Inhibition by different amino acids of the aspartate kinase and the homoserine kinase of the yeast Saccharomyces cerevisiae

In this paper, we describe a simple method to measure the yeast homoserine kinase and aspartate kinase activities, independently but in the same extract. With this method, we have determined some kinetic parameters for the physiological substrates of both enzymes, and investigated the inhibition exe...

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Bibliographic Details
Published in:FEBS letters 1991-01, Vol.278 (1), p.123-126
Main Authors: RAMOS, C, DELGADO, M. A, CALDERON, I. L
Format: Article
Language:English
Subjects:
Amino Acids - pharmacology
Analytical, structural and metabolic biochemistry
Aspartate Kinase - antagonists & inhibitors
Aspartate Kinase - metabolism
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Phosphotransferases (Alcohol Group Acceptor)
Phosphotransferases - antagonists & inhibitors
Phosphotransferases - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - metabolism
Substrate Specificity
Threonine - biosynthesis
Transferases
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Summary:In this paper, we describe a simple method to measure the yeast homoserine kinase and aspartate kinase activities, independently but in the same extract. With this method, we have determined some kinetic parameters for the physiological substrates of both enzymes, and investigated the inhibition exerted by different amino acids on these activities. Of all natural amino acids tested, only threonine inhibits effectively both enzymatic activities, although to a different degree. We did not find the reported inhibition by L-homoserine over the aspartate kinase. Altogether the data point to the aspartate kinase and to the threonine as the key factors in the regulation of this route.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(91)80098-N