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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
-
glucagon-like
- glp-1
- mellitus
- dpp-iv
- incretins
-
peptidase-4
- peptide-1
- lysosomal
- dipeptides
-
antidiabetic
-
glycemic
- cathepsins
-
prolyl
-
insulinotropic
- linagliptin
- vildagliptin
- metformin
-
glucose-dependent
- glucagon
-
postprandial
-
iv-deficient
- hypoglycemia
-
glucose-lowering
-
exopeptidase
- gip
- sulfonylurea
- aminopeptidases
-
iv-like
-
antihyperglycemic
-
repopulation
-
3.4.14.5
-
proline-specific
-
oligopeptidase
- saxagliptin
- gelatinase
-
incretin-based
- alogliptin
- thiazolidinediones
- liraglutide
-
excursion
-
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
-
-
-
-
dipeptidylpeptidase II
-
-
-
-
DP II
DPP II
DPP2
DPP7
DPPII
DPPV
fibroblast activation protein alpha
-
has dipeptidyl peptidase and a 170-kDa gelatinase activity
peptidase, dipeptidyl, II
-
-
-
-
QPP
quiescent cell proline dipeptidase
additional information
carboxytripeptidase
-
-
-
-
dipeptidyl aminopeptidase II
-
-
-
-
dipeptidyl arylamidase II
-
-
-
-
dipeptidyl peptidase II
-
-
-
-
quiescent cell proline dipeptidase
-
-
-
-
additional information
-
enzyme belongs to the Pro-X carboxypeptidase family S28
additional information
enzyme belongs to the Pro-X carboxypeptidase family S28
additional information
-
enzyme belongs to the Pro-X carboxypeptidase family S28
additional information
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
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
-
low activity
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
-
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
-
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
-
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
-
-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
Ala-Pro + amino-4-trifluoromethylcoumarin
-
-
-
?
Arg-Ala-2-naphthylamide + H2O
Arg-Ala + 2-naphthylamine
-
11% of the activity with Phe-Pro-2-naphthylamide
-
-
?
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
-
591% activity compared to Gly-Pro-7-amido-4-methylcoumarin
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
specific for proline
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
specific for proline
-
?
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
-
100% activity
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
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
-
-
-
-
?
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
-
-
-
-
?
Lys-Ala-2-naphthylamide + H2O
Lys-Ala + 2-naphthylamine
-
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
-
38% activity compared to Gly-Pro-7-amido-4-methylcoumarin
-
-
?
Lys-Pro-2-naphthylamide + H2O
Lys-Pro + 2-naphthylamine
-
46% of the activity with Phe-Pro-2-naphthylamide
-
-
?
additional information
?
-
-
Pro and Arg are the preferred penultimate residues
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Ala and Pro are the preferred residues in the P1 position
-
-
?
additional information
?
-
Ala and Pro are the preferred residues in the P1 position
-
-
?
additional information
?
-
-
no activity with Ala-Ala-Ala-Ala-Ala, Arg-Pro-Lys-Pro (substance P 1-4), and Arg-Pro-Pro-Gly-Phe (bradikinin1-5)
-
-
?
additional information
?
-
-
the enzyme contributes to the alveolar macrophage's proteolytic capabilities
-
-
?
additional information
?
-
-
the enzyme contributes to the alveolar macrophage's proteolytic capabilities
-
-
?
additional information
?
-
-
hydrolyzes specifically N-terminal X-alanine or X-proline from their respective arylamides and from tripeptides or tetrapeptides, but not from pentapeptides
-
-
?
additional information
?
-
-
possible role of the mast cell enzyme in remodelling of connective tissue
-
-
?
additional information
?
-
-
the enzyme may play a role in the segregation and degradation of specific regions of normal lens fiber cells
-
-
?
additional information
?
-
-
Ala and Pro are the preferred residues in the P1 position
-
-
?
additional information
?
-
-
Ala and Pro are the preferred residues in the P1 position
-
-
?
additional information
?
-
-
no activity with Gly-Arg-7-amido-4-methylcoumarin, Arg-Arg-7-amido-4-methylcoumarin, and Ala-Arg-7-amido-4-methylcoumarin
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
the enzyme contributes to the alveolar macrophage's proteolytic capabilities
-
-
?
additional information
?
-
-
the enzyme contributes to the alveolar macrophage's proteolytic capabilities
-
-
?
additional information
?
-
-
hydrolyzes specifically N-terminal X-alanine or X-proline from their respective arylamides and from tripeptides or tetrapeptides, but not from pentapeptides
-
-
?
additional information
?
-
-
possible role of the mast cell enzyme in remodelling of connective tissue
-
-
?
additional information
?
-
-
the enzyme may play a role in the segregation and degradation of specific regions of normal lens fiber cells
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,S)-(2E)-2-(1-fluoro-2-[(2-phenylethyl)amino]ethylidene)cyclopentanecarbonitrile
-
IC50: 0.0361 mM, low inhibitory potential against EC 3.4.14.5
(1R,S)-(2E)-2-(1-fluoro-2-[(4-fluorobenzyl)amino]ethylidene)cyclopentanecarbonitrile
-
IC50: 0.0404 mM, low inhibitory potential against EC 3.4.14.5
(1R,S)-(2Z)-2-(1-fluoro-2-[(2-phenylethyl)amino]ethylidene)cyclopentanecarbonitrile
-
IC50: 0.0329 mM, low inhibitory potential against EC 3.4.14.5
(1R,S)-(2Z)-2-(1-fluoro-2-[(4-fluorobenzyl)amino]ethylidene)cyclopentanecarbonitrile
-
IC50: 0.0873 mM, low inhibitory potential against EC 3.4.14.5
(3S)-4-[(3aR,6aR)-hexahydrocyclopenta[b]pyrrol-1(2H)-yl]-4-oxobutane-1,3-diamine
-
AX8819, potent and selective inhibitor of DPP II
(3S)-N1-(4-chlorobenzyl)-4-(2-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
-
IC50: 2.3 mM; IC50: 2.3 nM
(3S)-N1-(4-chlorobenzyl)-4-(3-fluoropiperidin-1-yl)-4-oxobutane-1,3-diamine
-
0.62 nM; IC50: 0.62 nM
(3S)-N1-(4-chlorobenzyl)-4-(3-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
-
IC50: 1.13 nM
(3S)-N1-(4-chlorobenzyl)-4-(4-fluoropiperidin-1-yl)-4-oxobutane-1,3-diamine
-
IC50: 0.39 nM
(3S)-N1-(4-chlorobenzyl)-4-(4-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
-
IC50: 0.55 nM
1-((2S)-2-amino-4-((4-chlorobenzyl)amino)butanoyl)piperidin-3-ol
-
IC50: 54.7 nM
1-((2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl)piperidine-2-carbonitrile
-
IC50: 6.5 nM
1-benzyl-N-(2-cyclohexylidene-2-fluoroethyl)-4-piperidinamine
-
IC50: 0.00104 mM, low inhibitory potential against EC 3.4.14.5
1-benzyl-N-(2-cyclopentylidene-2-fluoroethyl)-4-piperidinamine
-
IC50: 0.0013 mM, low inhibitory potential against EC 3.4.14.5
1-benzyl-N-[2-oxo-2-(1-piperidinyl)ethyl]-4-piperidinamine
-
IC50: 0.0031 mM, low inhibitory potential against EC 3.4.14.5
1-[(2S)-2-amino-4-(benzylamino)butanoyl]piperidine-2-carbonitrile
-
IC50: 4.0 nM
1-[(2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl]piperidin-3-ol
-
IC50: 54.7 nM
1-[(2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl]piperidine-2-carbonitrile
-
IC50: 6.5 nM
3-((3-(S)-amino-4-oxo-4-(1-piperidinyl)butyl)aminomethyl)-benzonitrile
-
IC50: 2.7 nM
4-oxo-4-(1-piperidinyl)-N1 -(4-piperidinyl)-1,3-(S)-butanedi-amine
-
IC50: 85 nM
4-oxo-4-(1-piperidinyl)-N1-(2-thienylmethyl)-1,3-(S)-butanediamine
-
IC50: 0.8 nM
4-oxo-4-(1-piperidinyl)-N1-(4-pyridinylmethyl)-1,3-(S)-butanediamine
-
IC50: 0.75 nM
4-oxo-4-(1-piperidinyl)-N3-(4-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 0.017 mM
4-oxo-N1-(3-phenylpropyl)-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 1.91 nM
6-((3-(S)-amino-4-oxo-4-(1-piperidinyl)butyl)amino)nicotinonitrile
-
IC50: 0.0046 mM
benzamidine
-
10% inhibition at 1 mM, preincubation at room temperature for 15 min
benzyl 4-[(2-cyclohexylidene-2-fluoroethyl)amino]-1-piperidinecarboxylate
-
IC50: 0.0128 mM, low inhibitory potential against EC 3.4.14.5
diisopropylfluorophosphate
-
complete inhibition at 1 mM, 25% inhibition at 0.1 mM, preincubation at room temperature for 15 min
Lys-Ala chloromethyl ketone
-
0.1 mM, complete inhibition, active-site-directed inhibitor
N-(1,3-benzodioxol-5-ylmethyl)-2-cyclohexylidene-2-fluoroethanamine
-
IC50: 0.0129 mM, low inhibitory potential against EC 3.4.14.5
N-(1,3-benzodioxol-5-ylmethyl)-2-cyclopentylideneethanamine
-
0.0075 mM; IC50: 0.0075 mM, low inhibitory potential against EC 3.4.14.5, low inhibitory potential against EC 3.4.14.5
N-(2-cyclohexylidene-2-fluoroethyl)-1-adamantanamine
-
IC50: 0.0913 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclohexylidene-2-fluoroethyl)-4-piperidinamine
-
IC50: 0.0042 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclohexylidene-2-fluoroethyl)-N-(2-phenylethyl)-amine
-
IC50: 0.011 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclohexylidene-2-fluoroethyl)-N-(4-fluorobenzyl)-amine
-
IC50: 0.0219 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclohexylidene-2-fluoroethyl)-N-(4-methoxybenzyl)amine
-
IC50: 0.0134 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclohexylidene-2-fluoroethyl)aniline
-
IC50: 0.1 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclohexylidene-2-fluoroethyl)cyclohexanamine
-
IC50: 0.5 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclopentylidene-2-fluoroethyl)-N-(2-phenylethyl)amine
-
IC50: 0.0272 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclopentylidene-2-fluoroethyl)-N-(2-pyridinylethyl)amine
-
IC50: 0.0096 mM, low inhibitory potential against EC 3.4.14.5; IC50: 0.0157 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclopentylidene-2-fluoroethyl)-N-(4-fluorobenzyl)amine
-
IC50: 0.0108 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclopentylidene-2-fluoroethyl)-N-(4-methoxy-benzyl)amine
-
IC50: 0.0155 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclopentylidene-2-fluoroethyl)cyclohexanamine
-
IC50: 0.09 mM, low inhibitory potential against EC 3.4.14.5
N-(2-cyclopentylideneethyl)cyclohexanamine
-
IC50: 0.062 mM; IC50: 0.062 mM, low inhibitory potential against EC 3.4.14.5, low inhibitory potential against EC 3.4.14.5
N-4(chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine dihydrochloride
-
-
N-benzyl-2-cyclohexylidene-2-fluoroethanamine
-
IC50: 0.034 mM, low inhibitory potential against EC 3.4.14.5
N-benzyl-2-cyclopentylidene-2-fluoroethanamine
-
IC50: 0.0378 mM, low inhibitory potential against EC 3.4.14.5
N-benzyl-2-cyclopentylideneethanamine
-
IC50: 0.026 mM; IC50: 0.026 mM, low inhibitory potential against EC 3.4.14.5, low inhibitory potential against EC 3.4.14.5
N-benzyl-2-oxo-2-(1-piperidinyl)ethaneamine
-
IC50: 0.397 mM, low inhibitory potential against EC 3.4.14.5
N-benzyl-2-thioxo-2-(1-piperidinyl)ethaneamine
-
IC50: 0.0484 mM, low inhibitory potential against EC 3.4.14.5
N-cyclohexyl-2-oxo-2-(1-piperidinyl)ethaneamine
-
IC50: 0.177 mM, low inhibitory potential against EC 3.4.14.5
N-cyclohexyl-2-thioxo-2-(1-piperidinyl)ethaneamine
-
IC50: 0.069 mM, low inhibitory potential against EC 3.4.14.5
N-cyclohexyl-2-thioxo-2-(1-pyrrolidinyl)ethaneamine
-
IC50: 0.092 mM, low inhibitory potential against EC 3.4.14.5
N-piperonyl-2-oxo-2-(1-piperidinyl)ethaneamine
-
IC50: 0.052 mM, low inhibitory potential against EC 3.4.14.5
N-piperonyl-2-oxo-2-(1-pyrrolidinyl)ethaneamine
-
IC50: 0.063 mM, low inhibitory potential against EC 3.4.14.5
N-piperonyl-2-thioxo-2-(1-piperidinyl)ethaneamine
-
IC50: 0.042 mM, low inhibitory potential against EC 3.4.14.5
N-piperonyl-2-thioxo-2-(1-pyrrolidinyl)ethaneamine
-
IC50: 0.067 mM, low inhibitory potential against EC 3.4.14.5
N-[3-(S)-amino-4-oxo-4-(1-piperidinyl)butyl]guanidine bis-(trifluoroacetate)
-
IC50: 0.0018 mM
N-[3-amino-1-(S)-(1-piperidinylcarbonyl)propyl]guanidine bis-(trifluoroacetate)
-
IC50: 0.0074 mM
N1 -(2-cyclopentylidene-2-fluoroethyl)-N3,N3-dimethyl-1,3-propanediamine
-
IC50: 0.0537 mM, low inhibitory potential against EC 3.4.14.5
N1 -(4-methoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 0.66 nM
N1,N1-di(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 4.2 nM
N1-(1-naphthylmethyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 1.31 nM
N1-(2,4-dimethoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 2.7 nM
N1-(2-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 0.23 nM
N1-(2-cyclohexylidene-2-fluoroethyl)-N3,N3-dimethyl-1,3-propanediamine
-
IC50: 0.0546 mM, low inhibitory potential against EC 3.4.14.5
N1-(2-methoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 1.85 nM
N1-(2-naphthylmethyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 1.1 nM
N1-(3-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 1.34 nM
N1-(3-methoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 1.77 nM
N1-(3-nitro-2-pyridinyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 0.0235 mM
N1-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 0.48 nM
N1-(4-chlorobenzyl)-N1-methyl-4-oxo-4-(1-piperidinyl)-1,3-butanediamine
-
IC50: 0.22 nm
N1-(cyclohexylmethyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 1.1 nM
N1-[2-(benzyloxy)benzyl]-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 0.39 nM
N1-[4-(benzyloxy)benzyl]-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
-
IC50: 0.41 nM
N3-benzyl-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine dihydrobromide
-
IC50: 0.0125 mM
N6-benzyloxycarbonyl-Lys-Pro
-
1 mM, 31% inhibition of DPP II-S, 41% inhibition of DPP II-M
PCMBS
-
77% inhibition at 1 mM, preincubation at room temperature for 15 min
PMSF
-
45% inhibition at 1 mM, preincubation at room temperature for 15 min
puromycin aminonucleoside
-
inhibition by cations increases with the size of the ion
(3S)-N1-(4-chlorobenzyl)-4-oxo-4-piperidin-1-ylbutane-1,3-diamine
-
IC50: 1.1 nM
(3S)-N1-(4-chlorobenzyl)-4-oxo-4-piperidin-1-ylbutane-1,3-diamine
-
UAMC00039, potent and specific inhibitor
4-(2-aminoethyl)benzenesulfonyl fluoride
-
60% inhibition at 1 mM, preincubation at room temperature for 15 min
bestatin
-
1 mM, 12% inhibition of DPP II-S, 21% inhibition of DPP II-M; no inhibition
Cu2+
-
40% inhibition at 1 mM, preincubation at room temperature for 15 min
Hg2+
-
complete inhibition at 1 mM, preincubation at room temperature for 15 min
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
-
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
-
-
puromycin
-
1 mM, 76% inhibition; inhibition by cations increases with the size of the ion
Tris
-
50 mM, 96% inhibition; inhibition by cations increases with the size of the ion
additional information
-
not inhibited by N-ethylmaleimide, p-chloromercuribenzoate, iodoacetate, iodoacetamide, beta-mercaptoethanol, cysteine, EDTA, EGTA, o-phenanthroline, or dithiothreitol
-
additional information
-
poor or no inhibition by EDTA, NEM, E-64, diprotin A, and actinonin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the Dpp2 gene is transcriptionally activated by Kruppel-like factor 2 and TOB1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.36
Gly-L-Pro-4-nitroanilide
-
enzyme from renal cortex, in acetic buffer (pH 5.5), at 37°C
1.1
Gly-L-Pro-4-nitroanilide
-
enzyme from lung, in acetic buffer (pH 5.5), at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.8
Gly-L-Pro-4-nitroanilide
-
enzyme from lung, in acetic buffer (pH 5.5), at 37°C
11.5
Gly-L-Pro-4-nitroanilide
-
enzyme from renal cortex, in acetic buffer (pH 5.5), at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000082 - 0.00145
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
0.000052
lysyl-piperidide
substrate: Lys-Ala-p-nitroanilide, pH 7.0, 37°C
0.000063
lysyl-piperidide
substrate: Ala-Pro-p-nitroanilide, pH 7.0, 37°C
0.000082
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
-
-
0.00095
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
substrate: Lys-Ala-p-nitroanilide, pH 5.5, 37°C
0.001
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
substrate: Lys-Ala-p-nitroanilide, pH 7.0, 37°C
0.00105
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
substrate: Ala-Pro-p-nitroanilide, pH 7.0, 37°C
0.00145
N-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butane-diamine dihydrochloride
substrate: Ala-Pro-p-nitroanilide, pH 5.5, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0361
(1R,S)-(2E)-2-(1-fluoro-2-[(2-phenylethyl)amino]ethylidene)cyclopentanecarbonitrile
Homo sapiens
-
IC50: 0.0361 mM, low inhibitory potential against EC 3.4.14.5
0.0404
(1R,S)-(2E)-2-(1-fluoro-2-[(4-fluorobenzyl)amino]ethylidene)cyclopentanecarbonitrile
Homo sapiens
-
IC50: 0.0404 mM, low inhibitory potential against EC 3.4.14.5
0.0329
(1R,S)-(2Z)-2-(1-fluoro-2-[(2-phenylethyl)amino]ethylidene)cyclopentanecarbonitrile
Homo sapiens
-
IC50: 0.0329 mM, low inhibitory potential against EC 3.4.14.5
0.0873
(1R,S)-(2Z)-2-(1-fluoro-2-[(4-fluorobenzyl)amino]ethylidene)cyclopentanecarbonitrile
Homo sapiens
-
IC50: 0.0873 mM, low inhibitory potential against EC 3.4.14.5
0.00000088
(3S)-4-[(3aR,6aR)-hexahydrocyclopenta[b]pyrrol-1(2H)-yl]-4-oxobutane-1,3-diamine
Homo sapiens
-
-
0.0000023 - 2.3
(3S)-N1-(4-chlorobenzyl)-4-(2-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
0.62
(3S)-N1-(4-chlorobenzyl)-4-(3-fluoropiperidin-1-yl)-4-oxobutane-1,3-diamine
Homo sapiens
-
IC50: 0.62 nM
0.00000113
(3S)-N1-(4-chlorobenzyl)-4-(3-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
Homo sapiens
-
IC50: 1.13 nM
0.00000039
(3S)-N1-(4-chlorobenzyl)-4-(4-fluoropiperidin-1-yl)-4-oxobutane-1,3-diamine
Homo sapiens
-
IC50: 0.39 nM
0.00000055
(3S)-N1-(4-chlorobenzyl)-4-(4-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
Homo sapiens
-
IC50: 0.55 nM
0.0000547
1-((2S)-2-amino-4-((4-chlorobenzyl)amino)butanoyl)piperidin-3-ol
Homo sapiens
-
IC50: 54.7 nM
0.000113
1-((2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl)piperidin-4-ol
Homo sapiens
-
IC50: 113 nM
0.0000065
1-((2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl)piperidine-2-carbonitrile
Homo sapiens
-
IC50: 6.5 nM
0.0255
1-([(4-fluorobenzyl)amino]acetyl)-2-pyrrolidinecarbonitrile
Homo sapiens
-
IC50: 0.0255 mM
0.00104
1-benzyl-N-(2-cyclohexylidene-2-fluoroethyl)-4-piperidinamine
Homo sapiens
-
IC50: 0.00104 mM, low inhibitory potential against EC 3.4.14.5
0.0013
1-benzyl-N-(2-cyclopentylidene-2-fluoroethyl)-4-piperidinamine
Homo sapiens
-
IC50: 0.0013 mM, low inhibitory potential against EC 3.4.14.5
0.0031
1-benzyl-N-[2-oxo-2-(1-piperidinyl)ethyl]-4-piperidinamine
Homo sapiens
-
IC50: 0.0031 mM, low inhibitory potential against EC 3.4.14.5
0.000004
1-[(2S)-2-amino-4-(benzylamino)butanoyl]piperidine-2-carbonitrile
Homo sapiens
-
IC50: 4.0 nM
0.0000547
1-[(2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl]piperidin-3-ol
Homo sapiens
-
IC50: 54.7 nM
0.000113
1-[(2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl]piperidin-4-ol
Homo sapiens
-
IC50: 113 nM
0.0000065
1-[(2S)-2-amino-4-[(4-chlorobenzyl)amino]butanoyl]piperidine-2-carbonitrile
Homo sapiens
-
IC50: 6.5 nM
0.0000027
3-((3-(S)-amino-4-oxo-4-(1-piperidinyl)butyl)aminomethyl)-benzonitrile
Homo sapiens
-
IC50: 2.7 nM
0.000085
4-oxo-4-(1-piperidinyl)-N1 -(4-piperidinyl)-1,3-(S)-butanedi-amine
Homo sapiens
-
IC50: 85 nM
0.0000008
4-oxo-4-(1-piperidinyl)-N1-(2-thienylmethyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.8 nM
0.00000075
4-oxo-4-(1-piperidinyl)-N1-(4-pyridinylmethyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.75 nM
0.017
4-oxo-4-(1-piperidinyl)-N3-(4-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.017 mM
0.0000009
4-oxo-N1-(2-phenylethyl)-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.9 nM
0.00000191
4-oxo-N1-(3-phenylpropyl)-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 1.91 nM
0.0015
4-oxo-N1-phenyl-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.0015 mM
0.0046
6-((3-(S)-amino-4-oxo-4-(1-piperidinyl)butyl)amino)nicotinonitrile
Homo sapiens
-
IC50: 0.0046 mM
0.0128
benzyl 4-[(2-cyclohexylidene-2-fluoroethyl)amino]-1-piperidinecarboxylate
Homo sapiens
-
IC50: 0.0128 mM, low inhibitory potential against EC 3.4.14.5
0.0129
N-(1,3-benzodioxol-5-ylmethyl)-2-cyclohexylidene-2-fluoroethanamine
Homo sapiens
-
IC50: 0.0129 mM, low inhibitory potential against EC 3.4.14.5
0.0075
N-(1,3-benzodioxol-5-ylmethyl)-2-cyclopentylideneethanamine
Homo sapiens
-
IC50: 0.0075 mM, low inhibitory potential against EC 3.4.14.5, low inhibitory potential against EC 3.4.14.5
0.0913
N-(2-cyclohexylidene-2-fluoroethyl)-1-adamantanamine
Homo sapiens
-
IC50: 0.0913 mM, low inhibitory potential against EC 3.4.14.5
0.0042
N-(2-cyclohexylidene-2-fluoroethyl)-4-piperidinamine
Homo sapiens
-
IC50: 0.0042 mM, low inhibitory potential against EC 3.4.14.5
0.011
N-(2-cyclohexylidene-2-fluoroethyl)-N-(2-phenylethyl)-amine
Homo sapiens
-
IC50: 0.011 mM, low inhibitory potential against EC 3.4.14.5
0.0219
N-(2-cyclohexylidene-2-fluoroethyl)-N-(4-fluorobenzyl)-amine
Homo sapiens
-
IC50: 0.0219 mM, low inhibitory potential against EC 3.4.14.5
0.0134
N-(2-cyclohexylidene-2-fluoroethyl)-N-(4-methoxybenzyl)amine
Homo sapiens
-
IC50: 0.0134 mM, low inhibitory potential against EC 3.4.14.5
0.1
N-(2-cyclohexylidene-2-fluoroethyl)aniline
Homo sapiens
-
IC50: 0.1 mM, low inhibitory potential against EC 3.4.14.5
0.5
N-(2-cyclohexylidene-2-fluoroethyl)cyclohexanamine
Homo sapiens
-
IC50: 0.5 mM, low inhibitory potential against EC 3.4.14.5
0.0272
N-(2-cyclopentylidene-2-fluoroethyl)-N-(2-phenylethyl)amine
Homo sapiens
-
IC50: 0.0272 mM, low inhibitory potential against EC 3.4.14.5
0.0108
N-(2-cyclopentylidene-2-fluoroethyl)-N-(4-fluorobenzyl)amine
Homo sapiens
-
IC50: 0.0108 mM, low inhibitory potential against EC 3.4.14.5
0.0155
N-(2-cyclopentylidene-2-fluoroethyl)-N-(4-methoxy-benzyl)amine
Homo sapiens
-
IC50: 0.0155 mM, low inhibitory potential against EC 3.4.14.5
0.09
N-(2-cyclopentylidene-2-fluoroethyl)cyclohexanamine
Homo sapiens
-
IC50: 0.09 mM, low inhibitory potential against EC 3.4.14.5
0.034
N-benzyl-2-cyclohexylidene-2-fluoroethanamine
Homo sapiens
-
IC50: 0.034 mM, low inhibitory potential against EC 3.4.14.5
0.0378
N-benzyl-2-cyclopentylidene-2-fluoroethanamine
Homo sapiens
-
IC50: 0.0378 mM, low inhibitory potential against EC 3.4.14.5
0.397
N-benzyl-2-oxo-2-(1-piperidinyl)ethaneamine
Homo sapiens
-
IC50: 0.397 mM, low inhibitory potential against EC 3.4.14.5
0.0484
N-benzyl-2-thioxo-2-(1-piperidinyl)ethaneamine
Homo sapiens
-
IC50: 0.0484 mM, low inhibitory potential against EC 3.4.14.5
0.177
N-cyclohexyl-2-oxo-2-(1-piperidinyl)ethaneamine
Homo sapiens
-
IC50: 0.177 mM, low inhibitory potential against EC 3.4.14.5
0.069
N-cyclohexyl-2-thioxo-2-(1-piperidinyl)ethaneamine
Homo sapiens
-
IC50: 0.069 mM, low inhibitory potential against EC 3.4.14.5
0.092
N-cyclohexyl-2-thioxo-2-(1-pyrrolidinyl)ethaneamine
Homo sapiens
-
IC50: 0.092 mM, low inhibitory potential against EC 3.4.14.5
0.052
N-piperonyl-2-oxo-2-(1-piperidinyl)ethaneamine
Homo sapiens
-
IC50: 0.052 mM, low inhibitory potential against EC 3.4.14.5
0.063
N-piperonyl-2-oxo-2-(1-pyrrolidinyl)ethaneamine
Homo sapiens
-
IC50: 0.063 mM, low inhibitory potential against EC 3.4.14.5
0.042
N-piperonyl-2-thioxo-2-(1-piperidinyl)ethaneamine
Homo sapiens
-
IC50: 0.042 mM, low inhibitory potential against EC 3.4.14.5
0.067
N-piperonyl-2-thioxo-2-(1-pyrrolidinyl)ethaneamine
Homo sapiens
-
IC50: 0.067 mM, low inhibitory potential against EC 3.4.14.5
0.0018
N-[3-(S)-amino-4-oxo-4-(1-piperidinyl)butyl]guanidine bis-(trifluoroacetate)
Homo sapiens
-
IC50: 0.0018 mM
0.0074
N-[3-amino-1-(S)-(1-piperidinylcarbonyl)propyl]guanidine bis-(trifluoroacetate)
Homo sapiens
-
IC50: 0.0074 mM
0.0537
N1 -(2-cyclopentylidene-2-fluoroethyl)-N3,N3-dimethyl-1,3-propanediamine
Homo sapiens
-
IC50: 0.0537 mM, low inhibitory potential against EC 3.4.14.5
0.00000066
N1 -(4-methoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.66 nM
0.0000042
N1,N1-di(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 4.2 nM
0.0000006
N1,N1-dibenzyl-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.6 nM
0.00000131
N1-(1-naphthylmethyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 1.31 nM
0.0000027
N1-(2,4-dimethoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 2.7 nM
0.00000023
N1-(2-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.23 nM
0.0546
N1-(2-cyclohexylidene-2-fluoroethyl)-N3,N3-dimethyl-1,3-propanediamine
Homo sapiens
-
IC50: 0.0546 mM, low inhibitory potential against EC 3.4.14.5
0.00000185
N1-(2-methoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 1.85 nM
0.0000011
N1-(2-naphthylmethyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 1.1 nM
0.00000134
N1-(3-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 1.34 nM
0.00000177
N1-(3-methoxybenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 1.77 nM
0.0235
N1-(3-nitro-2-pyridinyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.0235 mM
0.00000048
N1-(4-chlorobenzyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.48 nM
0.00000022
N1-(4-chlorobenzyl)-N1-methyl-4-oxo-4-(1-piperidinyl)-1,3-butanediamine
Homo sapiens
-
IC50: 0.22 nm
0.0000011
N1-(cyclohexylmethyl)-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 1.1 nM
0.00000203
N1-benzyl-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 2.03 nM
0.0000186
N1-cyclohexyl-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 18.6 nM
0.00000039
N1-[2-(benzyloxy)benzyl]-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.39 nM
0.00000041
N1-[4-(benzyloxy)benzyl]-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine
Homo sapiens
-
IC50: 0.41 nM
0.0125
N3-benzyl-4-oxo-4-(1-piperidinyl)-1,3-(S)-butanediamine dihydrobromide
Homo sapiens
-
IC50: 0.0125 mM
0.00000048
[(1R)-1-[[(2S)-2,4-diaminobutanoyl]amino]pentyl]boronic acid
Homo sapiens
-
-
0.0000023
(3S)-N1-(4-chlorobenzyl)-4-(2-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
Homo sapiens
-
IC50: 2.3 nM
2.3
(3S)-N1-(4-chlorobenzyl)-4-(2-methylpiperidin-1-yl)-4-oxobutane-1,3-diamine
Homo sapiens
-
IC50: 2.3 mM
0.00000048
(3S)-N1-(4-chlorobenzyl)-4-oxo-4-piperidin-1-ylbutane-1,3-diamine
Homo sapiens
-
-
0.0000011
(3S)-N1-(4-chlorobenzyl)-4-oxo-4-piperidin-1-ylbutane-1,3-diamine
Homo sapiens
-
IC50: 1.1 nM
0.0096
N-(2-cyclopentylidene-2-fluoroethyl)-N-(2-pyridinylethyl)amine
Homo sapiens
-
IC50: 0.0096 mM, low inhibitory potential against EC 3.4.14.5
0.0157
N-(2-cyclopentylidene-2-fluoroethyl)-N-(2-pyridinylethyl)amine
Homo sapiens
-
IC50: 0.0157 mM, low inhibitory potential against EC 3.4.14.5
0.062
N-(2-cyclopentylideneethyl)cyclohexanamine
Homo sapiens
-
IC50: 0.062 mM, low inhibitory potential against EC 3.4.14.5, low inhibitory potential against EC 3.4.14.5
0.026
N-benzyl-2-cyclopentylideneethanamine
Homo sapiens
-
IC50: 0.026 mM, low inhibitory potential against EC 3.4.14.5, low inhibitory potential against EC 3.4.14.5
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5 - 6
5.3
5.5
7.5 - 8.2
5.5
-
hydrolysis of Lys-Ala-4-methyoxy-2-naphthylamine or Lys-Ala-2-naphthylamide
5.5
-
hydrolysis of Lys-Ala-4-methyoxy-2-naphthylamine or Lys-Ala-2-naphthylamide
7.5 - 8.2
-
hydrolysis of Gly-Pro-2-naphthylamide or Gly-Pro-2-(4-methoxy)-naphthylamide
7.5 - 8.2
-
hydrolysis of Gly-Pro-2-naphthylamide or Gly-Pro-2-(4-methoxy)-naphthylamide
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.7 - 5.8
-
pH 3.5: about 85% of maximal activity, pH 5.8: about 45% of maximal activity
4 - 6
pH 4.0: about 50% of maximal activity, pH 6.0: about 40% of maximal activity, substrate: Lys-Ala-p-nitroanilide or Ala-Pro-p-nitroanilide
5 - 6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
6.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
mRNA expression in ipsilateral and contralateral cortices. Dipeptidyl peptidase II and aminopeptidase N are up-regulated ipsilaterally from 6 h to 7 days post ischemia
brenda
-
peritoneal, 10-20fold higher activity as compared with macrophages
brenda
additional information
-
in epithelial cells of convoluted tubuls, no activity in the glomeruli
brenda
-
low activity, alveolar, myometrical and of the red pulp
brenda
-
enzyme activity of prepuberal gilts rises with the onset of estrus, again just prior to ovulation on day 21, and during pregnancy. The activity is markedly elevated during the luteal and proestrous phases compared to the postovulatory phase. The highest specific activities occur at the proestrus when the follicle wall is undergoing breakdown
brenda
-
low activity, myometrium, myometrial macrophages, epithelium
brenda
additional information
-
the enzyme is largely cell-associated during exponential growth in batch culture, but is progressively released by the bacteria before the cells enter stationary phase. The enzyme is completely cell-bound during growth in continuous culture
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
compartmentalization of DPP II activity within lysosomal dense bodies that are concentrated primarily in the equatorial and sutural regions
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DPP2_HUMAN
492
0
54341
Swiss-Prot
Secretory Pathway (Reliability: 3)
DPP2_MOUSE
506
0
56254
Swiss-Prot
Secretory Pathway (Reliability: 2)
DPP2_RAT
500
0
55114
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A8B6HK76_MYTGA
473
0
52353
TrEMBL
Secretory Pathway (Reliability: 1)
G8SKZ2_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
462
0
51058
TrEMBL
-
A0A2P6RC87_ROSCH
140
0
16294
TrEMBL
other Location (Reliability: 2)
A0A812CDX0_SEPPH
498
0
55778
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1Z5KSD7_FISSO
555
1
61621
TrEMBL
other Location (Reliability: 5)
A0A8M1N4B9_DANRE
500
0
56159
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Z5K3C7_FISSO
557
1
63184
TrEMBL
Secretory Pathway (Reliability: 3)
A2QZS1_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
569
0
62928
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6J8CSL2_MYTCO
479
0
53359
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Z5K233_FISSO
563
1
64130
TrEMBL
other Location (Reliability: 3)
A0A1Z5KH93_FISSO
552
1
61117
TrEMBL
other Location (Reliability: 4)
A0A1Z5KTU3_FISSO
526
0
59466
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6RLY2_ROSCH
489
1
55063
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B2SBP9_GLYSO
512
1
57781
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Z5KJ47_FISSO
564
0
63951
TrEMBL
other Location (Reliability: 3)
A0A0D2NTH6_9CHLO
498
0
53788
TrEMBL
other Location (Reliability: 2)
A0A0B2SBJ9_GLYSO
492
1
55794
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1Z5KKS1_FISSO
565
1
64267
TrEMBL
other Location (Reliability: 4)
A0A1Z5JCR6_FISSO
557
1
63121
TrEMBL
Secretory Pathway (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
120000
130000
150000
-
enzyme from kidney cortex, in complex with adenosine deaminase, gel filtration
200000
54000
55000
58000
60000
98000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
trimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
2 h, 30% loss of activity without a stabilizer. 10% loss of activity after 4 h in presence of 1 mg/ml bovine serum albumin or 0.1% Tween 20
50
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in presence of stabilizing agents, the enzyme tolerates at least five subsequent freeze/thaw cycles
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, 20 mM sodium phosphate-buffered saline, pH 8.0, stable for at least several months
-
4°C, -20°C, or -80°C, purified enzyme is stable for at least 4 months in presence of 1 mg/ml bovine serum albumin
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with adenosine deaminase or dipeptidyl peptidase IV, DEAE cellulose column chromatography, DEAE-Sephadex A-50 gel filtration, Sephadex G-25 gel filtration, and Sephadex G-200 gel filtration
-
purification scheme includes an inhibitor-based affinity chromatographic step
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, sequence contains a leucine zipper motif
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is a potential urinary marker for the biochemical detection of kidney damage
medicine
-
mRNA expression in ipsilateral and contralateral cortices. Dipeptidyl peptidase II and aminopeptidase N are up-regulated ipsilaterally from 6 h to 7 days post ischemia. IPC1755, a non-selective protease inhibitor, reveals a significant reduction of cortical lesions after transient cerebral ischemia
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mantle, D.
Characterization of dipeptidyl and tripeptidyl aminopeptidases in human kidney soluble fraction
Clin. Chim. Acta
196
135-142
1991
Homo sapiens
brenda
Chan, S.A.T.; Toursarkissian, K.; Sweeny, J.P.; Jones, T.H.D.
Dipeptidyl-aminopeptidases and aminopeptidases in Dictyostelium discoideum
Biochem. Biophys. Res. Commun.
127
962-968
1985
Dictyostelium discoideum
brenda
Alba, F.; Arenas, J.C.; Lopez, M.A.
Properties of rat brain dipeptidyl aminopeptidases in the presence of detergents
Peptides
16
325-329
1995
Rattus norvegicus
brenda
Lynn, K.R.
The isolation and some properties of dipeptidyl peptidases II and III from porcine spleen
Int. J. Biochem.
23
47-50
1991
Sus scrofa
brenda
MacFarlane, S.; MacFarlane, G.T.
Formation of a dipeptidyl arylamidase by Bacteroides splanchnicus NCTC 10825 with specificities towards glycylprolyl-x and valylalanine-x substrates
J. Med. Microbiol.
46
547-555
1997
Odoribacter splanchnicus
brenda
Mentlein, R.; Struckhoff, G.
Purification of two dipeptidyl aminopeptidases II from rat brain and their action on proline-containing neuropeptides
J. Neurochem.
52
1284-1293
1989
Rattus norvegicus
brenda
Sakai, T.; Kojima, K.
Rapid chromatographic purification of dipeptidyl-aminopeptidase II from human kidney
J. Chromatogr.
416
131-137
1987
Homo sapiens
brenda
DiCarlantonio, G.; Talbot, P.; Dudenhausen, E.
Partial purification and characterization of dipeptidyl peptidase II (DPP II) from guinea pig testes
Gamete Res.
15
161-175
1986
Cavia porcellus
-
brenda
Eisenhauer, D.A.; McDonald, J.K.
A novel dipeptidyl peptidase II from the porcine ovary. Purification and characterization of a lysosomal serine protease showing enhanced specificity for prolyl bonds
J. Biol. Chem.
261
8859-8865
1986
Sus scrofa
brenda
Struckhoff, G.; Heymann, E.
Rat peritoneal mast cells release dipeptidyl peptidase II
Biochem. J.
236
215-219
1986
Rattus norvegicus
brenda
McDonald, J.K.; Eisenhauer, D.A.; Hoisington, A.R.
Complementary specificities of ovarian dipeptidyl peptidase II and tripeptidyl peptidase: collagenolytic potential and increased activity associated with ovulation in the hog
Prog. Clin. Biol. Res.
180
673-675
1985
Sus scrofa
brenda
Nagatsu, T.; Sakai, T.; Kojima, K.; Araki, E.; Sakakibara, S.; Fukasawa, K.; Harada, M.
A sensitive and specific assay for dipeptidyl-aminopeptidase II in serum and tissues by liquid chromatography-fluorometry
Anal. Biochem.
147
80-85
1985
Homo sapiens
brenda
Fukasawa, K.; Fukasawa, K.M.; Hiraoka, B.Y.; Harada, M.
Purification and properties of dipeptidyl peptidase II from rat kidney
Biochim. Biophys. Acta
745
6-11
1983
Rattus norvegicus
brenda
McDonald, J.K.; Schwabe, C.
Dipeptidyl peptidase II of bovine dental pulp. Initial demonstration and characterization as a fibroblastic, lysosomal peptidase of the serine class active on collagen-related peptides
Biochim. Biophys. Acta
616
68-81
1980
Bos taurus
brenda
Gossrau, R.; Lojda, Z.
Study on dipeptidylpeptidase II (DPP II)
Histochemistry
70
53-76
1980
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
McDonald, J.K.; Reilly, T.J.; Zeitman, B.B.; Ellis, S.
Dipeptidyl arylamidase II of the pituitary. Properties of lysylalanyl-beta-naphthylamide hydrolysis: inhibition by cations, distribution in tissues, and subcellular localization
J. Biol. Chem.
243
2028-2037
1968
Bos taurus, Rattus norvegicus
brenda
McDonald, J.K.; Leibach, F.H.; Grindeland, R.E.; Ellis, S.
Purification of dipeptidyl aminopeptidase II (dipeptidyl arylamidase II) of the anterior pituitary gland
J. Biol. Chem.
243
4143-4150
1968
Bos taurus
brenda
Sannes, P.L.
Subcellular localization of dipeptidyl peptidases II and IV in rat and rabbit alveolar macrophages
J. Histochem. Cytochem.
31
684-690
1983
Oryctolagus cuniculus, Rattus norvegicus
brenda
Huang, K.; Takagaki, M.; Kani, K.; Ohkubo, I.
Dipeptidyl peptidase II from porcine seminal plasma: purification, characterization, and its homology to granzymes, cytosolic cell proteinases (CCP 1-4)
Biochim. Biophys. Acta
1290
149-156
1996
Sus scrofa
brenda
Murao, S.; Kitade, T.; Oyama, H.; Shin, T.
Isolation and characterization of a dipeptidyl aminopeptidase from Streptomyces sp. WM-23
Biosci. Biotechnol. Biochem.
58
1545-1546
1994
Streptomyces sp., Streptomyces sp. WM-23
brenda
Gorthy, W.C.; Steward, D.E.; McDonald, J.K.
Localization of the lysosomal protease dipeptidyl peptidase II in the young normal rat lens: a correlative light and electron microscopic analysis
Curr. Eye Res.
11
531-542
1992
Rattus norvegicus
brenda
Leiting, B.; Pryor, K.D.; Wu, J.K.; Marsilio, F.; Patel, R.A.; Craik, C.S.; Ellman, J.A.; Cummings, R.T.; Thornberry, N.A.
Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
Biochem. J.
371
525-532
2003
Homo sapiens (Q9UHL4), Homo sapiens
brenda
Stoeckel-Maschek, A.; Mrestani-Klaus, C.; Stiebitz, B.; Demuth, H.U.; Neubert, K.
Thioxo amino acid pyrrolidides and thiazolidides: new inhibitors of proline specific peptidases
Biochim. Biophys. Acta
1479
15-31
2000
Homo sapiens, Sus scrofa
brenda
Dikov, A.; Dimitrova, M.; Pajpanova, T.; Krieg, R.; Halbhuber, K.J.
Histochemical method for dipeptidyl aminopeptidase II with a new anthraquinonyl hydrazide substrate
Cell. Mol. Biol.
46
1213-1218
2000
Rattus norvegicus
brenda
Araki, H.; Li, Y.; Yamamoto, Y.; Haneda, M.; Nishi, K.; Kikkawa, R.; Ohkubo, I.
Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase
J. Biochem.
129
279-288
2001
Rattus norvegicus
brenda
Sohar, N.; Sohar, I.; Hammer, H.
Lysosomal enzyme activities: new potential markers for Sjoegrens syndrome
Clin. Biochem.
38
1120-1126
2005
Homo sapiens
brenda
Maes, M.B.; Lambeir, A.M.; Gilany, K.; Senten, K.; Van der Veken, P.; Leiting, B.; Augustyns, K.; Scharpe, S.; De Meester, I.
Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7)
Biochem. J.
386
315-324
2005
Homo sapiens (Q9UHL4), Homo sapiens
brenda
Maes, M.B.; Martinet, W.; Schrijvers, D.M.; Van der Veken, P.; De Meyer, G.R.; Augustyns, K.; Lambeir, A.M.; Scharpe, S.; De Meester, I.
Dipeptidyl peptidase II and leukocyte cell death
Biochem. Pharmacol.
72
70-79
2006
Homo sapiens
brenda
Senten, K.; van der Veken, P.; De Meester, I.; Lambeir, A.M.; Scharpe, S.; Haemers, A.; Augustyns, K.
gamma-Amino-substituted analogues of 1-[(S)-2,4-diaminobutanoyl]piperidine as highly potent and selective dipeptidyl peptidase II inhibitors
J. Med. Chem.
47
2906-2916
2004
Homo sapiens
brenda
Van der Veken, P.; Senten, K.; Kertesz, I.; De Meester, I.; Lambeir, A.M.; Maes, M.B.; Scharpe, S.; Haemers, A.; Augustyns, K.
Fluoro-olefins as peptidomimetic inhibitors of dipeptidyl peptidases
J. Med. Chem.
48
1768-1780
2005
Homo sapiens
brenda
Danilova, O.; Li, B.; Szardenings, A.K.; Huber, B.T.; Rosenblum, J.S.
Synthesis and activity of a potent, specific azabicyclo[3.3.0]-octane-based DPP II inhibitor
Bioorg. Med. Chem. Lett.
17
507-510
2007
Homo sapiens
brenda
Chen, D.; Kennedy, A.; Wang, J.Y.; Zeng, W.; Zhao, Q.; Pearl, M.; Zhang, M.; Suo, Z.; Nesland, J.M.; Qiao, Y.; Ng, A.K.; Hirashima, N.; Yamane, T.; Mori, Y.; Mitsumata, M.; Ghersi, G.; Chen, W.T.
Activation of EDTA-resistant gelatinases in malignant human tumors
Cancer Res.
66
9977-9985
2006
Homo sapiens
brenda
Maes, M.B.; Scharpe, S.; De Meester, I.
Dipeptidyl peptidase II (DPPII), a review
Clin. Chim. Acta
380
31-49
2007
Bos taurus, Rattus norvegicus, Sus scrofa, Homo sapiens (Q9UHL4)
brenda
Van der Veken, P.; Haemers, A.; Augustyns, K.
Prolyl peptidases related to dipeptidyl peptidase IV: potential of specific inhibitors in drug discovery
Curr. Top. Med. Chem.
7
621-635
2007
Homo sapiens
brenda
Sentandreu, M.A.; Toldra, F.
Oligopeptides hydrolysed by muscle dipeptidyl peptidases can generate angiotensin-I converting enzyme inhibitory dipeptides
Eur. Food Res. Technol.
224
785-790
2007
Homo sapiens
brenda
Sentandreu, M.A.; Toldra, F.
Evaluation of ACE inhibitory activity of dipeptides generated by the action of porcine muscle dipeptidyl peptidases
Food Chem.
102
511-515
2007
Sus scrofa
brenda
Sharoyan, S.G.; Antonyan, A.A.; Mardanyan, S.S.; Lupidi, G.; Cuccioloni, M.; Angeletti, M.; Cristalli, G.
Complex of dipeptidyl peptidase II with adenosine deaminase
Biochemistry
73
943-949
2008
Bos taurus
brenda
Tye, C.E.; Lorenz, R.L.; Bartlett, J.D.
Lysosomal protease expression in mature enamel
Cells Tissues Organs
189
111-114
2009
Mus musculus
brenda
Bista, P.; Mele, D.A.; Baez, D.V.; Huber, B.T.
Lymphocyte quiescence factor Dpp2 is transcriptionally activated by KLF2 and TOB1
Mol. Immunol.
45
3618-3623
2008
Homo sapiens, Mus musculus
brenda
Rhnert, P.; Schmidt, W.; Emmerlich, P.; Goihl, A.; Wrenger, S.; Bank, U.; Nordhoff, K.; Tger, M.; Ansorge, S.; Reinhold, D.; Striggow, F.
Dipeptidyl peptidase IV, aminopeptidase N and DPIV/APN-like proteases in cerebral ischemia
J. Neuroinflammation
9
44
2012
Rattus norvegicus
brenda
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