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Article

The carboligation reaction of acetohydroxyacid synthase II: steady-state intermediate distributions in wild type and mutants by NMR.

Proceedings of the National Academy of Sciences of the United States of America - 18 Jan 2005

Tittmann Kai, Vyazmensky Maria, Hübner Gerhard, Barak Ze'ev, Chipman David M

Abstract excerpt

The thiamin diphosphate (ThDP)-dependent enzyme acetohydroxyacid synthase (AHAS) catalyzes the first common step in branched-chain amino acid biosynthesis. By specific ligation of pyruvate with the alternative acceptor substrates 2-ketobutyrate and pyruvate, AHAS controls the flux through this branch point and determines the relative rates of synthesis of isoleucine, valine, and leucine, respectively. We used...

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Identifiers

PMID: 15640355
DOI: 10.1073/pnas.0408210101
PMCID: PMC545553

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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.

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