Peptidyl-dipeptidase Dcp
Peptidyl-dipeptidase Dcp (EC 3.4.15.5, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is an enzyme.[1][2][3] It catalyses the following chemical 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
This zinc metallopeptidase is isolated from Escherichia coli and Salmonella typhimurium.
References
- ↑ Yaron, A. (1976). "Dipeptidyl carboxypeptidase from Escherichia coli". Methods Enzymol. 45: 599–610. doi:10.1016/s0076-6879(76)45053-x. PMID 13271.
- ↑ Henrich, B., Becker, S., Schroeder, U. and Plapp, R. (1993). "dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product". J. Bacteriol. 175: 7290–7300. PMID 8226676.
- ↑ Conlin, C.A. and Miller, C.G. (1995). "Oligopeptidase A and peptidyl-dipeptidase of Escherichia and Salmonella". Methods Enzymol. 248: 567–579. doi:10.1016/0076-6879(95)48036-6. PMID 7674945.
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