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3.4.14.5: dipeptidyl-peptidase IV

This is an abbreviated version!
For detailed information about dipeptidyl-peptidase IV, go to the full flat file.

Word Map on EC 3.4.14.5

Reaction

release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline =

Synonyms

(GLP1)-degrading enzyme, ACT3, ADA binding protein, ADA-binding protein, ADABP, adenosine deaminase binding protein, Adenosine deaminase complexing protein, adenosine deaminase-binding protein, amino acyl-prolyl dipeptidyl aminopeptidase, aminopeptidase, glycylproline, Bile canaliculus domain-specific membrane glycoprotein, CD26, CD26 peptidase, CD26/dipeptidyl peptidase, CD26/DP IV, DAP IV, DapB, dapUm, dipeptidyl aminopeptidase IV, dipeptidyl dipeptidase IV, dipeptidyl peptidase 4, dipeptidyl peptidase 8, dipeptidyl peptidase 9, dipeptidyl peptidase IV, dipeptidyl peptidase-4, dipeptidyl peptidase-IV, dipeptidyl-aminopeptidase IV, dipeptidyl-peptidase 4, dipeptidyl-peptidase IV (CD26), dipeptidyl-peptide hydrolase, dipeptidylpeptidase 4a, dipeptidylpeptidase 4b, dipeptidylpeptidase IV, dipeptidylpeptidase IV/CD26, dipeptidylpeptidase-IV, DP IV, DP-IV, DPIV, DPP, DPP IV, DPP IV/CD26, DPP-4, DPP-IV, DPP4, DPP8, DPP9, DPPIV, DppIVA, DppIVB, glucagon-like peptide 1-degrading enzyme, Gly-Pro-naphthylamidase, glycoprotein GP110, glycylproline aminopeptidase, glycylproline-dipeptidyl-aminopeptidase, glycylprolyl aminopeptidase, glycylprolyl dipeptidylaminopeptidase, GP110 glycoprotein, h-DPPIV, hDPPIV, leukocyte antigen CD26, lymphocyte, antigen CD26, More, omega DPPIV, omega enzyme, omega gene product, Pep X, peptidase, dipeptidyl, IV, PepX, postproline dipeptidyl aminopeptidase IV, prolyl-dipeptidyl-aminopeptidase, sipeptidyl peptidase IV, T cell triggering molecule Tp103, T-cell activation antigen CD26, THAM, Thymocyte-activating molecule, TP103, type IV dipeptidyl aminopeptidase, WC10, X-PDAP, X-prolyl dipeptidyl aminopeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro-dipeptidyl-aminopeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases
                3.4.14.5 dipeptidyl-peptidase IV

Expression

Expression on EC 3.4.14.5 - dipeptidyl-peptidase IV

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both high-fat and high-sucrose diet-fed rats show significantly higher plasma DPP IV activity than normal diet-fed rats in the order of high-fat diet>high-sucrose diet>normal diet
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DPIV expression is progressively downregulated in endometrial adenocarcinoma
DPP IV activity isincreased in plasma of hypertensive patients with concomitant pulmonary hypertension and in atrial tissue of patients with chronic persistent atrial fibrillation
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DPP-IV mRNA and protein levels are null or markedly reduced in non-small cell lung cancer cell lines, endometrial cancer, colon adenocarcinoma, and melanoma cells
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DPP-IV protein expression is up-regulated in thyroid cancer, lung cancer, follicular thyroid cancer, and glioma
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high-fat and high-sucrose diets do not significantly affect DPP IV activity and mRNA expression in the kidney
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high-fat, but not high-sucrose diet causes a significant decrease in DPP IV activity in the liver as compared to the control
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monosodium glutamate and/or food deprivation decreases the activity of DPPIV insensitive to diprotin A in the soluble and membrane-bound fraction from the hypothalamus, as well as the activity of DPPIV sensitive to diprotin A in the soluble fraction from the hypothalamus and in the membrane-bound fraction from the hippocampus
monosodium glutamate and/or food deprivation increases the activity of DPPIV insensitive to diprotin A in the membrane-bound fraction from the hippocampus
plasma DPP4 activity increases progressively with time after streptozotocin treatment in wild type rats, the kidney of wild type rats show decreased DPP4 activity with increased Dpp4 mRNA after streptozotocin treatment
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the activity of dipeptidyl peptidase IV is elevated up to 3fold in mucopolysacharidoses patients
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