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- ******************************************
- * Serine carboxypeptidases, active sites *
- ******************************************
-
- All known carboxypeptidases are either metallo carboxypeptidases or serine
- carboxypeptidases (EC 3.4.16.5 and EC 3.14.16.6). The catalytic activity of
- the serine carboxypeptidases, like that of the trypsin family serine
- proteases, is provided by a charge relay system involving an aspartic acid
- residue hydrogen-bonded to a histidine, which is itself hydrogen-bonded to a
- serine [1]. Proteins known to be serine carboxypeptidases are:
-
- - Barley and wheat serine carboxypeptidases I, II, and III [2].
- - Yeast carboxypeptidase Y (YSCY) (gene PRC1), a vacuolar protease involved
- in degrading small peptides.
- - Yeast KEX1 protease, involved in killer toxin and alpha-factor precursor
- processing.
- - Fission yeast sxa2, a probable carboxypeptidase involved in degrading or
- processing mating pheromones [3].
- - Penicilium janthinellum carboxypetidase S1 [4].
- - Vertebrate protective protein / cathepsin A [5], a lysosomal protein which
- is not only a carboxypeptidase but also essential for the activity of both
- beta-galactosidase and neuraminidase.
-
- The sequences surrounding the active site serine and histidine residues are
- highly conserved in all these serine carboxypeptidases.
-
- -Consensus pattern: [LIVM]-x-[GT]-E-S-Y-[AG]-[GS]
- [S is the active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [LIVM]-x-[GDN]-[AG]-[SG]-H-x-V-P
- [H is the active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- sxa2.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: June 1994 / Patterns and text revised.
-
- [ 1] Liao D.I., Remington S.J.
- J. Biol. Chem. 265:6528-6531(1990).
- [ 2] Sorensen S.B., Svendsen I., Breddam K.
- Carlsberg Res. Commun. 54:193-202(1989).
- [ 3] Imai Y., Yamamoto M.
- Mol. Cell. Biol. 12:1827-1834(1992).
- [ 4] Svendsen I., Hofmann T., Endrizzi J., Remington J., Breddam K.
- FEBS Lett. 333:39-43(1993).
- [ 5] Galjart N.J., Morreau H., Willemsen R., Gillemans N., Bonten E.J.,
- D'Azzo A.
- J. Biol. Chem. 266:14754-14762(1991).
-