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

  1. Yaron, A. (1976). "Dipeptidyl carboxypeptidase from Escherichia coli". Methods Enzymol. 45: 599–610. doi:10.1016/s0076-6879(76)45053-x. PMID 13271.
  2. 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. doi:10.1128/jb.175.22.7290-7300.1993. PMC 206872. PMID 8226676.
  3. 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.
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