Oligopeptidase A
| Oligopeptidase A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.70 | ||||||||
| CAS no. | 394250-11-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Oligopeptidase A (EC 3.4.24.70, 68000-M signalpeptide hydrolase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
This enzyme is known from Escherichia coli and Salmonella typhimurium.
References
- ^ Novak, P.; Dev, I.K. (1988). "Degradation of a signal peptide by protease IV and oligopeptidase A". J. Bacteriol. 170: 5067–5075. PMID 3053642.
- ^ Conlin, C.A.; Vimr, E.R.; Miller, C.G. (1992). "Oligopeptidase A is required for normal phage P22 development". J. Bacteriol. 174: 5869–5880. PMID 1522065.
- ^ Conlin, C.A.; Trun, N.J.; Silhavy, T.J.; Miller, C.G. (1992). "Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene". J. Bacteriol. 174: 5881–5887. PMID 1325967.
- ^ Conlin, C.A.; Miller, C.G. (1995). "Oligopeptidase A and peptidyl-dipeptidase of Escherichia and Salmonella". Methods Enzymol. 248: 567–579. doi:10.1016/0076-6879(95)48036-6. PMID 7674945.
External links
- Oligopeptidase+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH)