The Enzyme Database

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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, 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. [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. [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. [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]
[EC 3.4.24.70 created 1996]
 
 


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