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-Reference-Cited by-同舟云学术

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

Published:2003-04 Issue:14 Volume:278 Page:11903-11908
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

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

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference22 articles.

1. [11] Chemical syntheses of substrates of sterol biosynthesis

2. Isoprenoid biosynthesis in higher plants and in Escherichia coli: on the branching in the methylerythritol phosphate pathway and the independent biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate

3. Escherichia coli Open Reading Frame 696 Is idi , a Nonessential Gene Encoding Isopentenyl Diphosphate Isomerase

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