Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids

McCourt, J. A. and Duggleby, R. G. (2006) Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids. Amino Acids, 31 2: 173-210.


Author McCourt, J. A.
Duggleby, R. G.
Title Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids
Journal name Amino Acids   Check publisher's open access policy
ISSN 0939-4451
Publication date 2006
Sub-type Article (original research)
DOI 10.1007/s00726-005-0297-3
Volume 31
Issue 2
Start page 173
End page 210
Total pages 38
Place of publication New York
Publisher Springer
Collection year 2006
Language eng
Subject C1
270108 Enzymes
780105 Biological sciences
270102 Cell Metabolism
Abstract The branched-chain amino acids are synthesized by plants, fungi and microorganisms, but not by animals. Therefore, the enzymes of this pathway are potential target sites for the development of antifungal agents, antimicrobials and herbicides. Most research has focused upon the first enzyme in this biosynthetic pathway, acetohydroxyacid synthase (AHAS) largely because it is the target site for many commercial herbicides. In this review we provide a brief overview of the important properties of each enzyme within the pathway and a detailed summary of the most recent AHAS research, against the perspective of work that has been carried out over the past 50 years.
Keyword Acetohydroxyacid Synthase
Acetolactate Synthase
Branched-chain Amino Acids
Thiamin Diphosphate
Flavin Adenine Dinucleotide
Herbicide
Inhibitor
Mechanism
Protein Structure
Biochemistry & Molecular Biology
Tobacco Acetolactate Synthase
Site-directed Mutagenesis
Escherichia-coli K-12
Alpha-isopropylmalate Synthase
Altered Feedback Sensitivity
Thiamin Diphosphate Enzymes
Herbicide Binding-site
Barley Hordeum-vulgare
Arabidopsis-thaliana
Crystal-structure
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 08:23:32 EST