IUBMB Enzyme Nomenclature

EC 3.4.15.5

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 names: dipeptidyl carboxypeptidase (Dcp); dipeptidyl carboxypeptidase

Comments: Known from Escherichia coli and Salmonella typhimurium. A zinc metallopeptidase in peptidase family M3 (thimet oligopeptidase family). Ac-AlaAla-Ala is a good test substrate [3]. Inhibited by captopril, as is peptidyl-dipeptidase A. Formerly EC 3.4.15.3, and included in EC 3.4.15.1, peptidyl-dipeptidase A.

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 395642-28-1

References

1. Yaron, A. Dipeptidyl carboxypeptidase from Escherichia coli. Methods Enzymol. 45 (1976) 599-610. [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. [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 3.4.15.5 created 1981 as EC 3.4.15.3, modified 1989, transferred 1996 to EC 3.4.15.5]


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