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- *************************************
- * Prephenate dehydratase signatures *
- *************************************
-
- Prephenate dehydratase (EC 4.2.1.51) (PDT) catalyzes the decarboxylation of
- prephenate into phenylpyruvate. In microorganisms PDT is involved in the
- terminal pathway of the biosynthesis of phenylalanine. In some bacteria such
- as Escherichia coli PDT is part of a bifunctional enzyme (P-protein) that also
- catalyzes the transformation of chorismate into prephenate (chorismate
- mutase) while in other bacteria it is a monofunctional enzyme. The sequence of
- monofunctional PDT align well with the C-terminal part of that of P-proteins
- [1].
-
- As signature patterns for PDT we selected two conserved regions. The first
- region contains a conserved threonine which has been said to be essential for
- the activity of the enzyme in E. coli. The second region includes a conserved
- glutamate. Both regions are in the C-terminal part of PDT.
-
- -Consensus pattern: [FY]-x-[LIVM]-x(2)-[LIVM]-x(5)-[DN]-x(5)-T-R-F-[LIVM]-x-
- [LIVM]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [LIVM]-[ST]-[KR]-[LIVM]-E-[ST]-R-P
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: October 1993 / First entry.
-
- [ 1] Fischer R.S., Zhao G., Jensen R.A.
- J. Gen. Microbiol. 137:1293-1301(1991).
-