Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.

doi:10.1006/jmbi.2001.5419

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Article

Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.

Journal of molecular biology - 22 Mar 2002

Pang Siew Siew, Duggleby Ronald G, Guddat Luke W

Abstract excerpt

Acetohydroxyacid synthase (AHAS; EC 4.1.3.18) catalyzes the first step in branched-chain amino acid biosynthesis. The enzyme requires thiamin diphosphate and FAD for activity, but the latter is unexpected, because the reaction involves no oxidation or reduction. Due to its presence in plants, AHAS is a target for sulfonylurea and imidazolinone herbicides. Here, the crystal structure to 2.6 A resolution of the...

Topics

Acetolactate Synthase
Amino Acid Sequence
Binding Sites
Catalytic Domain
Crystallography, X-Ray
Dimerization
Enzyme Inhibitors
Flavin-Adenine Dinucleotide
Herbicides
Imidazoles
Magnesium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Sequence Data

Mutation

Niacin

Protein Conformation

Sequence Homology, Amino Acid

Thiamine Pyrophosphate

Source

Open in PubMed

Identifiers

PMID: 11902841
DOI: 10.1006/jmbi.2001.5419

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-11902841-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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