PMID: 3143610Jan 1, 1988

Yeast pyruvate kinase: essential lysine residues in the active site

The International Journal of Biochemistry
M ImaraiJ Eyzaguirre


1. Yeast pyruvate kinase was purified to near homogeneity and subjected to chemical modification by trinitrobenzenesulfonate and by P1, P2-bis (5' pyridoxal) diphosphate. 2. Labeled peptides were isolated and their amino acid composition was determined. 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. Protection experiments indicate that this lysine is located at the nucleotide binding site.


Sep 27, 1979·Biochemical and Biophysical Research Communications·S C JohnsonJ M Cardenas
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Nov 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·T IsobeA Tsugita
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Jan 15, 1986·European Journal of Biochemistry·H InoueT Tanaka
Feb 15, 1987·Archives of Biochemistry and Biophysics·G BezaresS Bazaes
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Jun 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·N Lonberg, W Gilbert
Sep 1, 1983·Analytical Biochemistry·J Kyte, H Rodriguez
Jun 4, 1982·Biochimica Et Biophysica Acta·M V Hinrichs, J Eyzaguirre

Related Concepts

Pyruvate Kinase
Pyruvate Kinase Measurement
R-Type Pyruvate Kinase
Urine Lysine Measurement
Lysine Hydrochloride
Saccharomyces cerevisiae
Amino Acid [EPC]
Muscle Enzyme

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