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MetaCyc Reaction: 3.4.15.5

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.4.15.5

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655 : dipeptidyl carboxypeptidase II Inferred from experiment : dcp

Supersedes EC number: 3.4.15.3

Reaction Locations: periplasmic space (sensu Gram-negative Bacteria)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Mass balance status: Balance undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: peptidyl-dipeptidase Dcp

Enzyme Commission Synonyms: dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase

Taxonomic Range: Bacteria

Enzyme Commission Summary:
This enzyme catalyzes 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.

Known from Escherichia coli and Salmonella typhimurium. A zinc metallopeptidase in peptidase family M3 (thimet oligopeptidase family). Ac-Ala-|-Ala-Ala is a good test substrate [Conlin95]. Inhibited by captopril, as is peptidyl-dipeptidase A. Formerly EC 3.4.15.3, and included in EC 3.4.15.1, peptidyl-dipeptidase A.

Citations: [Deutch78, Yaron72, Yaron76, Henrich93]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:3.4.15.5 , ENZYME:EC:3.4.15.5 , IUBMB-ExplorEnz:EC:3.4.15.5 , UniProt:RELATED-TO:P24171 , UniProt:RELATED-TO:P27236


References

Conlin95: Conlin CA, Miller CG (1995). "Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium." Methods Enzymol 248;567-79. PMID: 7674945

Deutch78: Deutch CE, Soffer RL (1978). "Escherichia coli mutants defective in dipeptidyl carboxypeptidase." Proc Natl Acad Sci U S A 75(12);5998-6001. PMID: 216006

Henrich93: 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(22);7290-300. PMID: 8226676

Yaron72: Yaron A, Mlynar D, Berger A (1972). "A dipeptidocarboxypeptidase from E. coli." Biochem Biophys Res Commun 47(4);897-902. PMID: 4554640

Yaron76: Yaron A (1976). "Dipeptidyl carboxypeptidase from Escherichia coli." Methods Enzymol 45;599-610. PMID: 13271


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sun Aug 30, 2015, biocyc14.