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Information on EC 3.4.13.19 - membrane dipeptidase and Organism(s) Homo sapiens and UniProt Accession Q86TI2

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.13 Dipeptidases
                3.4.13.19 membrane dipeptidase
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q86TI2 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide
hydrolysis of dipeptides
Synonyms
renal dipeptidase, membrane dipeptidase, mbd-3, dhp-i, mbd-1, rdpase, mbd-2, dipeptide hydrolase, nonspecific dipeptidase, lysosomal dipeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43 kDa renal band 3-related protein
-
-
-
-
aminodipeptidase
dehydropeptidase I (DPH I)
-
-
-
-
DHP-I
-
-
-
-
dipeptidase
-
-
-
-
dipeptide hydrolase
-
-
-
-
dipeptidyl hydrolase
-
-
-
-
glycosyl-phosphatidylinositol-anchored renal dipeptidase
-
-
-
-
lysosomal dipeptidase
-
-
MBD-1
-
-
-
-
MBD-2
-
-
-
-
MBD-3
-
-
-
-
MDP
-
-
-
-
membrane-associated dipeptidase
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microsomal MBD
-
nonspecific dipeptidase
-
-
-
-
RDP
-
-
-
-
renal dipeptidase
-
-
-
-
Ser-Met dipeptidase
-
original name
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
CAS REGISTRY NUMBER
COMMENTARY hide
9031-99-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]-2-methylpropanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2R,3S)-2-[[(2R)-2-amino-3-phenylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2R,3S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2R,3S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]-2-methylpropanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]propanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-biphenyl-4-ylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]-4-methylpentanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-naphthalen-2-ylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-3-cyclohexyl-2-(dimethylamino)propanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-3-cyclohexyl-2-(formylamino)propanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-3-cyclohexyl-2-(methylamino)propanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala + H2O
Ala + Ala
show the reaction diagram
-
-
-
-
?
B-type natriuretic peptide 1-32 + H2O
B-type natriuretic peptide 3-32 + ?
show the reaction diagram
-
-
-
-
?
Gly-D-Phe + H2O
Gly + D-Phe
show the reaction diagram
-
-
-
-
?
Gly-Gly + H2O
Gly + Gly
show the reaction diagram
-
-
-
-
?
Gly-Leu + H2O
Gly + Leu
show the reaction diagram
Gly-Phe + H2O
Gly + Phe
show the reaction diagram
-
-
-
-
?
Gly-Trp + H2O
Gly + Trp
show the reaction diagram
-
-
-
-
?
Gly-Val + H2O
Gly + Val
show the reaction diagram
-
-
-
-
?
glycyldehydrophenylalanine + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
L-cystinyl-bis-glycine + H2O
?
show the reaction diagram
-
-
-
-
?
L-Leu-L-Leu + H2O
L-Leu + L-Leu
show the reaction diagram
-
-
-
-
?
Leu-Gly + H2O
Leu + Gly
show the reaction diagram
-
-
-
-
?
leukotriene D4 + H2O
leukotriene E4
show the reaction diagram
-
-
-
?
Met-Met + H2O
Met + Met
show the reaction diagram
-
-
-
-
?
N-[([(1S,2R)-2-[(3-cyclohexyl-L-alanyl)amino]-3-hydroxy-1-methylpropyl]oxy)carbonyl]-2'-deoxy-2'-methylidenecytidine + H2O
?
show the reaction diagram
-
-
-
-
?
N-[([(1S,2S)-2-[(3-cyclohexyl-L-alanyl)amino]-1,4-dimethyl-3-oxopentyl]oxy)carbonyl]-2'-deoxy-2'-methylidenecytidine + H2O
?
show the reaction diagram
-
-
-
-
?
Phe-Gly + H2O
Phe + Gly
show the reaction diagram
-
-
-
-
?
Phe-Tyr + H2O
Phe + Tyr
show the reaction diagram
-
-
-
-
?
pro-B-type natriuretic peptide 1-108 + H2O
pro-B-type natriuretic peptide 3-108 + ?
show the reaction diagram
-
-
-
-
?
S-N-ethylmaleimide-L-cysteinyl-glycine + H2O
?
show the reaction diagram
-
-
-
-
?
Trp-Gly + H2O
Trp + Gly
show the reaction diagram
-
-
-
-
?
Val-Gly + H2O
Val + Gly
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
1 mM, activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1G244
i.e. (2S)-2-amino-4-[4-[bis(4-fluorophenyl)methyl]-1-piperazinyl]-1-(1,3-dihydro-2H-isoindol-2-yl)-1,4-butanedione, specific inhibitor of DPP8 and DPP9
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-(trifluoromethyl)phenyl)acrylic acid
-
50% inhibition at 10 nM
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-bromophenyl)acrylic acid
-
50% inhibition at 6 nM
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-fluorophenyl)acrylic acid
-
50% inhibition at 5 nM
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-iodophenyl)acrylic acid
-
50% inhibition at 8 nM
1,10-phenanthroline
-
-
bestatin
-
non-competitive
Cilastatin
Co2+
-
-
cysteine
-
-
Dansylethylenediamine
-
cilastatin protects
DTT
-
reversible, competitive
EDTA
-
-
N-bromosuccinimide
-
-
N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
-
cilastatin protects
p-hydroxymercuribenzoate
-
-
Pro-Ala
-
competitive to hydrolysis of Gly-Leu
additional information
-
importance of Glu25 in the catalytic activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.22
Gly-L-Leu
-
-
0.99
Gly-L-Phe
-
-
2.03
Gly-L-Trp
-
-
11
Gly-L-Val
-
-
0.79
Gly-Leu
-
-
0.102
glycyldehydrophenylalanine
-
-
0.21
L-Leu-Gly
-
-
0.056 - 0.086
L-Leu-L-Leu
0.67
L-Phe-Gly
-
-
0.15
L-Trp-Gly
-
-
0.09
L-Val-Gly
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
enzyme form F
9 - 11
-
enzyme form S
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
enzyme form S
70
-
enzyme form F
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 4.8
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isolated from skin
Manually annotated by BRENDA team
additional information
-
not found in liver or hematopoietic progenitor cells such as colony-forming units of granulocyte-macrophage
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
low expression level
Manually annotated by BRENDA team
and perinucleus
Manually annotated by BRENDA team
-
the active site faces towards the microvillar membrane of a kidney tubule
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
survival and the proliferative capacity are significantly diminished in the presence of 10 microM of inhibitor 1G244, both in fibroblasts and in HaCaT cells. DPP9 gene silencing results in decreased adhesion of fibroblasts, as well as in decreased migration of fibroblasts and HaCaTcells. DPP9 accumulates on the edges of plasma membranes of fibroblasts and keratinocytes adhering to surface
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DPP9_HUMAN
863
0
98263
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
115000
-
1 * 94000 + 1 * 115000, enzyme form S, SDS-PAGE
130000
-
SDS-PAGE under nonreducing conditions
135000
-
enzyme form F, gel filtration
180000
-
gel filtration
200000
-
enzyme form S, gel filtration
218000
-
gel filtration
220000
-
HPLC gel filtration
59000
62000
-
2 * 62000, SDS-PAGE under reducing conditions
66000
-
2 * 66000, enzyme form F, SDS-PAGE
94000
-
1 * 94000 + 1 * 115000, enzyme form S, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
tetramer
-
4 * 59000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
additional information
-
not a glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
unstable below, both enzyme forms
647108
8
-
both enzyme forms stable
647108
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
enzyme form S is unstable above
53
-
12 min, about 50% loss of activity
60
-
enzyme form F is stable up to
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 forms different in electrophoretic mobility: form S (slow) and F (fast)
-
partial
-
ultracentrifugation and Superose 12 (10/300) gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) Codon Plus-RIL cells
-
expressed in Mus musculus
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
in 20 mM Tris-HCl, pH 8.0, 500 mM arginine, containing 1 mM reduced glutathione, 0.2 mM oxidized glutathione, and sodium chloride
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Priestman, D.A.; Butterworth, J.
Prolinase and non-specific dipeptidase of human kidney
Biochem. J.
231
689-694
1985
Homo sapiens
Manually annotated by BRENDA team
Hooper, N.M.; Keen, J.N.; Turner, A.J.
Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme
Biochem. J.
265
429-433
1990
Homo sapiens
Manually annotated by BRENDA team
Park, H.S.; Kim, D.H.; Kwark, H.S.E.; Park, S.K.; Kang, S.K.; Chung, B.H.; Yoo, G.S.
Human renal dipeptidase from kidneys of renal stone patients: partial purification
Arch. Pharm. Res.
16
295-299
1993
Homo sapiens
-
Manually annotated by BRENDA team
Adachi, H.; Katayama, T.; Nakazato, H.; Tsujimoto, M.
Importance of Glu-125 in the catalytic activity of human renal dipeptidase
Biochim. Biophys. Acta
1163
42-48
1993
Homo sapiens
Manually annotated by BRENDA team
Adachi, H.; Kubota, I.; Okamura, N.; Iwata, H.; Tsujimoto, M.; Nakazato, H.; Nishihara, T.; Noguchi, T.
Purification and characterization of human microsomal dipeptidase
J. Biochem.
105
957-961
1989
Homo sapiens
Manually annotated by BRENDA team
Brewis, I.A.; Ferguson, M.A.J.; Mehlert, A.; Turner, A.J.; Hooper, N.M.
Structures of the glycosyl-phosphatidylinositol anchors of porcine and human renal membrane dipeptidase. Comprehensive structural studies on the porcine anchor and interspecies comparison of the glycan core structures
J. Biol. Chem.
270
22946-22956
1995
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Adachi, H.; Katayama, T.; Inuzuka, C.; Oikawa, S.; Tsujimoto, M.; Nakazato, H.
Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form
J. Biol. Chem.
265
15341-15345
1990
Homo sapiens
Manually annotated by BRENDA team
Campbell, B.J.; Forrester, L.J.; Zahler, W.L.; Burks, M.
beta-Lactamase activity of purified and partially characterized human renal dipeptidase
J. Biol. Chem.
259
14586-14590
1984
Homo sapiens
Manually annotated by BRENDA team
Campbell, B.J.; Di Shih, Y.; Forrester, L.J.; Zahler, W.L.
Specificity and inhibition studies of human renal dipeptidase
Biochim. Biophys. Acta
956
110-118
1988
Homo sapiens
Manually annotated by BRENDA team
Sugiura, M.; Ito, Y.; Hirano, K.; Sawaki, S.
Purification and properties of human kidney dipeptidases
Biochim. Biophys. Acta
522
541-550
1978
Homo sapiens
Manually annotated by BRENDA team
Nitani, Y.; Satow, Y.; Adachi, H.; Tsujimoto, M.
Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis
J. Mol. Biol.
321
177-184
2002
Homo sapiens
Manually annotated by BRENDA team
Gurulingappa, H.; Buckhalts, P.; Kinzler, K.W.; Vogelstein, B.; Khan, S.R.
Synthesis and evaluation of aminophosphinic acid derivatives as inhibitors of renal dipeptidase
Bioorg. Med. Chem. Lett.
14
3531-3533
2004
Homo sapiens
Manually annotated by BRENDA team
Murphy, R.C.; Gijon, M.A.
Biosynthesis and metabolism of leukotrienes
Biochem. J.
405
379-395
2007
Homo sapiens (P16444)
Manually annotated by BRENDA team
Dolenc, I.; Pain, R.; Turk, V.
Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization
Biol. Chem.
388
47-51
2007
Homo sapiens
Manually annotated by BRENDA team
Kohchi, Y.; Hattori, K.; Oikawa, N.; Mizuguchi, E.; Isshiki, Y.; Aso, K.; Yoshinari, K.; Shirai, H.; Miwa, M.; Inagaki, Y.; Ura, M.; Ogawa, K.; Okabe, H.; Ishitsuka, H.; Shimma, N.
Design and synthesis of novel prodrugs of 2-deoxy-2-methylidenecytidine activated by membrane dipeptidase overexpressed in tumor tissues
Bioorg. Med. Chem. Lett.
17
2241-2245
2007
Homo sapiens
Manually annotated by BRENDA team
Lam, C.S.; Burnett, J.C.; Costello-Boerrigter, L.; Rodeheffer, R.J.; Redfield, M.M.
Alternate circulating pro-B-type natriuretic peptide and B-type natriuretic peptide forms in the general population
J. Am. Coll. Cardiol.
49
1193-1202
2007
Homo sapiens
Manually annotated by BRENDA team
Gabrilovac, J.; Cupic, B.; Zapletal, E.; Kraus, O.; Jakic-Razumovic, J.
Dipeptidyl peptidase 9 (DPP9) in human skin cells
Immunobiology
222
327-342
2017
Homo sapiens (Q86TI2)
Manually annotated by BRENDA team