home *** CD-ROM | disk | FTP | other *** search
- *********************************************
- * Serine proteases, V8 family, active sites *
- *********************************************
-
- A number of prokaroytic proteases have been shown [1,2] to be evolutionary
- related; their catalytic activity is provided by a charge relay system similar
- to that of the trypsin family of serine proteases but which probably evolved
- by independent convergent evolution. The sequence around the residues involved
- in the catalytic triad (aspartic acid, serine and histidine) are completely
- different from that of the analogous residues in the trypsin serine proteases
- and can be used as signatures specific to that category of proteases. The
- proteases which are known to belong to this family are listed below.
-
- - Staphylococcus aureus V8 proteinase, which preferentially cleaves peptide
- bonds on the carboxyl-terminal side of aspartate and glutamate and which is
- widely used in protein sequencing studies.
- - Bacillus licheniformis glutamate specific endopeptidase (GSE) [3], which
- like V8 cleaves on the carboxyl-terminal side of acidic residues, but with
- a strong preference for glutamate.
- - Staphylococcus aureus exfoliative (or epidermolytic) toxins A (gene eta)
- and B (gene etb). These toxins cause impetigous diseases commonly referred
- to as staphylococcal scalded skin syndrome (SSSS) and have been shown [1]
- to possess proteolytic activity.
-
- -Consensus pattern: [ST]-G-[LIVMFYW](3)-G-x(2)-T-[LIVM]-x-T-x(2)-H
- [H 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: T-x(2)-G-[NQ]-S-G-S-x-[LIVM]-F
- [The first 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.
-
- -Last update: June 1992 / First entry.
-
- [ 1] Dancer S.J., Garratt R., Saldanha J., Jhoti H., Evans R.
- FEBS Lett. 268:129-132(1990).
- [ 2] Bailey C.J., Smith T.P.
- Biochem. J. 269:535-537(1990).
- [ 3] Svendsen I., Breddam K.
- Eur. J. Biochem. 204:165-171(1992).
-