Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 3.4.14.5

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

EC Number: 3.4.14.5

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: dipeptidyl-peptidase IV

Enzyme Commission Synonyms: dipeptidyl aminopeptidase IV, Xaa-Pro-dipeptidyl-aminopeptidase, Gly-Pro naphthylamidase, postproline dipeptidyl aminopeptidase IV, lymphocyte antigen CD26, glycoprotein GP110, dipeptidyl peptidase IV, glycylproline aminopeptidase, X-prolyl dipeptidyl aminopeptidase, pep X, leukocyte antigen CD26, glycylprolyl dipeptidylaminopeptidase, dipeptidyl-peptide hydrolase, glycylprolyl aminopeptidase, dipeptidyl-aminopeptidase IV, DPP IV/CD26, amino acyl-prolyl dipeptidyl aminopeptidase, T cell triggering molecule Tp103, X-PDAP

Enzyme Commission Summary:
This enzyme catalyzes Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.

A homodimer. An integral protein of the plasma membrane of lymphocytes and other mammalian cells, in peptidase family S9 (prolyl oligopeptidase family). The reaction is similar to that of the unrelated EC 3.4.14.11 Xaa-Pro dipeptidyl-peptidase of lactococci.

Citations: [Misumi92, David93, Ikehara94]

Relationship Links: BRENDA:EC:3.4.14.5 , ENZYME:EC:3.4.14.5 , IUBMB-ExplorEnz:EC:3.4.14.5 , UniProt:RELATED-TO:P14740 , UniProt:RELATED-TO:P22411 , UniProt:RELATED-TO:P27487 , UniProt:RELATED-TO:Q7M2P2


References

David93: David F, Bernard AM, Pierres M, Marguet D (1993). "Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases." J Biol Chem 268(23);17247-52. PMID: 8102366

Ikehara94: Ikehara Y, Ogata S, Misumi Y (1994). "Dipeptidyl-peptidase IV from rat liver." Methods Enzymol 244;215-27. PMID: 7845210

Misumi92: Misumi Y, Hayashi Y, Arakawa F, Ikehara Y (1992). "Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface." Biochim Biophys Acta 1131(3);333-6. PMID: 1352704


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 18.5 on Thu Dec 18, 2014, BIOCYC14A.