Peptidyl-dipeptidase Dcp
Appearance
Peptidyl-dipeptidase Dcp | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.15.5 | ||||||||
CAS no. | 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 | ||||||||
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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 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 U.S. National Library of Medicine Medical Subject Headings (MeSH)