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Information on EC 3.4.13.18 - cytosol nonspecific dipeptidase and Organism(s) Homo sapiens and UniProt Accession Q96KP4
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EC Tree
3.4.13.18 cytosol nonspecific dipeptidaseSpecify your search results
Word Map
- 3.4.13.18
- prolidase
-
3.4.13.11
-
carnosinase
-
glycosyl-phosphatidylinositol
- pro-leu
- iminopeptidase
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids
Synonyms
prolinase, cndp2, glycyl-l-leucine dipeptidase, cpgl-b, non-specific dipeptidase, glycylleucine dipeptidase, glycyl-glycine dipeptidase, glycyl-l-leucine hydrolase, glycylleucine peptidase, iminodipeptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diglycinase
-
-
-
-
dipeptidase, glycylglycine
-
-
-
-
Gly-Leu hydrolase
-
-
-
-
glycyl-glycine dipeptidase
-
-
-
-
glycyl-L-leucine dipeptidase
-
-
-
-
glycyl-L-leucine hydrolase
-
-
-
-
glycyl-L-leucine peptidase
-
-
-
-
glycyl-leucine dipeptidase
-
-
-
-
glycylleucine dipeptidase
-
-
-
-
glycylleucine dipeptide hydrolase
-
-
-
-
glycylleucine hydrolase
-
-
-
-
glycylleucine peptidase
-
-
-
-
human cytosolic non-specific dipeptidase
-
prolinase and carnosinase activity reside in the same enzyme
iminodipeptidase
-
-
-
-
L-amino-acyl-L-amino-acid hydrolase
-
-
-
-
L-prolylglycine dipeptidase
-
-
-
-
N2-beta-alanylarginine dipeptidase
-
-
-
-
non-specific dipeptidase
-
-
-
-
Peptidase A
-
-
-
-
Pro-X dipeptidase
-
-
-
-
Pro-Xaa dipeptidase
-
-
-
-
prolinase
prolyl dipeptidase
prolinase
-
-
-
-
prolyl dipeptidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
CAS REGISTRY NUMBER
COMMENTARY
9025-31-4
-
9032-23-9
-
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
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
?
-
-
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
-
-
?
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
?
-
-
DPP8-v3 may play a key role in the immunoregulation of testes and accordingly may influence spermatogenesis and male fertility
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
-
0.1 mM, increases prolinase activity in normal erythrocytes against Pro-Gly, Pro-Glu, Pro-Leu, Pro-Ser and Pro-Phe
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
(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
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
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-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
Mn2+
-
0.1 mM, inhibits prolinase activity in normal erythrocytes against Pro-Ala, Pro-Val, Pro-Met, Pro-Asp
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ala
-
prolinase activity in erythrocytes from both the normal control and the patients with prolidase (EC 3.4.13.9) deficiency is activated
Gly
-
prolinase activity in erythrocytes from both the normal control and the patients with prolidase (EC 3.4.13.9) deficiency is activated
Ser
-
prolinase activity in erythrocytes from both the normal control and the patients with prolidase (EC 3.4.13.9) deficiency is activated
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000019
(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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
predominantly expressed in testis and pancreas, 5fold higher expression level in human adult than that in fetal testes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). CNDP2_HUMAN
475
0
52878
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Q-Sepharose column chromatography, and Superdex 200 HR gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Priestman, D.A.; Butterworth, J.
Prolinase and non-specific dipeptidase of human kidney
Biochem. J.
231
689-694
1985
Homo sapiens
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
-
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
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
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
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
-
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
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
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
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
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
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
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
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
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)
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