|PROSITE documentation PDOC00289 [for PROSITE entry PS00324]|
Aspartokinase (EC 126.96.36.199) (AK)  catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine.
In Escherichia coli, there are three different isozymes which differ in their sensitivity to repression and inhibition by Lys, Met and Thr. AK1 (gene thrA) and AK2 (gene metL) are bifunctional enzymes which both consist of an N-terminal AK domain and a C-terminal homoserine dehydrogenase domain. AK1 is involved in threonine biosynthesis and AK2, in that of methionine. The third isozyme, AK3 (gene lysC), is monofunctional and involved in lysine synthesis. In yeast, there is a single isozyme of AK (gene HOM3).
As a signature pattern for AK, we selected a conserved region located in the N-terminal extremity.Last update:
November 1995 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Rafalski J.A. Falco S.C.|
|Title||Structure of the yeast HOM3 gene which encodes aspartokinase.|
|Source||J. Biol. Chem. 263:2146-2151(1988).|