Peptidyl-dipeptidase Dcp
| Peptidyl-dipeptidase Dcp | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.15.5 | ||||||||
| CAS number | 395642-28-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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.; 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.; 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.
External links
- Peptidyl-dipeptidase Dcp at the US National Library of Medicine Medical Subject Headings (MeSH)
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