PROSITE: PDOC00149 (documentation)
View entry in NiceSite format
{PDOC00149}
{PS00165; DEHYDRATASE_SER_THR}
{BEGIN}
**********************************************************************
* 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: [DESH]-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.
-Other sequence(s) detected in SWISS-PROT: 12.
-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: November 1995 / 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).
+----------------------------------------------------------------------------+
| This PROSITE entry is copyright by the Swiss Institute of Bioinformatics |
| (SIB). There are no restrictions on its use by non-profit institutions as |
| long as its content is in no way modified and this statement is not |
| removed. Usage by and for commercial entities requires a license agreement |
| (See http://www.isb-sib.ch/announce/ or email to license@isb-sib.ch). |
+----------------------------------------------------------------------------+
{END}