Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Binding Sites
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 11902841
DOI: 10.1006/jmbi.2001.5419

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.PMID 11902841Read ↗

Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase.Semantic proximity Read ↗

Systematic characterization of mutations in yeast acetohydroxyacid synthase. Interpretation of herbicide-resistance data.Semantic proximity Read ↗

Structural basis of resistance to herbicides that target acetohydroxyacid synthase.Semantic proximity Read ↗

Computational insights into herbicide resistance via acetohydroxyacid synthase in Ambrosia artemisiifolia.Semantic proximity Read ↗

An acetohydroxy acid synthase mutant reveals a single site involved in multiple herbicide resistance.Semantic proximity Read ↗

Structural and functional evaluation of three well-conserved serine residues in tobacco acetohydroxyacid synthase.Semantic proximity Read ↗

Computational design of novel inhibitors to overcome weed resistance associated with acetohydroxyacid synthase (AHAS) P197L mutant.Semantic proximity Read ↗

Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid synthase: characterization of the catalytic properties and sensitivity to inhibitors of four defined mutants.Semantic proximity Read ↗

Resistance to AHAS inhibitor herbicides: current understanding.Semantic proximity Read ↗

Interrogating the Inhibition Mechanisms of Human Aldehyde Oxidase by X-ray Crystallography and NMR Spectroscopy: The Raloxifene Case.Semantic proximity Read ↗

Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.Semantic proximity Read ↗

PPO Inhibitors as a Key Focus in Herbicide DiscoverySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.