home *** CD-ROM | disk | FTP | other *** search
- ******************************************************************
- * Cys/Met metabolism enzymes pyridoxal-phosphate attachment site *
- ******************************************************************
-
- A number of pyridoxal-dependent enzymes involved in the metabolism of
- cysteine, homocysteine and methionine have been shown [1,2] to be evolutionary
- related. These are:
-
- - Cystathionine gamma-lyase (EC 4.4.1.1) (gamma-cystathionase), which
- catalyzes the transformation of cystathionine into cysteine, oxobutanoate
- and ammonia. This is the final reaction in the transulfuration pathway that
- leads from methionine to cysteine in eukaryotes.
- - Cystathionine gamma-synthase (EC 4.2.99.9), which catalyzes the conversion
- of cysteine and succinyl-homoserine into cystathionine and succinate: the
- first step in the biosynthesis of methionine from cysteine in bacteria
- (gene metB).
- - Cystathionine beta-lyase (EC 4.4.1.8) (beta-cystathionase), which catalyzes
- the conversion of cystathionine into homocysteine, pyruvate and ammonia:
- the second step in the biosynthesis of methionine from cysteine in bacteria
- (gene metC).
- - OAH/OAS sulfhydrylase, which catalyzes the conversion of acetylhomoserine
- into homocysteine and that of acetylserine into cysteine (gene MET17 or
- MET25 in yeast).
-
- These enzymes are proteins of about 400 amino-acid residues. The pyridoxal-P
- group is attached to a lysine residue located in the central section of these
- enzymes; the sequence around this residue is highly conserved and can be used
- as a signature pattern to detect this class of enzymes.
-
- -Consensus pattern: D-[LIVM]-x(3)-[SAGC](2)-T-K-[YW]-[LIVM]-x-G-H-[SG]
- [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: NONE.
- -Last update: October 1993 / First entry.
-
- [ 1] Ono B.I., Tanaka K., Naito K., Heike C., Shinoda S., Yamamoto S.,
- Ohmori S., Oshima T., Toh-E A.
- J. Bacteriol. 174:3339-3347(1992).
- [ 2] Barton A.B., Kaback D.B., Clark M.W., Keng T., Ouellette B.F.F.,
- Storms R.K., Zeng B., Zhong W.W., Fortin N., Delaney S., Bussey H.
- Yeast 9:363-369(1993).
-