Everything about Aspartokinase totally explained
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 isn't 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.. Absence from animals makes these enzymes key targets for new herbicides and biocides and for improvements in nutritional value of crops.
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