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Article

Ligand-induced conformational changes in wild-type and mutant yeast pyruvate kinase.

Protein engineering - 1 Dec 1996

Collins R A, Kelly S M, Price N C, Fothergill-Gilmore L A, Muirhead H

Abstract excerpt

A mutant form of pyruvate kinase in which serine 384 has been mutated to proline has been engineered in the yeast Saccharomyces cerevisiae. Residue 384 is located in a helix in a subunit interface of the tetrameric enzyme, and the mutation was anticipated to alter the conformation of the helix and hence destabilize the interface. Previous results indicate that the mutant favours the T quaternary conformation over...

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Identifiers

PMID: 9010934
DOI: 10.1093/protein/9.12.1203

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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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