The Enzyme Database

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Accepted name: peptidyl-dipeptidase Dcp
Reaction: Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyse bonds in which P1′ is Pro, or both P1 and P1′ are Gly
Other name(s): dipeptidyl carboxypeptidase (Dcp); dipeptidyl carboxypeptidase
Comments: Known from Escherichia coli and Salmonella typhimurium. A zinc metallopeptidase in peptidase family M3 (thimet oligopeptidase family). Ac-Ala┼Ala-Ala is a good test substrate [3]. Inhibited by captopril, as is peptidyl-dipeptidase A. Formerly EC, and included in EC, peptidyl-dipeptidase A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 395642-28-1
1.  Yaron, A. Dipeptidyl carboxypeptidase from Escherichia coli. Methods Enzymol. 45 (1976) 599–610. [DOI] [PMID: 13271]
2.  Henrich, B., Becker, S., Schroeder, U. and Plapp, R. dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product. J. Bacteriol. 175 (1993) 7290–7300. [DOI] [PMID: 8226676]
3.  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 created 1981 as EC, modified 1989, transferred 1996 to EC]

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