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Article

Yeast allosteric chorismate mutase is locked in the activated state by a single amino acid substitution.

Biochemistry - 17 Apr 1990

Schmidheini T, Mösch H U, Evans J N, Braus G

Abstract excerpt

Chorismate mutase, a branch-point enzyme in the aromatic amino acid pathway of Saccharomyces cerevisiae, and also a mutant chorismate mutase with a single amino acid substitution in the C-terminal part of the protein have been purified approximately 20-fold and 64-fold from overproducing strains, respectively. The wild-type enzyme is activated by tryptophan and subject to feedback inhibition by tyrosine, whereas...

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PMID: 2187528
DOI: 10.1021/bi00467a011

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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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