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 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.
Ramos
C
C
Departamento de Genética y Biotecnia, Facultad de Biología, Universidad de Sevilla, Spain.
Delgado
M A
MA
Calderon
I L
IL
D000596:Amino Acids / Q000494:pharmacology*; D001222:Aspartate Kinase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D010770:Phosphotransferases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D017853:Phosphotransferases (Alcohol Group Acceptor); D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism; D013379:Substrate Specificity; D013912:Threonine / Q000096:biosynthesis
D000596:Amino Acids; D013912:Threonine; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C021370:homoserine kinase; D001222:Aspartate Kinase