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Information on EC 3.4.14.2 - dipeptidyl-peptidase II
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3.4.14.2 dipeptidyl-peptidase IISpecify your search results
Word Map
- 3.4.14.2
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glucagon-like
- glp-1
- mellitus
- dpp-iv
- incretins
-
peptidase-4
- peptide-1
- lysosomal
- dipeptides
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antidiabetic
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glycemic
- cathepsins
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prolyl
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insulinotropic
- linagliptin
- vildagliptin
- metformin
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glucose-dependent
- glucagon
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postprandial
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iv-deficient
- hypoglycemia
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glucose-lowering
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exopeptidase
- gip
- sulfonylurea
- aminopeptidases
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iv-like
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antihyperglycemic
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repopulation
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3.4.14.5
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proline-specific
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oligopeptidase
- saxagliptin
- gelatinase
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incretin-based
- alogliptin
- thiazolidinediones
- liraglutide
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excursion
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gliptins
-
sodium-glucose
- retrorsine
-
exenatide
-
post-proline
- diprotin
-
tripeptidyl
-
crevicular
- analysis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
release of an N-terminal dipeptide, Xaa-Yaa-/-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides
Synonyms
dipeptidyl peptidase, seprase, dpp ii, dipeptidyl peptidase ii, fibroblast activation protein alpha, dpp-ii, dppii, dp ii, dipeptidyl aminopeptidase ii, dipeptidylpeptidase ii, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
brain dipeptidyl aminopeptidase A
carboxytripeptidase
dipeptidyl aminopeptidase II
dipeptidyl arylamidase II
dipeptidyl peptidase
dipeptidyl peptidase 2
dipeptidyl peptidase II
dipeptidyl-aminopeptidase II
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dipeptidylpeptidase II
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DP II
DPP II
DPP2
DPP7
DPPII
DPPV
fibroblast activation protein alpha
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has dipeptidyl peptidase and a 170-kDa gelatinase activity
peptidase, dipeptidyl, II
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QPP
quiescent cell proline dipeptidase
additional information
carboxytripeptidase
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-
-
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dipeptidyl aminopeptidase II
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-
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dipeptidyl arylamidase II
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dipeptidyl peptidase II
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quiescent cell proline dipeptidase
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-
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additional information
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enzyme belongs to the Pro-X carboxypeptidase family S28
additional information
enzyme belongs to the Pro-X carboxypeptidase family S28
additional information
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enzyme belongs to the Pro-X carboxypeptidase family S28
additional information
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enzyme belongs to the Pro-X carboxypeptidase family S28
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal dipeptide, Xaa-Yaa-/-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
exopeptidase, N-terminus dipeptide
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CAS REGISTRY NUMBER
COMMENTARY
76199-23-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ala-Ala-2-nitroanilide + H2O
Ala-Ala + 2-nitroaniline
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low activity
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
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39% activity compared to Met-Ala-Ser
-
-
?
Ala-Ala-p-nitroanilide + H2O
Ala-Ala + p-nitroaniline
-
481% activity compared to Gly-Pro-7-amido-4-methylcoumarin
-
-
?
Arg-Pro-2-naphthylamide + H2O
Arg-Pro + 2-naphthylamine
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27% of the activity with Phe-Pro-2-naphthylamide
-
-
?
Gly-Ala-7-amido-4-methylcoumarin + H2O
Gly-Ala + 7-amino-4-methylcoumarin
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-Gly-Gly + H2O
Gly-Pro + Gly-Gly
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16% activity compared to Met-Ala-Ser
-
-
?
L-Lys-L-Ala-5-chloro-1-anthraquinonylhydrazide-2HBr + H2O
L-Lys-L-Ala + 5-Cl-1-anthraquinonylhydrazine + HBr
-
i.e. Lys-Ala-CAH, synthetic substrate for colorimetric assay
i.e. CAH, forms a highly insoluble, deeply colored hydrazone when coupled to an aromatic aldehyde, e.g. 4-nitrobenzaldehyde or piperonal, useful for histochemical detection of the enzyme
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
-
?
Nle-Pro-7-amido-4-methylcoumarin + H2O
Nle-Pro + 7-amino-4-methylcoumarin
-
-
?
Phe-Pro-4-methylcoumarin 7-amide + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
Ala-Pro + amino-4-trifluoromethylcoumarin
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-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
Ala-Pro + amino-4-trifluoromethylcoumarin
-
-
-
?
Arg-Ala-2-naphthylamide + H2O
Arg-Ala + 2-naphthylamine
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11% of the activity with Phe-Pro-2-naphthylamide
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-
?
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
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591% activity compared to Gly-Pro-7-amido-4-methylcoumarin
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-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
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specific for proline
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?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
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specific for proline
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
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100% activity
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
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562% activity compared to Gly-Pro-7-amido-4-methylcoumarin
-
-
?
L-Lys-L-Ala-7-amido-4-methylcoumarin + H2O
L-Lys-L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Lys-L-Ala-7-amido-4-methylcoumarin + H2O
L-Lys-L-Ala + 7-amino-4-methylcoumarin
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-
-
-
?
Lys-Ala-2-(4-methoxy)-naphthylamide Lys-Ala-4-methoxy-2-naphthylamide + H2O
?
-
-
-
-
?
Lys-Ala-2-(4-methoxy)-naphthylamide Lys-Ala-4-methoxy-2-naphthylamide + H2O
?
-
-
-
-
?
Lys-Ala-2-naphthylamide + H2O
Lys-Ala + 2-naphthylamine
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-
-
-
?
Lys-Ala-2-naphthylamide + H2O
Lys-Ala + 2-naphthylamine
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15% of the activity with Phe-Pro-2-naphthylamide
-
-
?
Lys-Ala-4-methylcoumaryl-7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-4-methylcoumaryl-7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
?
Lys-Ala-4-methylcoumaryl-7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
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38% activity compared to Gly-Pro-7-amido-4-methylcoumarin
-
-
?
Lys-Pro-2-naphthylamide + H2O
Lys-Pro + 2-naphthylamine
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46% of the activity with Phe-Pro-2-naphthylamide
-
-
?
additional information
?
-
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Pro and Arg are the preferred penultimate residues
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-
?
additional information
?
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no hydrolysis occurs if either the carboxyl group or the amino group of otherwise susceptible tripeptides is blocked. Tetrapeptides, tripeptide esters and dipeptides are not attacked
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?
additional information
?
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Ala and Pro are the preferred residues in the P1 position
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?
additional information
?
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