Aspartate kinase
Definition:
EC Tree > 2 Transferases > 2.7 Transferring phosphorus-containing groups > 2.7.2 Phosphotransferases with a carboxy group as acceptor > 2.7.2.4 aspartate kinase
Aspartate kinase is the first committed enzyme of the aspartate-family pathway. It phosphorylates L-aspartate on the beta-carboxyl, releasing ADP and 4-phospho-L-aspartate, feeding lysine, methionine, threonine and isoleucine biosynthesis. The E. coli enzyme is multifunctional, also carrying EC 1.1.1.3 homoserine dehydrogenase (two of four Arabidopsis isoenzymes likewise). The equilibrium favors the reverse, non-physiological direction. It occurs in viruses and cellular organisms.
Aspartate kinase is the first committed enzyme of the aspartate-family pathway. It phosphorylates L-aspartate on the beta-carboxyl, releasing ADP and 4-phospho-L-aspartate, feeding lysine, methionine, threonine and isoleucine biosynthesis. The E. coli enzyme is multifunctional, also carrying EC 1.1.1.3 homoserine dehydrogenase (two of four Arabidopsis isoenzymes likewise). The equilibrium favors the reverse, non-physiological direction. It occurs in viruses and cellular organisms.
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