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- **********************************************************************
- * Serine/threonine dehydratases pyridoxal-phosphate attachment site *
- **********************************************************************
-
- Serine and threonine dehydratases [1,2] are functionally and structurally
- related pyridoxal-phosphate dependent enzymes:
-
- - L-Serine dehydratase (EC 4.2.1.13) and D-Serine dehydratase (EC 4.2.1.14)
- catalyze the dehydratation of L-serine (respectively D-serine) into ammonia
- and pyruvate.
- - Threonine dehydratase (EC 4.2.1.16) (TDH) catalyzes the dehydratation of
- threonine into alpha-ketobutarate and ammonia. In Escherichia coli and
- other microorganisms, two classes of TDH are known to exist. One is
- involved in the biosynthesis of isoleucine, the other in hydroxamino acid
- catabolism.
-
- Threonine synthase (EC 4.2.99.2) 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.
-
- -Consensus pattern: [DE]-x(4,5)-[STVG]-x-[AS]-[FYI]-K-[DLIFSA]-[RVMF]-[GA]-
- [LIVMGA]
- [The K is the pyridoxal-P attachment site]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for Corynebacterium glutamicum threonine synthase.
- -Other sequence(s) detected in SWISS-PROT: 4.
-
- -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: June 1994 / Pattern and text revised.
-
- [ 1] Ogawa H., Gomi T., Konishi K., Date T., Naakashima H., Nose K.,
- Matsuda Y., Peraino C., Pitot H.C., Fujioka M.
- J. Biol. Chem. 264:15818-15823(1989).
- [ 2] Datta P., Goss T.J., Omnaas J.R., Patil R.V.
- Proc. Natl. Acad. Sci. U.S.A. 84:393-397(1987).
- [ 3] Parsot C.
- EMBO J. 5:3013-3019(1986).
- [ 4] Grabowski R., Hofmeister A.E.M., Buckel W.
- Trends Biochem. Sci. 18:297-300(1993).
-