_337/Aroc/1 }}
__TOC__
Chorismate Synthase is the last enzyme present in the shikimate pathway<ref name= "planta"> PMID:9951731</ref>, a process which converts phosphoenolpyruvate, and erythrose 4-phosphate to chorismate in a series of seven steps.<ref name= "review"> PMID:15012217</ref> The shikimate pathway is essential in the production of the amino acids phenylalanine, tryptophan and tyrosine, all essential amino acids.<ref name= "main"> PMID:16459102</ref>

=Structure=
This protein is in a unique form containing four subunits, and forming a homotetramer.<ref name= "pizza"> PMID:15095868</ref> The protein also contains a unique β-α-β sandwich fold.<ref name = "pizza"/>
<structure load= 1um0 size=250 frame =’1’ align=’left’ caption= 'Fig. 1. Chorismate synthase complexed with FMN, from PDB 1um0' scene= />
The protein also has a cofactor bound within each monomer of the protein. This cofactor is FMN which is located within the active site of the protein.<ref name = "pizza"/> Each of these cofactors are bound non-covalently within the protein in the reduced form.<ref name = "pizza"/>

==Function==
The purpose of chorismate synthase is to convert 5-enolpyruvylshikimate 3-phosphate to chorismate, an essential step in the formation of indole rings used in the essential amino acids phenylalanine, tyrosine, and tryptophan.<ref name = "planta" /> The reduced flavin is believed to have one of a couple functions. It either has a structural role helping with formation of the structure, or reduces a sulfhydryl group in the protein residue, either aiding with binding or with having a catalytic effect.<ref name ="planta" /> The enzyme is monofunctional, requiring another enzyme to reduce the flavin cofactor, or addition of extra reduced flavin to add to the enzyme.<ref name = "review" />
=Mechanism=
In this reaction the 5-enolpyruvylshikimate 3-phosphate, is reduced forming a second double bond in the benzene ring attached to the phosphate.<ref name = "review" /> It appears that the phosphate group is reduced allowing the benzene ring to have a free electron pair to form a double bond with.<ref name = "review" /> As well the double bond which originally existed, experiences a hydrogen shift and the second double bond occurs to form resonance.<ref name = "review" />
=References=
<references />

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2011-04-03T05:15:25Z

Craig Murray:

Index.php/Sandbox Reserved 337

2011-03-17T20:29:20Z

Craig Murray:

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2011-03-15T19:21:27Z

Craig Murray:

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2011-03-14T20:59:53Z

Craig Murray:

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2011-03-07T16:32:46Z

Craig Murray:

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=Chorismate synthase=
{{STRUCTURE_1ztb | PDB=1ztb | SCENE=Index.php/Sandbox_Reserved_337/Aroc/1 }}
__TOC__
=Structure=
==Function==
=Pathway=
=References=

Index.php/Sandbox Reserved 337

2011-03-04T19:44:16Z

Craig Murray:

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2011-03-03T03:39:45Z

Craig Murray:

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2011-03-03T03:34:51Z

Craig Murray:

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2011-03-03T03:19:47Z

Craig Murray:

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2011-03-03T02:04:04Z

Craig Murray: New page: ==This is a placeholder== This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click "Show Preview" at the bottom of this page to see how...