YEAST PYRUVATE-KINASE - ESSENTIAL LYSINE RESIDUES IN THE ACTIVE-SITE
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Date
1988
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Abstract
Yeast pyruvate kinase was purified to near homogeneity and subjected to chemical modification by trinitrobenzenesulfonate and by P1, P2-bis (5'' pyridoxal) diphosphate. Labeled peptides were isolated and their amino acid composition was determined. 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. Protection experiments indicate that this lysine is located at the nucleotide binding site.