Sandbox341
From Proteopedia
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| + | 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). | ||
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<Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />==This is a placeholder== | <Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />==This is a placeholder== | ||
Revision as of 05:40, 3 April 2011
INTRODUCTION
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.
MECHANISM
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).
STRUCTURE
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).
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| 3cin, resolution 1.70Å () | |||||||||
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| Ligands: | , , | ||||||||
| Gene: | TM1419, TM_1419 (Thermotoga maritima MSB8) | ||||||||
| Activity: | Inositol-3-phosphate synthase, with EC number 5.5.1.4 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
