Aspartate kinase

Aspartate kinase (aspartokinase, aspartic kinase) is an enzyme that catalyzes the phosphorylation of the amino acid aspartate. This reaction is the first step in the biosynthesis of three essential amino acids: methionine, lysine, and threonine, known as the 'aspartate family'. The gene for aspartokinase is present only in microorganisms and plants; it is not present in animals, which must obtain aspartate-family amino acids in their diet.(See Template:Leucine metabolism in humans – this diagram does not include the pathway for β-leucine synthesis via leucine 2,3-aminomutase) Aspartate kinase (aspartokinase, aspartic kinase) is an enzyme that catalyzes the phosphorylation of the amino acid aspartate. This reaction is the first step in the biosynthesis of three essential amino acids: methionine, lysine, and threonine, known as the 'aspartate family'. The gene for aspartokinase is present only in microorganisms and plants; it is not present in animals, which must obtain aspartate-family amino acids in their diet. In Escherichia coli, aspartokinase is present as three independently regulated isozymes, each of which is specific to one of the three downstream biochemical pathways. This allows the independent regulation of the rates of methionine, lysine, and threonine production. The forms that produce threonine and lysine are subject to feedback inhibition, and all three can be repressed at the level of gene expression by high concentrations of their end-products. Absence from animals makes these enzymes key targets for new herbicides and biocides and for improvements in nutritional value of crops. This protein may use the morpheein model of allosteric regulation.