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PROSITE documentation PDOC00149 |
Serine and threonine dehydratases [1,2] are functionally and structurally related pyridoxal-phosphate dependent enzymes:
Threonine synthase (EC 4.2.3.1) is also a pyridoxal-phosphate enzyme, it catalyzes the transformation of homoserine-phosphate into threonine. It has been shown [3] that threonine synthase is distantly related to the serine/ threonine dehydratases.
In all these enzymes, the pyridoxal-phosphate group is attached to a lysine residue. The sequence around this residue is sufficiently conserved to allow the derivation of a pattern specific to serine/threonine dehydratases and threonine synthases.
Note:Some bacterial L-serine dehydratases - such as those from Escherichia coli - are iron-sulfur proteins [4] and do not belong to this family.
Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Ogawa H. Gomi T. Konishi K. Date T. Nakashima H. Nose K. Matsuda Y. Peraino C. Pitot H.C. Fujioka M. |
Title | Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. | |
Source | J. Biol. Chem. 264:15818-15823(1989). | |
PubMed ID | 2674117 |
2 | Authors | Datta P. Goss T.J. Omnaas J.R. Patil R.V. |
Title | Covalent structure of biodegradative threonine dehydratase of Escherichia coli: homology with other dehydratases. | |
Source | Proc. Natl. Acad. Sci. U.S.A. 84:393-397(1987). | |
PubMed ID | 3540965 |
3 | Authors | Parsot C. |
Title | Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase. | |
Source | EMBO J. 5:3013-3019(1986). | |
PubMed ID | 3098560 |
4 | Authors | Grabowski R. Hofmeister A.E.M. Buckel W. |
Title | Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters. | |
Source | Trends Biochem. Sci. 18:297-300(1993). | |
PubMed ID | 8236444 |