Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor.

Autor: J. Wouters, Y. Oudjama, V. Stalon, L. Droogmans, C.D. Poulter
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Zdroj: Proteins; Feb2004, Vol. 54 Issue 2, p216-221, 6p
Abstrakt: 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 Å 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. Proteins 2003;53:000–000. © 2003 Wiley-Liss, Inc. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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