Enzymology, Structure, and Dynamics of Acetohydroxy Acid Isomeroreductase

• Published in: Accounts of chemical research Vol. 34; no. 5; pp. 399 - 408
• Main Authors: Dumas, Renaud, Biou, Valérie, Halgand, Frédéric, Douce, Roland, Duggleby, Ronald G
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 01-05-2001
• Subjects: Alcohol Oxidoreductases - antagonists & inhibitors; Alcohol Oxidoreductases - chemistry; Alcohol Oxidoreductases - metabolism; Amino Acid Sequence; Catalysis; Ketol-Acid Reductoisomerase; Molecular Sequence Data; Sequence Homology, Amino Acid; Structure-Activity Relationship; Subcellular Fractions - enzymology
• ISSN: 0001-4842; 1520-4898
• DOI: 10.1021/ar000082w

Acetohydroxy acid isomeroreductase is a key enzyme involved in the biosynthetic pathway of the amino acids isoleucine, valine, and leucine. This enzyme is of great interest in agrochemical research because it is present only in plants and microorganisms, making it a potential target for specific herbicides and fungicides. Moreover, it catalyzes an unusual two-step reaction that is of great fundamental interest. With a view to characterizing both the mechanism of inhibition by potential herbicides and the complex reaction mechanism, various techniques of enzymology, molecular biology, mass spectrometry, X-ray crystallography, and theoretical simulation have been used. The results and conclusions of these studies are described briefly in this paper.