PMID:14696183
| Citation |
Wouters, J, Oudjama, Y, Stalon, V, Droogmans, L and Poulter, CD (2004) Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor. Proteins 54:216-21 |
|---|---|
| Abstract |
Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate. Analysis of the 1.97 A crystal structure of the inactive C67A mutant of E. coli isopentenyl diphosphate:dimethylallyl diphosphate isomerase complexed with the mechanism-based inactivator 3,4-epoxy-3-methyl-1-butyl diphosphate is in agreement with an isomerization mechanism involving Glu 116, Tyr 104, and Cys 67. In particular, the results are consistent with a mechanism where Glu116 is involved in the protonation step and Cys67 in the elimination step. |
| Links |
PubMed Online version:10.1002/prot.10573 |
| Keywords |
Binding Sites; Carbon-Carbon Double Bond Isomerases/antagonists & inhibitors; Carbon-Carbon Double Bond Isomerases/chemistry; Carbon-Carbon Double Bond Isomerases/genetics; Carbon-Carbon Double Bond Isomerases/metabolism; Crystallography, X-Ray; Enzyme Inhibitors/chemistry; Enzyme Inhibitors/metabolism; Enzyme Inhibitors/pharmacology; Epoxy Compounds/chemistry; Epoxy Compounds/metabolism; Epoxy Compounds/pharmacology; Escherichia coli/enzymology; Escherichia coli/genetics; Isomerism; Organophosphorus Compounds/chemistry; Organophosphorus Compounds/metabolism; Organophosphorus Compounds/pharmacology; Point Mutation/genetics; Protons |
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