Aspartate kinase and homoserine dehydrogenase of Candida utilis

Aspartate kinase and homoserine dehydrogenase activity were assayed in a dialyzed cell-free extract of Candida utilis. Aspartate kinase was partly inhibited by ATP-Mg and by Mg2+ alone. There appear to be two isoenzymes of aspartate kinase in the yeast, one heat-labile, the other relatively heat-stable. The first is subject to feedback inhibition by threonine, the other is threonine-resistant. Neither aspartate kinase nor homoserine dehydrogenase is the rate-limiting enzyme in methionine biosynthesis. Homoserine dehydrogenase measured in the forward direction showed an activity five times higher than aspartate kinase. No regulatory interaction could be demonstrated for this enzyme. No repression of aspartate kinase and homoserine dehydrogenase synthesis by threonine, methionine or both amino acids was observed.