| EC |
3.4.24.70 |
| Accepted name: |
oligopeptidase A |
| 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 [4] |
| Other name(s): |
68000-M signalpeptide hydrolase |
| Comments: |
Known from Escherichia coli and Salmonella typhimurium. A zinc metallopeptidase, in peptidase family M3 (thimet oligopeptidase family), but differs from thimet oligopeptidase in lack of thiol-activation |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 394250-11-4 |
| References: |
| 1. |
Novak, P. and Dev, I.K. Degradation of a signal peptide by protease IV and oligopeptidase A. J. Bacteriol. 170 (1988) 5067–5075. [DOI] [PMID: 3053642] |
| 2. |
Conlin, C.A., Vimr, E.R. and Miller, C.G. Oligopeptidase A is required for normal phage P22 development. J. Bacteriol. 174 (1992) 5869–5880. [DOI] [PMID: 1522065] |
| 3. |
Conlin, C.A., Trun, N.J., Silhavy, T.J. and Miller, C.G. Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene. J. Bacteriol. 174 (1992) 5881–5887. [DOI] [PMID: 1325967] |
| 4. |
Conlin, C.A. and Miller, C.G. Oligopeptidase A and peptidyl-dipeptidase of Escherichia and Salmonella. Methods Enzymol. 248 (1995) 567–579. [PMID: 7674945] |
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| [EC 3.4.24.70 created 1996] |
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