Characterization of the Conformational Changes of Acetohydroxy Acid Isomeroreductase Induced by the Binding of Mg2+ Ions, NADPH, and a Competitive Inhibitor
Author:
Affiliation:
1. Institut de Biologie Structurale, CEA/CNRS, 41 Avenue des Martyrs, 38027 Grenoble Cedex, France, and Unité Mixte CNRS/Rhône-Poulenc, 14-20 Rue Pierre Baizet, 69263 Lyon Cedex 09, France
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi982412e
Reference30 articles.
1. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65Aresolution
2. Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli
3. Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogues: correlation of the slow, competitive, inhibition kinetics of enzyme activity and herbicidal effects
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