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Article

Mutagenesis of the active site lysine 221 of the pyruvate kinase from Bacillus stearothermophilus.

Journal of biochemistry - 1 Feb 2005

Sakai Hiroshi

Abstract excerpt

Lysine 221 of the pyruvate kinase from Bacillus stearothermophilus was mutated to arginine, leucine, asparatic acid and cysteine. All the mutated enzymes were 10(4) to 10(5) times less active than the wild-type enzyme. The cysteine-free enzyme C9S/C268S, and the enzyme C9S/C268S/K221C, which possessed a unique sulfhydryl group at position 221, were prepared. The former had comparable activity to the wild-type...

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Identifiers

PMID: 15749828
DOI: 10.1093/jb/mvi027

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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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