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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
beta-Ala-L-His + H2O
beta-Ala + L-His
D-Leu-Gly + H2O
D-Leu + Gly
Gly-His + H2O
Gly + His
-
-
-
?
Gly-L-Ala + H2O
Gly + L-Ala
-
-
-
-
?
Gly-L-Asn + H2O
Gly + L-Asn
-
-
-
-
?
Gly-L-Lys + H2O
Gly + L-Lys
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
Gly-Tyr + H2O
Gly + Tyr
-
-
-
?
His-Ala + H2O
His + Ala
-
-
-
?
Hyp-Gly + H2O
Hyp + Gly
-
-
-
?
L-Ala-4-methylcoumarin 7-amide + H2O
L-Ala + 7-amino-4-methylcoumarin
L-Ala-Gly + H2O
L-Ala + Gly
L-Ala-L-Ser + H2O
L-Ala + L-Ser
-
-
-
?
L-Leu-L-Phe + H2O
L-Leu + L-Phe
-
-
-
-
?
L-Lys-4-methylcoumarin 7-amide + H2O
L-Lys + 7-amino-4-methylcoumarin
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-Arg + H2O
Leu + Arg
-
-
-
?
Leu-Leu-Leu + H2O
?
-
-
-
-
?
Leu-Pro-p-nitroanilide + H2O
Leu-Pro + p-nitroaniline
-
-
-
-
?
Leu-Ser + H2O
Leu + Ser
-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
-
-
-
-
?
Met-Glu + H2O
Met + Glu
-
-
-
?
Met-Gly + H2O
Met + Gly
-
-
-
?
Met-Phe + H2O
Met + Phe
-
-
-
?
Met-Pro-p-nitroanilide + H2O
Met-Pro + p-nitroaniline
-
-
-
-
?
N-(3,5-dicarboxy-4-methyl-2-pyrrolcarbonyl)glycine + H2O
?
-
-
-
-
?
Phe-Leu + H2O
Phe + Leu
-
-
-
?
Phe-Met + H2O
Phe + Met
-
-
-
?
Pro-Asp + H2O
Pro + Asp
-
-
-
-
?
Pro-Glu + H2O
Pro + Glu
-
-
-
-
?
Pro-Ile + H2O
Pro + Ile
-
-
-
?
Pro-Leu-NH2 + H2O
Pro + Leu-NH2
-
-
-
?
Pro-Lys + H2O
Pro + Lys
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
?
Pro-Ser + H2O
Pro + Ser
-
-
-
-
?
Ser-Phe + H2O
Ser + Phe
-
-
-
?
Ser-Pro-p-nitroanilide + H2O
Ser-Pro + p-nitroaniline
-
-
-
-
?
Thr-Leu + H2O
Thr + Leu
-
-
-
?
additional information
?
-
Ala-Ala + H2O
Ala + Ala
-
-
-
?
Ala-Ala + H2O
Ala + Ala
-
-
-
?
Ala-Ile + H2O
Ala + Ile
-
best substrate for the tumor enzyme
-
?
Ala-Ile + H2O
Ala + Ile
-
best substrate for the tumor enzyme
-
?
Ala-Ile + H2O
Ala + Ile
-
-
-
?
Ala-Leu + H2O
Ala + Leu
-
-
-
?
Ala-Leu + H2O
Ala + Leu
-
-
-
?
Ala-Leu + H2O
Ala + Leu
-
-
-
?
Ala-Leu + H2O
Ala + Leu
-
-
-
?
Ala-Leu + H2O
Ala + Leu
-
-
-
?
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
-
-
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
-
-
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
-
-
-
-
?
carnosine + H2O
?
-
-
-
?
carnosine + H2O
?
-
-
-
?
carnosine + H2O
?
-
-
-
?
D-Leu-Gly + H2O
D-Leu + Gly
-
-
-
-
?
D-Leu-Gly + H2O
D-Leu + Gly
-
-
-
-
?
Gly-Gly + H2O
Gly + Gly
-
-
-
?
Gly-Gly + H2O
Gly + Gly
-
-
-
?
Gly-Ile + H2O
Gly + Ile
-
-
-
?
Gly-Ile + H2O
Gly + Ile
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
-
-
?
Gly-Phe + H2O
Gly + Phe
-
-
-
?
Gly-Phe + H2O
Gly + Phe
-
-
-
?
Gly-Phe + H2O
Gly + Phe
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Val + H2O
Gly + Val
-
-
-
?
Gly-Val + H2O
Gly + Val
-
-
-
?
L-Ala-4-methylcoumarin 7-amide + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-4-methylcoumarin 7-amide + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
?
L-Lys-4-methylcoumarin 7-amide + H2O
L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Lys-4-methylcoumarin 7-amide + H2O
L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
?
Met-Ala + H2O
Met + Ala
-
best substrate for E. coli enzyme
-
?
Met-Ala + H2O
Met + Ala
-
-
-
?
Met-Ala + H2O
Met + Ala
-
-
-
?
Met-Ala + H2O
Met + Ala
-
-
-
?
Met-Leu + H2O
Met + Leu
-
-
-
?
Met-Leu + H2O
Met + Leu
-
-
-
?
Phe-Gly + H2O
Phe + Gly
-
-
-
?
Phe-Gly + H2O
Phe + Gly
-
-
-
?
Pro-Ala + H2O
Pro + Ala
-
-
-
?
Pro-Ala + H2O
Pro + Ala
-
-
-
?
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-Gly + H2O
Pro + Gly
-
-
-
?
Pro-Gly + H2O
Pro + Gly
-
-
-
-
?
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-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
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-Met + H2O
Pro + Met
-
-
-
-
?
Pro-Met + H2O
Pro + Met
-
-
-
?
Pro-Met + H2O
Pro + Met
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
?
Pro-Phe + H2O
Pro + Phe
-
-
-
?
Pro-Val + H2O
Pro + Val
-
-
-
?
Pro-Val + H2O
Pro + Val
-
-
-
-
?
additional information
?
-
-
not: Gly-Pro
-
-
?
additional information
?
-
-
not: Gly-Pro
-
-
?
additional information
?
-
-
hydrolyzes dipeptides and dipeptidyl amides with L-proline or hydroxy-L-proline at the N-terminus
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
the tumor enzyme has the highest maximal velocities with substrates containing uncharged bulky C-terminal and small, uncharged N-terminal side chains, the bacterial enzyme hydrolyzes most rapidly substrates with long or flat N-terminal R-groups and small or positively charged C-terminal groups
-
-
?
additional information
?
-
-
only unsubstituted L-alpha-dipeptides
-
-
?
additional information
?
-
-
-
-
-
?
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
-
-
?
additional information
?
-
-
not: Leu-Pro
-
-
?
additional information
?
-
-
not: Gly-Tyr
-
-
?
additional information
?
-
-
not: Leu-Pro
-
-
?
additional information
?
-
-
not: Gly-Tyr
-
-
?
additional information
?
-
-
not: Gly-Pro
-
-
?
additional information
?
-
-
not: Gly-Pro
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
not: Lys-Gly
-
-
?
additional information
?
-
-
not: Gly-Asp
-
-
?
additional information
?
-
-
peptides with small NH2-terminal and bulky nonpolar COOH-terminal R groups are preferred
-
-
?
additional information
?
-
-
the tumor enzyme has the highest maximal velocities with substrates containing uncharged bulky C-terminal and small, uncharged N-terminal side chains, the bacterial enzyme hydrolyzes most rapidly substrates with long or flat N-terminal R-groups and small or positively charged C-terminal groups
-
-
?
additional information
?
-
-
not: Asp-Gly
-
-
?
additional information
?
-
-
only unsubstituted L-alpha-dipeptides
-
-
?
additional information
?
-
-
only unsubstituted L-alpha-dipeptides
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
not: L-Pro-Gly
-
-
?
additional information
?
-
-
not: Gly-Gly
-
-
?
additional information
?
-
-
not: Gly-Gly
-
-
?
additional information
?
-
-
not: some of the arginine- and aspartic acid-containing dipeptides
-
-
?
additional information
?
-
-
not: Gly-Pro
-
-
?
additional information
?
-
-
not: Gly-L-His
-
-
?
additional information
?
-
-
not: Leu-Leu
-
-
?
additional information
?
-
-
not: Ala-Leu
-
-
?
additional information
?
-
-
no or very poor substrate: Leu-4-methylcoumarin 7-amide, Met-4-methylcoumarin 7-amide, Phe-4-methylcoumarin 7-amide, L-Lys-L-Ala-4-methylcoumarin 7-amide
-
-
?
additional information
?
-
-
no or very poor substrate: Leu-4-methylcoumarin 7-amide, Met-4-methylcoumarin 7-amide, Phe-4-methylcoumarin 7-amide, L-Lys-L-Ala-4-methylcoumarin 7-amide
-
-
?
additional information
?
-
-
substrates must contain uncharged side chains and free alpha-amino and carboxyl groups
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
not: anserine
-
-
?
additional information
?
-
-
not: Gly-Gly-Gly
-
-
?
additional information
?
-
-
not: N-Ac-Met
-
-
?
additional information
?
-
-
strictly L-stereospecific
-
-
?
additional information
?
-
-
some activity against peptides with 3 or more residues but none against peptides containing acidic or D-amino acids
-
-
?
additional information
?
-
-
no tripeptidase or arylamidase activity
-
-
?
additional information
?
-
-
only unsubstituted L-alpha-dipeptides
-
-
?
additional information
?
-
-
not: dipeptides containing beta-amino acids
-
-
?
additional information
?
-
-
not: homocarnosine
-
-
?
additional information
?
-
-
not: beta-Ala-Lys
-
-
?
additional information
?
-
-
not: Gly-His-Gly
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
Gly-Leu
-
competitive inhibitor of L-Ala-Gly hydrolysis
L-alanine
-
poor competitive inhibitor of Ala-Gly hydrolysis
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-(2-pyrrolcarbonyl)glycine
-
inhibits cleavage of Pro-Gly
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
phenylmethylsulfonyl fluoride
-
-
phloretin
-
inhibits at 1 mM
additional information
-
inhibition by high substrate concentrations is observed in cases where the Km is low
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
1,7-phenanthroline has no effect
2-mercaptoethanol
-
-
Co2+
-
when substrates are cleaved rapidly by dipeptidase, addition of Co2+ inhibits the reaction. The more slowly a substrate is hydrolyzed in the absence of metals, the greater the activating effect
Co2+
-
hydrolysis of the relative poor substrates, Pro-Gly and Gly-Gly is activated, whereas that of Ala-Gly is inhibited
cysteine
-
-
D-Forms of dipeptides
-
-
D-Forms of dipeptides
-
-
D-Leu-Gly
-
competitive inhibitor of L-Ala-Gly hydrolysis
D-Leu-Gly
-
competitive inhibitor of L-Ala-Gly hydrolysis
DTT
-
-
EDTA
-
-
iodoacetate
-
-
Iodosobenzoate
-
-
Mn2+
-
when substrates are cleaved rapidly by dipeptidase, addition of Mn2+ inhibits the reaction. The more slowly a substrate is hydrolyzed in the absence of metals, the greater the activating effect
Mn2+
-
0.1 mM, inhibits prolinase activity in normal erythrocytes against Pro-Ala, Pro-Val, Pro-Met, Pro-Asp
Mn2+
-
hydrolysis of the relative poor substrates, Pro-Gly and Gly-Gly is activated, whereas that of Ala-Gly is inhibited
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Pb2+
-
-
Zn2+
-
inhibits, but activation in phosphate buffer
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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
29
Gly-L-Asn
-
tumor enzyme
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
0.28
Ala-Leu
-
tumor enzyme
0.44
Ala-Leu
-
Tris buffer
1
Ala-Leu
-
phosphate buffer
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
4.4
Gly-Ile
-
Tris buffer
10
Gly-Ile
-
phosphate buffer
3.16
Gly-L-Leu
-
-
0.79
Gly-Leu
-
at pH 8.0 and 9.2
2.74
Gly-Leu
-
Tris buffer
10
Gly-Leu
-
phosphate buffer
2.4
Gly-Phe
-
Tris buffer
10
Gly-Phe
-
phosphate buffer
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
3.6
Gly-Val
-
Tris buffer
8
Gly-Val
-
phosphate buffer
0.33
Leu-Gly
-
tumor enzyme
0.25
Leu-Leu
-
tumor enzyme
0.25
Leu-Leu
-
tumor enzyme
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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Nordwig, A.; Mayer, H.
The cleavage of prolyl peptides by kidney peptidases. Detection of a new peptidase capable of removing N-terminal proline
Hoppe-Seyler's Z. Physiol. Chem.
354
380-383
1973
Sus scrofa
brenda
Sarid, S.; Berger, A.; Katchalski, E.
Proline iminopeptidase. II. Purification and comparison with iminodipeptidase (prolidase)
J. Biol. Chem.
237
2207-2212
1962
Escherichia coli, Sus scrofa
brenda
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
48
173-179
1994
Homo sapiens
brenda
Patterson, E.K.
A dipeptidase from Escherichia coli B
Methods Enzymol.
45
377-386
1976
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Patterson, E.K.
A dipeptidase from Ehrlich Lettre mouse ascites tumor cells
Methods Enzymol.
45
386-393
1976
Mus musculus
brenda
Lenney, J.F.
Human cytosolic carnosinase: evidence of identity with prolinase, a non-specific dipeptidase
Biol. Chem. Hoppe-Seyler
371
167-171
1990
Homo sapiens
brenda
Lenney, J.F.
Separation and characterization of two carnosine-splitting cytosolic dipeptidases from hog kidney (carnosinase and non-specific dipeptidase)
Biol. Chem. Hoppe-Seyler
371
433-440
1990
Sus scrofa
brenda
Priestman, D.A.; Butterworth, J.
Prolinase and non-specific dipeptidase of human kidney
Biochem. J.
231
689-694
1985
Homo sapiens
brenda
Patterson, E.K.; Gatmaitan, J.S.; Hayman, S.
Substrate specificity and pH dependence of dipeptidases purified from Escherichia coli B and from mouse ascites tumor cells
Biochemistry
12
3701-3709
1973
Escherichia coli, Mus musculus
brenda
Hayman, S.; Patterson, E.K.
Purification and properties of a mouse ascites tumor dipeptidase, a metalloenzyme
J. Biol. Chem.
246
660-669
1971
Mus musculus
brenda
Kunze, N.; Kleinkauf, H.; Bauer, K.
Characterization of two carnosine-degrading enzymes from rat brain. Partial purification and characterization of a carnosinase and a beta-alanyl-arginine hydrolase
Eur. J. Biochem.
160
605-613
1986
Rattus norvegicus
brenda
Plancot, M.T.; Han, K.K.
Purification and characterization of an intracellular dipeptidase from Mycobacterium phlei
Eur. J. Biochem.
28
327-333
1972
Mycolicibacterium phlei, Mycolicibacterium phlei 689
brenda
Roehm, K.H.
Properties of a highly purified dipeptidase (EC 3.4.13.?) from brewers yeast
Hoppe-Seyler's Z. Physiol. Chem.
355
675-686
1974
Saccharomyces cerevisiae
brenda
Myara, I.; Brosset, M.; Lemonnier, A.
Tissue distribution of prolidase and prolinase activity in man and rat
Med. Sci. Res.
15
965-966
1987
Homo sapiens, Rattus norvegicus
-
brenda
Das, M.; Radhakrishnan, A.N.
Glycyl-L-leucine hydrolase, a versatile master dipeptidase from monkey small intestine
Biochem. J.
135
609-615
1973
Platyrrhini
brenda
Noren, O.; Sjoestroem, H.; Josefsson, L.
Studies on a soluble dipeptidase from pig intestinal mucosa. I. Purification and specificity
Biochim. Biophys. Acta
327
446-456
1973
Sus scrofa
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.
354
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.
8
438-439
1980
Homo sapiens
brenda
Das, M.; Radhakrishnan, A.N.
Substrate specificity of a highly active dipeptidase purified from monkey small intestine
Biochem. J.
128
463-465
1972
Platyrrhini
brenda
Hanck, A.; Schreiner, A.
N-(3,5-dicarboxy-4methyl-2-pyrrolylcarbonyl)aminosaeuren als moegliche Substrate fur Prolinase
Hoppe-Seyler's Z. Physiol. Chem.
351
90-94
1970
Sus scrofa
brenda
Mayer, H.; Nordwig, A.
The cleavage of prolyl peptides by kidney peptidases. Purification of iminodipeptidase (prolinase)
Hoppe-Seyler's Z. Physiol. Chem.
354
371-379
1973
Sus scrofa
brenda
Akrawi, A.F.; Bailey, G.S.
Purification and specificity of prolyl dipeptidase from bovine kidney
Biochim. Biophys. Acta
422
170-178
1976
Bos taurus
brenda
Akrawi, A.F.; Bailey, G.S.
The separation of prolyl dipeptidase from other dipeptidases of bovine kidney
Biochem. Soc. Trans.
5
272-274
1977
Bos taurus
brenda
Mikasa, H.; Sasaki, K.
Simultaneous measurement of prolidase and prolinase acitvities in erythrocytes using an isotachophoretic analyser
J. Chromatogr.
343
179-185
1985
Homo sapiens
brenda
Booth, M.; Donnelly, W.J.; Fhaolain, I.N.; Jennings, P.V.; O'Cuinn, G.
Proline-specific peptidases of Streptococcus cremoris AM2
J. Dairy Res.
57
79-88
1990
Lactococcus cremoris, Lactococcus cremoris AM2
-
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
-
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
Varmanen, P.; Steele, J.; Palva, A.
Characterization of a prolinase gene and its product and an adjacent ABC transporter gene from Lactobacillus helveticus
Microbiology
142
809-816
1996
Lactobacillus helveticus, Lactobacillus helveticus 53/7
brenda
Shao, W.; Yueksel, G.Ue.; Dudley, E.G.; Parkin, K.L.; Steele, J.L.
Biochemical and molecular characterization of PepR, a dipeptidase, from Lactobacillus helveticus CNRZ32
Appl. Environ. Microbiol.
63
3438-3443
1997
Lactobacillus helveticus, Lactobacillus helveticus CNRZ32
brenda
Gelman, A.; Kuz'mina, V.; Drabkin, V.; Glatman, L.
Temperature dependent characteristics of intestinal glycyl-L-leucine dipeptidase in boreal zone fish
Comp. Biochem. Physiol. B
136
323-329
2003
Abramis brama, Perca fluviatilis, Sander lucioperca
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
Gromova, L.V.
Effect of phloretin and phloridzin on properties of digestion and absorption in the rat small intestine
J. Evol. Biochem. Physiol.
42
454-460
2006
Rattus norvegicus
-
brenda
Aoki, A.; Shibata, Y.; Okano, S.; Maruyama, F.; Amano, A.; Nakagawa, I.; Abiko, Y.
Transition metal ions induce carnosinase activity in PepD-homologous protein from Porphyromonas gingivalis
Microb. Pathog.
52
17-24
2012
Porphyromonas gingivalis, Porphyromonas gingivalis TDC60
brenda
Andreyeva, E.N.; Ogienko, A.A.; Dubatolova, T.D.; Oshchepkova, A.L.; Kozhevnikova, E.N.; Ivankin, A.V.; Pavlova, G.A.; Kopyl, S.A.; Pindyurin, A.V.
A toolset to study functions of Cytosolic non-specific dipeptidase 2 (CNDP2) using Drosophila as a model organism
BMC Genet.
20
31
2019
Drosophila melanogaster (Q8MT58), Drosophila melanogaster
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