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
| 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 | ||||||||
| |||||||||
This zinc metallopeptidase is isolated from Escherichia coli and Salmonella typhimurium.
References
- Yaron A (1976). "Dipeptidyl carboxypeptidase from Escherichia coli". Methods in Enzymology. 45: 599–610. doi:10.1016/s0076-6879(76)45053-x. PMID 13271.
- Henrich B, Becker S, Schroeder U, Plapp R (November 1993). "dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product". Journal of Bacteriology. 175 (22): 7290–300. doi:10.1128/jb.175.22.7290-7300.1993. PMC 206872. PMID 8226676.
- Conlin CA, Miller CG (1995). "Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium". Methods in Enzymology. 248: 567–79. 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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