|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 126.96.36.199
The direction shown, i.e. which substrates are on the left and right sides, 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: 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 188.8.131.52 Xaa-Pro dipeptidyl-peptidase of lactococci.
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
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
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