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. Wouters, Y. Oudjama, Sam J. Barkley, C. Tricot, V. Stalon, L. Droogmans, C. Dale Poulter

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Résumé

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 Å) 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.

langue originaleAnglais
Pages (de - à)11903-11908
Nombre de pages6
journalJournal of Biological Chemistry
Volume278
Numéro de publication14
Les DOIs
Etat de la publicationPublié - 4 avr. 2003

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