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 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.
Original language | English |
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Pages (from-to) | 11903-11908 |
Number of pages | 6 |
Journal | Journal of Biological Chemistry |
Volume | 278 |
Issue number | 14 |
DOIs | |
Publication status | Published - 4 Apr 2003 |
Keywords
- Biosynthesis
- Ctalysis
- Crystal structure
- Escherichia coli
- Isomerization