PMID:12540835
| Citation |
Wouters, J, Oudjama, Y, Barkley, SJ, Tricot, C, Stalon, V, Droogmans, L and Poulter, CD (2003) Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors. J. Biol. Chem. 278:11903-8 |
|---|---|
| Abstract |
Isopentenyl diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The reaction involves protonation and deprotonation of the isoprenoid unit and proceeds through a carbocationic transition state. Analysis of the crystal structures (2 A) of complexes of Escherichia coli IPP.DMAPPs isomerase with a transition state analogue (N,N-dimethyl-2-amino-1-ethyl diphosphate) and a covalently attached irreversible inhibitor (3,4-epoxy-3-methyl-1-butyl diphosphate) indicates that Glu-116, Tyr-104, and Cys-67 are involved in the antarafacial addition/elimination of protons during isomerization. This work provides a new perspective about the mechanism of the reaction. |
| Links |
PubMed Online version:10.1074/jbc.M212823200 |
| Keywords |
Carbon-Carbon Double Bond Isomerases/antagonists & inhibitors; Carbon-Carbon Double Bond Isomerases/chemistry; Carbon-Carbon Double Bond Isomerases/metabolism; Catalytic Domain; Crystallography; Cysteine/chemistry; Epoxy Compounds/pharmacology; Escherichia coli/enzymology; Glutamic Acid/chemistry; Kinetics; Organophosphorus Compounds/pharmacology; Protein Structure, Secondary; Tyrosine/chemistry |
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