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Ala-Ala-p-nitroanilide + H2O
Ala-Ala + p-nitroaniline
-
-
-
?
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
Asp-Pro-p-nitroanilide + H2O
Asp-Pro + p-nitroaniline
carnosine + H2O
?
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
lactate + L-isoleucine
N-L-lactoyl-L-isoleucine + H2O
-
-
-
?
lactate + L-phenylalanine
N-L-lactoyl-L-phenylalanine + H2O
-
-
-
?
lactate + L-tryptophan
N-L-lactoyl-L-tryptophan + H2O
-
-
-
?
lactate + L-tyrosine
N-L-lactoyl-L-tyrosine + H2O
-
-
-
?
Leu-Pro-p-nitroanilide + H2O
Leu-Pro + p-nitroaniline
-
-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
-
-
-
-
?
Met-Pro-p-nitroanilide + H2O
Met-Pro + p-nitroaniline
-
-
-
-
?
Pro-Asp + H2O
Pro + Asp
-
-
-
-
?
Pro-Glu + H2O
Pro + Glu
-
-
-
-
?
Pro-Ile + H2O
Pro + Ile
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
?
Pro-Ser + H2O
Pro + Ser
-
-
-
-
?
Ser-Pro-p-nitroanilide + H2O
Ser-Pro + p-nitroaniline
-
-
-
-
?
additional information
?
-
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
-
-
-
?
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
-
-
-
-
?
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
-
-
-
?
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
-
-
-
-
?
Asp-Pro-p-nitroanilide + H2O
Asp-Pro + p-nitroaniline
-
-
-
?
Asp-Pro-p-nitroanilide + H2O
Asp-Pro + p-nitroaniline
-
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Pro-Ala + H2O
Pro + Ala
-
-
-
?
Pro-Ala + H2O
Pro + Ala
-
-
-
?
Pro-Ala + H2O
Pro + Ala
-
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
-
?
Pro-Met + H2O
Pro + Met
-
-
-
?
Pro-Met + H2O
Pro + Met
-
-
-
-
?
Pro-Val + H2O
Pro + Val
-
-
-
?
Pro-Val + H2O
Pro + Val
-
-
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
not: Gly-Pro
-
-
?
additional information
?
-
-
not: Gly-Pro
-
-
?
additional information
?
-
-
DPP8-v3 may play a key role in the immunoregulation of testes and accordingly may influence spermatogenesis and male fertility
-
-
?
additional information
?
-
-
the enzyme catalyzes cleavage at the carboxyl side of the proline residue at the penultimate position
-
-
?
additional information
?
-
CNDP2 catalyzes the formation of N-lactoyl-amino acids. The plasma levels of of N-lactoyl-amino acids strongly correlate with plasma levels of lactate and amino acids
-
-
?
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(1S)-1-cyclohexyl-2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethanamine
-
IC50: 24 nM
(1S)-1-cyclohexyl-2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethanamine
-
IC50: 3016 nM
(1S)-1-cyclohexyl-2-oxo-2-piperidin-1-ylethanamine
-
IC50: 1448 nM
(1S)-1-cyclohexyl-2-oxo-2-pyrrolidin-1-ylethanamine
-
IC50: 78 nM
(2S)-1-[(2S)-2-amino-4-(3,4-dihydroisoquinolin-2(1H)-yl)-4-oxobutanoyl]pyrrolidine-2-carbonitrile
-
IC50: 19 nM
(2S)-1-[(2S)-2-amino-4-(4-[bis(4-fluorophenyl)methyl]piperazin-1-yl)-4-oxobutanoyl]pyrrolidine-2-carbonitrile
-
IC50: 16 nM
(2S)-2-amino-2-cyclohexyl-1-[(2R)-2-(iminomethyl)cyclopentyl]ethanone
-
IC50: 27 nM
(2S,3S)-3-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)pentan-2-amine
-
IC50: 364 nM
1-(1,3-dihydro-2H-isoindol-2-yl)-4-(3,4-dihydroisoquinolin-2(1H)-yl)-1,4-dioxobutan-2-amine
-
IC50: 555 nM
1-(1,3-dihydro-2H-isoindol-2-yl)-4-(6,7-dimethoxy-3,4-dihydroisoquinolin-2(1H)-yl)-1,4-dioxobutan-2-amine
-
IC50: 150 nM
4-(4-[bis(4-fluorophenyl)methyl]piperazin-1-yl)-1-(1,3-dihydro-2H-isoindol-2-yl)-1,4-dioxobutan-2-amine
-
IC50: 14 nM
6-([2-({2-[(2S)-2-cyanopyrrolidin-1-yl]-2-oxoethyl}amino)ethyl]amino)nicotinonitrile
-
IC50: 4574 nM
Carnosinase substrates
-
-
-
DL-homocysteine
-
strong inhibition at 10 and 50 mM, in the presence of 0.1 mM MnCl2
DL-methionine
-
strong inhibition at 10 and 50 mM, in the presence of 0.1 mM MnCl2
L-leucine
-
strong inhibition of prolinase activity against Pro-Gly regardless wether MnCl2 is present or not
L-methionine
-
inhibition at 10 and 50 mM, in the presence of 0.1 mM MnCl2
L-Val
-
strong inhibition of prolinase activity against Pro-Gly regardless wether MnCl2 is present or not
N-acetyl-L-methionine
-
strong inhibition at 10 and 50 mM, in the presence of 0.1 mM MnCl2
NVP LAF237
-
i.e.vildagliptin, IC50: 14219 nM
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Zn2+
-
inhibits, but activation in phosphate buffer
Mn2+
-
-
Mn2+
-
0.1 mM, inhibits prolinase activity in normal erythrocytes against Pro-Ala, Pro-Val, Pro-Met, Pro-Asp
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Adenocarcinoma
Prolidase and prolinase activities in moderately and poorly differentiated lung adenocarcinoma.
Adenocarcinoma of Lung
Prolidase and prolinase activities in moderately and poorly differentiated lung adenocarcinoma.
Carcinoma
Quantitative proteomics approach to screening of potential diagnostic and therapeutic targets for laryngeal carcinoma.
Carcinoma, Hepatocellular
Effect of ethanol on prolidase I and prolinase activity in the human hepatoma cell line Hep G2.
Carcinoma, Hepatocellular
Identification of carboxypeptidase of glutamate like-B as a candidate suppressor in cell growth and metastasis in human hepatocellular carcinoma.
Colonic Neoplasms
Up-regulation of CNDP2 facilitates the proliferation of colon cancer.
Diabetes Mellitus, Type 1
Exclusion of polymorphisms in carnosinase genes (CNDP1 & CNDP2) as cause of diabetic nephropathy in type 1 diabetes mellitus. Results of large case - control and follow - up studies.
Diabetes Mellitus, Type 2
Common variants in CNDP1 and CNDP2, and risk of nephropathy in type 2 diabetes.
Diabetic Nephropathies
Common variants in CNDP1 and CNDP2, and risk of nephropathy in type 2 diabetes.
Diabetic Nephropathies
Exclusion of polymorphisms in carnosinase genes (CNDP1 & CNDP2) as cause of diabetic nephropathy in type 1 diabetes mellitus. Results of large case - control and follow - up studies.
Diabetic Nephropathies
Exclusion of polymorphisms in carnosinase genes (CNDP1 and CNDP2) as a cause of diabetic nephropathy in type 1 diabetes: results of large case-control and follow-up studies.
Diabetic Nephropathies
The influence of carnosinase gene polymorphisms on diabetic nephropathy risk in African-Americans.
Fibrosarcoma
Activity of lysosomal and nonlysosomal proteases of fibrosarcoma induced by methylcholanthrene.
Hepatitis, Chronic
Determination of prolinase activity in plasma. Application to liver disease and its relation with prolidase activity.
Infections
Changes in the intestinal enzyme activity of lambs during chronic infection with Trichostrongylus vitrinus.
Liver Diseases
Determination of prolinase activity in plasma. Application to liver disease and its relation with prolidase activity.
Liver Diseases, Alcoholic
Plasma prolidase and prolinase activity in alcoholic liver disease.
Neoplasm Metastasis
CNDP2 Acts as an Activator for Human Ovarian Cancer Growth and Metastasis via the PI3K/AKT Pathway.
Neoplasm Metastasis
Identification of carboxypeptidase of glutamate like-B as a candidate suppressor in cell growth and metastasis in human hepatocellular carcinoma.
Neoplasm Metastasis
Quantitative proteomics approach to screening of potential diagnostic and therapeutic targets for laryngeal carcinoma.
Neoplasms
A toolset to study functions of Cytosolic non-specific dipeptidase 2 (CNDP2) using Drosophila as a model organism.
Neoplasms
Activity of lysosomal and nonlysosomal proteases and contents of protein and its degradation products in the blood serum of rats with fibrosarcoma induced by methylcholanthrene.
Neoplasms
Identification of carboxypeptidase of glutamate like-B as a candidate suppressor in cell growth and metastasis in human hepatocellular carcinoma.
Neoplasms
Underexpressed CNDP2 participates in gastric cancer growth inhibition through activating the MAPK signaling pathway.
Obesity
The Combined Effects of Genetic Variation in the CNDP1 and CNDP2 Genes and Dietary Carbohydrate and Carotene Intake on Obesity Risk.
Ovarian Neoplasms
CNDP2 Acts as an Activator for Human Ovarian Cancer Growth and Metastasis via the PI3K/AKT Pathway.
Parkinson Disease
Proteomic profiling of the substantia nigra demonstrates CNDP2 overexpression in Parkinson's disease.
Prolidase Deficiency
Biochemical investigations on prolidase and prolinase in erythrocytes from patients with prolidase deficiency.
Prolidase Deficiency
Characteristics and partial purification of prolidase and prolinase from leukocytes of a normal human and a patient with prolidase deficiency.
Prolidase Deficiency
Characteristics of prolinase against various iminodipeptides in erythrocyte lysates from a normal human and a patient with prolidase deficiency.
Prolidase Deficiency
Plasma prolidase and prolinase activity in prolidase deficiency.
Prolidase Deficiency
Prolinase activity in prolidase-deficient fibroblasts.
Stomach Neoplasms
Underexpressed CNDP2 participates in gastric cancer growth inhibition through activating the MAPK signaling pathway.
Uremia
Prolidase and prolinase activities in the erythrocytes of patients with chronic uremia.
xaa-pro dipeptidase deficiency
Biochemical investigations on prolidase and prolinase in erythrocytes from patients with prolidase deficiency.
xaa-pro dipeptidase deficiency
Characteristics and partial purification of prolidase and prolinase from leukocytes of a normal human and a patient with prolidase deficiency.
xaa-pro dipeptidase deficiency
Characteristics of prolinase against various iminodipeptides in erythrocyte lysates from a normal human and a patient with prolidase deficiency.
xaa-pro dipeptidase deficiency
Plasma prolidase and prolinase activity in prolidase deficiency.
xaa-pro dipeptidase deficiency
Prolinase activity in prolidase-deficient fibroblasts.
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1.42
Ala-Ala-p-nitroanilide
-
-
0.12 - 2.72
Ala-Pro-p-nitroanilide
0.027 - 1.673
Arg-Pro-p-nitroanilide
2.05 - 2.668
Asp-Pro-p-nitroanilide
0.79
Gly-Leu
-
at pH 8.0 and 9.2
0.48 - 4.599
Gly-Pro-p-nitroanilide
0.023 - 0.39
Leu-Pro-p-nitroanilide
0.016 - 1.358
Lys-Pro-p-nitroanilide
0.029 - 0.988
Met-Pro-p-nitroanilide
0.47
Pro-Ala
-
at pH 8.0 and 9.2
0.238 - 7.462
Ser-Pro-p-nitroanilide
0.12
Ala-Pro-p-nitroanilide
-
-
0.127
Ala-Pro-p-nitroanilide
-
wild type enzyme
1.495
Ala-Pro-p-nitroanilide
-
mutant enzyme F822A
2.219
Ala-Pro-p-nitroanilide
-
mutant enzyme V833A
2.397
Ala-Pro-p-nitroanilide
-
mutant enzyme Y844A
2.72
Ala-Pro-p-nitroanilide
-
mutant enzyme H859A
0.027
Arg-Pro-p-nitroanilide
-
wild type enzyme
0.27
Arg-Pro-p-nitroanilide
-
mutant enzyme H859A
0.31
Arg-Pro-p-nitroanilide
-
-
1.673
Arg-Pro-p-nitroanilide
-
mutant enzyme F822A
2.05
Asp-Pro-p-nitroanilide
-
-
2.668
Asp-Pro-p-nitroanilide
-
wild type enzyme
0.48
Gly-Pro-p-nitroanilide
-
-
0.528
Gly-Pro-p-nitroanilide
-
wild type enzyme
2.731
Gly-Pro-p-nitroanilide
-
mutant enzyme H859A
4.599
Gly-Pro-p-nitroanilide
-
mutant enzyme F822A
0.023
Leu-Pro-p-nitroanilide
-
wild type enzyme
0.348
Leu-Pro-p-nitroanilide
-
mutant enzyme H859A
0.39
Leu-Pro-p-nitroanilide
-
mutant enzyme F822A
0.016
Lys-Pro-p-nitroanilide
-
wild type enzyme
0.507
Lys-Pro-p-nitroanilide
-
mutant enzyme H859A
1.358
Lys-Pro-p-nitroanilide
-
mutant enzyme F822A
0.029
Met-Pro-p-nitroanilide
-
wild type enzyme
0.325
Met-Pro-p-nitroanilide
-
mutant enzyme H859A
0.988
Met-Pro-p-nitroanilide
-
mutant enzyme F822A
6.8
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from healthy patients, activated by 0.1 mM MnCl2 and 20 mM Gly
8.6
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2 and 20 mM Gly
9.7
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2
13.2
Pro-Gly
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C
13.2
Pro-Gly
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 10 mM L-methionine
13.8
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from healthy patients, activated by 0.1 mM MnCl2
15.1
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from healthy patients, activated by 20 mM Gly
15.85
Pro-Gly
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 50 mM L-methionine
16.7
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 20 mM Gly
18.2
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, without activating compound
23.57
Pro-Gly
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 10 mM D,L-homocysteine
26.9
Pro-Gly
-
pH 7.8, 37°, erythrocyte lysate from healthy patients, without activating compound
56.33
Pro-Gly
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 50 mM D,L-homocysteine
4.2
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 20 mM Gly
5
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2 and 20 mM Gly
8.1
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, without activating compound
8.35
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from healthy patients, activated by 20 mM Gly
9.7
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2
9.9
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from healthy patients, activated by 0.1 mM MnCl2 and 20 mM Gly
11.81
Pro-Met
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C
13.24
Pro-Met
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 10 mM L-methionine
15.58
Pro-Met
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 50 mM L-methionine
17.6
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from healthy patients, without activating compound
19.1
Pro-Met
-
pH 7.8, 37°C, erythrocyte lysate from healthy patients, activated by 0.1 mM MnCl2
22.3
Pro-Met
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 10 mM D,L-homocysteine
46.78
Pro-Met
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 50 mM D,L-homocysteine
3.2
Pro-Val
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 20 mM Gly
5.5
Pro-Val
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2 and 20 mM Gly
7.9
Pro-Val
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, without activating compound
10.1
Pro-Val
-
pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2
14.7
Pro-Val
-
pH 7.8, 37°C, erythrocxyte lysate from healthy patients, activated by 20 mM Gly
17.3
Pro-Val
-
pH 7.8, 37°C, erythrocyte lysate from healthy patients, activated by 0.1 mM MnCl2 and 20 mM Gly
19.1
Pro-Val
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C
19.54
Pro-Val
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 10 mM L-methionine
24.69
Pro-Val
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 50 mM L-methionine
26
Pro-Val
-
pH 7.8, 37°C, erythrocyte lysate from healthy patients, without activating compound
28.6
Pro-Val
-
pH 7.8, 37°C, erythrocxyte lysate from healthy patients, activated by 0.1 mM MnCl2
45.6
Pro-Val
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 10 mM D,L-homocysteine
75.2
Pro-Val
-
in 50 mM Tris-HCl buffer (pH 7.8) with 2 mM or 20 mM MnCl2, at 37°C, in the presence of 50 mM D,L-homocysteine
0.238
Ser-Pro-p-nitroanilide
-
wild type enzyme
2.249
Ser-Pro-p-nitroanilide
-
mutant enzyme F822A
7.462
Ser-Pro-p-nitroanilide
-
mutant enzyme H859A
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0.000024
(1S)-1-cyclohexyl-2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethanamine
Homo sapiens
-
IC50: 24 nM
0.003016
(1S)-1-cyclohexyl-2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethanamine
Homo sapiens
-
IC50: 3016 nM
0.001448
(1S)-1-cyclohexyl-2-oxo-2-piperidin-1-ylethanamine
Homo sapiens
-
IC50: 1448 nM
0.000078
(1S)-1-cyclohexyl-2-oxo-2-pyrrolidin-1-ylethanamine
Homo sapiens
-
IC50: 78 nM
0.000019
(2S)-1-[(2S)-2-amino-4-(3,4-dihydroisoquinolin-2(1H)-yl)-4-oxobutanoyl]pyrrolidine-2-carbonitrile
Homo sapiens
-
IC50: 19 nM
0.000016
(2S)-1-[(2S)-2-amino-4-(4-[bis(4-fluorophenyl)methyl]piperazin-1-yl)-4-oxobutanoyl]pyrrolidine-2-carbonitrile
Homo sapiens
-
IC50: 16 nM
0.000027
(2S)-2-amino-2-cyclohexyl-1-[(2R)-2-(iminomethyl)cyclopentyl]ethanone
Homo sapiens
-
IC50: 27 nM
0.000364
(2S,3S)-3-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)pentan-2-amine
Homo sapiens
-
IC50: 364 nM
0.000555
1-(1,3-dihydro-2H-isoindol-2-yl)-4-(3,4-dihydroisoquinolin-2(1H)-yl)-1,4-dioxobutan-2-amine
Homo sapiens
-
IC50: 555 nM
0.00015
1-(1,3-dihydro-2H-isoindol-2-yl)-4-(6,7-dimethoxy-3,4-dihydroisoquinolin-2(1H)-yl)-1,4-dioxobutan-2-amine
Homo sapiens
-
IC50: 150 nM
0.000014
4-(4-[bis(4-fluorophenyl)methyl]piperazin-1-yl)-1-(1,3-dihydro-2H-isoindol-2-yl)-1,4-dioxobutan-2-amine
Homo sapiens
-
IC50: 14 nM
0.004574
6-([2-({2-[(2S)-2-cyanopyrrolidin-1-yl]-2-oxoethyl}amino)ethyl]amino)nicotinonitrile
Homo sapiens
-
IC50: 4574 nM
0.014219
NVP LAF237
Homo sapiens
-
i.e.vildagliptin, IC50: 14219 nM
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Masuda, S.; Watanabe, H.; Morioka, M.; Fujita, Y.; Ageta, T.; Kodama, H.
Characteristics of partially purified prolidase and prolinase from the human prostate
Acta Med. Okayama
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1994
Homo sapiens
brenda
Lenney, J.F.
Human cytosolic carnosinase: evidence of identity with prolinase, a non-specific dipeptidase
Biol. Chem. Hoppe-Seyler
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1990
Homo sapiens
brenda
Priestman, D.A.; Butterworth, J.
Prolinase and non-specific dipeptidase of human kidney
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1985
Homo sapiens
brenda
Myara, I.; Brosset, M.; Lemonnier, A.
Tissue distribution of prolidase and prolinase activity in man and rat
Med. Sci. Res.
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1987
Homo sapiens, Rattus norvegicus
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brenda
Gruendig, C.A.; Hanson, H.
Partial purification and properties of glycyl-L-leucine hydrolase (EC 3.4.3.2) from human milk
Hoppe-Seyler's Z. Physiol. Chem.
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487-500
1973
Homo sapiens
brenda
Karim, A.; Kelley, G.J.C.; Murphy, R.F.; Elmore, D.T.; Bridges, J.M.
Development of a radiochemical assay for glycyl-leucine dipeptidase in human B- and T-lymphocytes
Biochem. Soc. Trans.
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1980
Homo sapiens
brenda
Mikasa, H.; Sasaki, K.
Simultaneous measurement of prolidase and prolinase acitvities in erythrocytes using an isotachophoretic analyser
J. Chromatogr.
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1985
Homo sapiens
brenda
Gacko, M.; Palka, J.; Worowska, A.; Glowinski, S.
Activity of prolidase and prolinase in the wall of aortic aneurysm
Bull. Pol. Acad. Sci. Biol. Sci.
46
103-106
1998
Homo sapiens
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brenda
Myara, I.; Cosson, C.; Pourci, M.L.; Moatti, N.; Lemmonier, A.
Effect of ethanol on prolidase I and prolinase activity in the human hepatoma cell line Hep G2
Clin. Chim. Acta
219
195-197
1993
Homo sapiens
brenda
Chen, Y.S.; Chien, C.H.; Goparaju, C.M.; Hsu, J.T.; Liang, P.H.; Chen, X.
Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells
Protein Expr. Purif.
35
142-146
2004
Homo sapiens
brenda
Zhu, H.; Zhou, Z.M.; Lu, L.; Xu, M.; Wang, H.; Li, J.M.; Sha, J.H.
Expression of a novel dipeptidyl peptidase 8 (DPP8) transcript variant, DPP8-v3, in human testis
Asian J. Androl.
7
245-255
2005
Homo sapiens
brenda
Jiaang, W.T.; Chen, Y.S.; Hsu, T.; Wu, S.H.; Chien, C.H.; Chang, C.N.; Chang, S.P.; Lee, S.J.; Chen, X.
Novel isoindoline compounds for potent and selective inhibition of prolyl dipeptidase DPP8
Bioorg. Med. Chem. Lett.
15
687-691
2005
Homo sapiens
brenda
Wang, W.; Liu, G.; Yamashita, K.; Manabe, M.; Kodama, H.
Characteristics of prolinase against various iminodipeptides in erythrocyte lysates from a normal human and a patient with prolidase deficiency
Clin. Chem. Lab. Med.
42
1102-1108
2004
Homo sapiens
brenda
Zhang, P.; Chan, D.W.; Zhu, Y.; Li, J.J.; Ng, I.O.; Wan, D.; Gu, J.
Identification of carboxypeptidase of glutamate like-B as a candidate suppressor in cell growth and metastasis in human hepatocellular carcinoma
Clin. Cancer Res.
12
6617-6625
2006
Homo sapiens (Q96KP4), Homo sapiens
brenda
Uramatsu, M.; Liu, G.; Uramatsu, S.; Zhang, M.; Wang, W.; Nakayama, K.; Manabe, M.; Kodama, H.
Different effects of sulfur amino acids on prolidase and prolinase activity in normal and prolidase-deficient human erythrocytes
Clin. Chim. Acta
375
129-135
2007
Homo sapiens
brenda
Lee, H.J.; Chen, Y.S.; Chou, C.Y.; Chien, C.H.; Lin, C.H.; Chang, G.G.; Chen, X.
Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8
J. Biol. Chem.
281
38653-38662
2006
Homo sapiens
brenda
Jansen, R.S.; Addie, R.; Merkx, R.; Fish, A.; Mahakena, S.; Bleijerveld, O.B.; Altelaar, M.; IJlst, L.; Wanders, R.J.; Borst, P.; van de Wetering, K.
N-lactoyl-amino acids are ubiquitous metabolites that originate from CNDP2-mediated reverse proteolysis of lactate and amino acids
Proc. Natl. Acad. Sci. USA
112
6601-6606
2015
Homo sapiens (Q96KP4)
brenda