Aspartokinase

Aspartokinase (or Aspartate 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 aspartkinase is present only in microorganisms and plants; it is not present in animals, who must obtain aspartate-family amino acids in their diet.

In E. 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. [cite journal|author=Voet D, Voet JG.
year= 2004|title=Biochemistry 3rd ed. Wiley: Hoboken, NJ.|volume=1|pmid=16729065|doi=10.1038/msb4100040|journal=Molecular Systems Biology|pages=E1] . Absence from animals makes these enzymes key targets for new herbicides and biocides and for improvements in nutritional value of crops. [cite journal|author=Viola RE.|journal=Acc Chem Res.|year= 2001|vol=34|title=The central enzymes of the aspartate family of amino acid biosynthesis|pmid=11352712|pages=339–49|doi=10.1021/ar000057q|volume=34]

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