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Article

Dissociation of the tetrameric phosphoglycerate mutase from yeast by a mutation in the subunit contact region.

The Biochemical journal - 1 Nov 1993

White M F, Fothergill-Gilmore L A, Kelly S M, Price N C

Abstract excerpt

Phosphoglycerate mutases from different sources exhibit a variety of quaternary structures (tetramer, dimer and monomer). To perturb the tetrameric structure of yeast phosphoglycerate mutase we have prepared a mutant enzyme in which Lys-168 in the subunit-contact region has been replaced by proline. The K168P mutant enzyme undergoes dissociation to dimers at low concentrations; thus on lowering the concentration...

Topics

Circular Dichroism
Enzyme Stability
Guanidine
Guanidines
Kinetics
Lysine
Macromolecular Substances
Mutagenesis, Site-Directed
Mutation
Phosphoglycerate Mutase
Proline

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Protein Denaturation

Protein Folding

Protein Structure, Secondary

Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 8240286
DOI: 10.1042/bj2950743
PMCID: PMC1134623

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8240286-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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