Yeast pyruvate kinase: essential lysine residues in the active site

Mónica Imarai, Patricio Hinrichsen, Sergio Bazaes, Marcela Wilkens, Jaime Eyzaguirre

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

1. 1. Yeast pyruvate kinase was purified to near homogeneity and subjected to chemical modification by trinitrobenzenesulfbnate and by P1, P2-bis (5′ pyridoxal) diphosphate. 2. 2. Labeled peptides were isolated and their amino acid composition was determined. 3. 3. The results suggest that yeast pyruvate kinase has an essential lysine residue, and that this residue is in a location equivalent to an essential lysine described in the muscle enzyme. 4. 4. Protection experiments indicate that this lysine is located at the nucleotide binding site.

Original languageEnglish
Pages (from-to)1001-1008
Number of pages8
JournalInternational Journal of Biochemistry
Volume20
Issue number9
DOIs
Publication statusPublished - 1 Jan 1988

ASJC Scopus subject areas

  • Biochemistry

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