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PROSITE documentation PDOC00800

Homoserine dehydrogenase signature





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

HOMOSER_DHGENASE, PS01042; Homoserine dehydrogenase signature  (PATTERN)


References

1AuthorsThomas D. Barbey R. Surdin-Kerjan Y.
TitleEvolutionary relationships between yeast and bacterial homoserine dehydrogenases.
SourceFEBS Lett. 323:289-293(1993).
PubMed ID8500624

2AuthorsCami B. Clepet C. Patte J.-C.
TitleEvolutionary comparisons of three enzymes of the threonine biosynthetic pathway among several microbial species.
SourceBiochimie 75:487-495(1993).
PubMed ID8395899



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