| 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 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 3.4.15.3, and included in EC 3.4.15.1, peptidyl-dipeptidase A. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 395642-28-1 |
| References: |
| 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] |
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| [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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