PROSITE documentation PDOC00800Homoserine dehydrogenase signature
Homoserine dehydrogenase (EC 1.1.1.3) (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.
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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). | |
| PubMed ID | 8500624 |
| 2 | Authors | Cami B. Clepet C. Patte J.-C. |
| Title | Evolutionary comparisons of three enzymes of the threonine biosynthetic pathway among several microbial species. | |
| Source | Biochimie 75:487-495(1993). | |
| PubMed ID | 8395899 |
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