Yeast pyruvate kinase: essential lysine residues in the active site

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

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

6 Citas (Scopus)

Resumen

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.

Idioma originalInglés
Páginas (desde-hasta)1001-1008
Número de páginas8
PublicaciónInternational Journal of Biochemistry
Volumen20
N.º9
DOI
EstadoPublicada - 1 ene 1988

Áreas temáticas de ASJC Scopus

  • Bioquímica

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