|PROSITE documentation PDOC00800|
Homoserine dehydrogenase (EC 188.8.131.52) (HDh) [1,2] catalyzes NAD-dependent reduction of aspartate β-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. The latter participates in the biosynthesis of threonine and then isoleucine as well as in that of methionine.
HDh is found either as a single chain protein as in some bacteria and yeast, or as a bifunctional enzyme consisting of an N-terminal aspartokinase domain and a C-terminal HDh domain as in bacteria such as Escherichia coli and in plants.
As a signature pattern, we selected the best conserved region of Hdh. This is a segment of 23 to 24 residues located in the central section and that contains two conserved aspartate residues.Last update:
July 1998 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Thomas D. Barbey R. Surdin-Kerjan Y.|
|Title||Evolutionary relationships between yeast and bacterial homoserine dehydrogenases.|
|Source||FEBS Lett. 323:289-293(1993).|
|2||Authors||Cami B. Clepet C. Patte J.-C.|
|Title||Evolutionary comparisons of three enzymes of the threonine biosynthetic pathway among several microbial species.|