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Information on EC 3.1.3.5 - 5'-nucleotidase and Organism(s) Rattus norvegicus and UniProt Accession P21588

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.5 5'-nucleotidase
IUBMB Comments
Wide specificity for 5'-nucleotides.
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P21588
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
5'-nucleotidase, ecto-5'-nucleotidase, ectonucleotidase, 5'nucleotidase, 5'-nt, cn-ii, ecto-nucleotidase, pyrimidine 5'-nucleotidase, cytosolic 5'-nucleotidase, ampase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ecto-5'-nucleotidase
-
5'-adenylic phosphatase
-
-
-
-
5'-AMP nucleotidase
-
-
-
-
5'-AMPase
-
-
-
-
5'-mononucleotidase
-
-
-
-
5'-nucleotidase
-
-
5'nucleotidase
adenosine 5'-monophosphatase
-
-
-
-
adenosine 5'-phosphatase
-
-
-
-
adenosine monophosphatase
-
-
-
-
AMP phosphatase
-
-
-
-
AMP phosphohydrolase
-
-
-
-
AMPase
-
-
-
-
CD73 antigen
-
-
-
-
ecto 5'-nucleotidase
-
-
ecto-5'-NT/CD73
-
-
ecto-5'-nucleotidase
ecto-5'-nucleotidase/CD73
-
-
ecto-5'nucleotidase
-
-
ecto-nucleotidase
-
-
ectonucleotidase
-
-
IMP 5'-nucleotidase
-
-
-
-
snake venom 5'-nucleotidase
-
-
-
-
thymidine monophosphate nucleotidase
-
-
-
-
UMPase
-
-
-
-
uridine 5'-nucleotidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5'-ribonucleotide phosphohydrolase
Wide specificity for 5'-nucleotides.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-73-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
a 5'-ribonucleotide + H2O
a ribonucleoside + phosphate
show the reaction diagram
-
-
-
?
1,N6-ethenoadenosine 5'-phosphate + H2O
1,N6-ethenoadenosine ribonucleoside + phosphate
show the reaction diagram
-
45% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
2-(cyclohexylethylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylethylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-(cyclohexylmethylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylmethylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-(cyclohexylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-(cyclopentylthio)adenosine 5'-monophosphate + H2O
2-(cyclopentylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-(dioxanylethylthio)adenosine 5'-monophosphate + H2O
2-(dioxanylethylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-(dioxolanylethylthio)adenosine 5'-monophosphate + H2O
2-(dioxolanylethylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-(hexylthio)adenosine 5'-monophosphate + H2O
2-(hexylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-(propylthio)adenosine 5'-monophosphate + H2O
2-(propylthio)adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3-beta-ribofuranosyladenine 5'-monophosphate + H2O
3-beta-ribofuranosyladenine + phosphate
show the reaction diagram
-
24% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-AMP + H2O
?
show the reaction diagram
-
the enzyme is responsible for the production of adenosine in the cardiac tissue
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
5'-CMP + xanthosine
XMP + cytidine
show the reaction diagram
-
-
-
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
show the reaction diagram
5'-dCMP + H2O
deoxycytidine + phosphate
show the reaction diagram
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
show the reaction diagram
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
show the reaction diagram
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
5'-GMP + xanthosine
XMP + guanosine
show the reaction diagram
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
5'-IMP + xanthosine
XMP + inosine
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
5'-UMP + xanthosine
XMP + uridine
show the reaction diagram
-
-
-
-
?
5'-XMP + H2O
xanthosine + phosphate
show the reaction diagram
-
-
-
?
6-chloropurine ribonucleoside 5'-monophosphate + H2O
6-chloropurine ribonucleoside + phosphate
show the reaction diagram
-
50% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
adenosine 5'-O-thiophosphate + H2O
?
show the reaction diagram
-
6% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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
a 5'-ribonucleotide + H2O
a ribonucleoside + phosphate
show the reaction diagram
-
-
-
?
5'-AMP + H2O
?
show the reaction diagram
-
the enzyme is responsible for the production of adenosine in the cardiac tissue
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
0.1 mM activates, 4 mM inhibits, plasma membrane enzyme
Mn2+
-
0.1 mM activates, 4 mM inhibits, plasma membrane enzyme
NaCl
-
activation, cytosolic enzyme
Zn2+
-
a Zn2+-binding enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-pentyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
-
1-tert-butyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
-
1-tert-butyl-5-chloro-6-(2-hydroxy-5-methylphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
-
1-tert-butyl-5-chloro-6-(2-hydroxyphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
-
2-(3-methyl-1,5-diphenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
-
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
-
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
-
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
-
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
-
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
3,8-dimethyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
3,8-dimethyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
3-methyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
5-chloro-3-methyl-1-phenyl-6-(2-propoxyphenyl)-1H-pyrazolo[3,4-b]pyridine
-
5-chloro-6-(2-(heptyloxy)phenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
-
5-chloro-6-(2-hydroxy-5-methylphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
-
5-chloro-6-(2-hydroxyphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
-
5-chloro-6-(2-methoxyphenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
-
6-chloro-7-(2-hydroxy-5-methylphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
6-chloro-7-(2-hydroxyphenyl)-1-methylpyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
6-chloro-7-(2-hydroxyphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
7-methoxy-3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
alpha,beta-methylene-ADP
-
sulfamic acid
-
1-amino-2-methyl-4-(phenylamino)anthracene-9,10-dione
-
4% inhibition at 1 mM
1-amino-4-(1-anthracenylamino)-9,10-dioxo-9,10 dihydroanthracene-2-sulfonate
-
-
1-amino-4-(1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
competitive mechanism
1-amino-4-(2,3-dimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
39% inhibition at 1 mM
1-amino-4-(2,4-dimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
47% inhibition at 1 mM
1-amino-4-(2,5-dimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
26% inhibition at 1 mM
1-amino-4-(2-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
47% inhibition at 1 mM
1-amino-4-(2-anthracenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
competitive mechanism
1-amino-4-(2-carboxy-4-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
52% inhibition at 1 mM
1-amino-4-(2-carboxy-4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-carboxy-5-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
27% inhibition at 1 mM
1-amino-4-(2-carboxy-5-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
60% inhibition at 1 mM
1-amino-4-(2-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-ethoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
56% inhibition at 1 mM
1-amino-4-(2-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-methoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
9% inhibition at 1 mM
1-amino-4-(2-methyl-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
33% inhibition at 1 mM
1-amino-4-(2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
14% inhibition at 1 mM
1-amino-4-(3,4-dimethoxyphenethylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
44% inhibition at 1 mM
1-amino-4-(3-amino-2,4,6-trimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(3-amino-4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(3-amino-5-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
44% inhibition at 1 mM
1-amino-4-(3-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
31% inhibition at 1 mM
1-amino-4-(3-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
26% inhibition at 1 mM
1-amino-4-(3-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-amino-3-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-bromo-2-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
56% inhibition at 1 mM
1-amino-4-(4-bromophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-carboxymethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
26% inhibition at 1 mM
1-amino-4-(4-chlorophenethylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
62% inhibition at 1 mM
1-amino-4-(4-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-ethoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
31% inhibition at 1 mM
1-amino-4-(4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-phenoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-phenylaminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
37% inhibition at 1 mM
1-amino-4-(4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(5-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(6-carboxy-2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(6-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(8-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(9-phenanthrenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
58% inhibition at 1 mM
1-amino-4-(benzylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
43% inhibition at 1 mM
1-amino-4-(cyclohexylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(cyclopentylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
51% inhibition at 1 mM
1-amino-4-(isopropylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
15% inhibition at 1 mM
1-amino-4-(phenethylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
53% inhibition at 1 mM
1-amino-4-bromo-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
-
-
1-amino-4-[4-(diethoxyphosphoryl)methylphenylamino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
28% inhibition at 1 mM
3-(2-(3,4,5-trimethoxybenzylideneamino)thiazol-4-yl)-2Hchromen-2-one
-
-
3-(2-(3-chlorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(3-methoxy-4-phenoxybenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(3-nitrobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(4-bromobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(4-chlorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(4-fluorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(furan-2-ylmethyleneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
4-(3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzenesulfonic acid
-
-
5-ethynyl-2',3'-dideoxyuridine
-
-
6-amino-4-hydroxynaphthalene-2-sulfonic acid
-
most potent inhibitor of the screen
adenosine
-
-
adenosine 5'-(alpha,beta-methylene)diphosphate
agglutinin
-
enzyme from glioblastoma cells
-
alpha,beta-methylene ADP
-
-
alpha,beta-methylene-ADP
-
-
alpha/beta-methylene-ADP
-
a specific CD73 inhibitor
alphabeta-methylene ADP
-
0.05 mM
Ammonium molybdate
-
17.6% residual activity at 0.1 mM ammonium molybdate
clomipramine
-
enzymatic activity is decreased by the antidepressant clomipramine after in vitro exposure
concanavalin A
-
Cu2+
-
inhibition of cytosolic and membrane-bound enzyme
fluoxetine
L-arginine
-
21% inhibition at 0.1 mM
nitric oxide
-
-
nortriptyline
sertraline
-
enzymatic activity is decreased by the antidepressant sertraline after in vitro exposure
sodium 1-amino-9,10-dioxo-4-(phenylamino)-9,10-dihydroanthracene-2-sulfonate
-
-
sulfamic acid
-
-
tetrasodium 4-[[4-([4-[(4-amino-9,10-dioxo-3-sulfonato-9,10-dihydroanthracen-1-yl)amino]-2-sulfonatophenyl]amino)-6-chloro-1,3,5-triazin-2-yl]amino]benzene-1,2-disulfonate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
-
-
D-Aspartate
-
-
ferric nitrate
-
activation between 0.001 mM and 1 mM
indomethacin
-
0.1 mM, causes 52% increase of activity in vivo after 48 h
interferon-beta
-
-
-
L-aspartate
-
-
triiodothyronine
-
treatment with 50 nM significantly increases ecto-5'-NT/CD73 mRNA expression in vivo
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0065
1,N6-ethenoadenosine 5'-phosphate
-
-
0.007
3-beta-ribofuranosyladenine 5'-monophosphate
-
-
0.0056 - 14
5'-AMP
0.035 - 17
5'-CMP
0.077 - 35
5'-dAMP
1.1
5'-dGMP
-
-
0.7
5'-dIMP
-
-
0.014 - 22
5'-dTMP
0.0064 - 0.7
5'-GMP
0.008 - 0.2
5'-IMP
0.048 - 0.074
5'-TMP
0.014 - 6
5'-UMP
2.9
5'-XMP
-
-
0.0053
6-chloropurine ribonucleoside 5'-monophosphate
-
-
0.002
adenosine 5'-O-thiophosphate
-
-
0.02 - 0.1348
AMP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00293
1-amino-4-(1-anthracenylamino)-9,10-dioxo-9,10 dihydroanthracene-2-sulfonate
-
-
0.00053
1-amino-4-(1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00015
1-amino-4-(2-anthracenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00026
1-amino-4-(2-carboxy-4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00653
1-amino-4-(2-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00184
1-amino-4-(2-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00274
1-amino-4-(2-methyl-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00147
1-amino-4-(2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.036
1-amino-4-(3-amino-2,4,6-trimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0252
1-amino-4-(3-amino-4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0123
1-amino-4-(3-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.01
1-amino-4-(4-amino-3-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.000297
1-amino-4-(4-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0113
1-amino-4-(4-bromophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00481
1-amino-4-(4-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00567
1-amino-4-(4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00062
1-amino-4-(4-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.36
1-amino-4-(4-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00151
1-amino-4-(4-phenoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00343
1-amino-4-(4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0117
1-amino-4-(5-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00343
1-amino-4-(6-carboxy-2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0153
1-amino-4-(6-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00605
1-amino-4-(8-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00166
1-amino-4-(cyclohexylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00091
ADP
-
in 10 mM HEPES (pH 7.4), 2 mM MgCl2, and 1 mM CaCl2
0.00087
alpha,beta-methylene-ADP
-
in 10 mM HEPES (pH 7.4), 2 mM MgCl2, and 1 mM CaCl2
0.0089
ATP
-
in 10 mM HEPES (pH 7.4), 2 mM MgCl2, and 1 mM CaCl2
0.0152
sodium 1-amino-9,10-dioxo-4-(phenylamino)-9,10-dihydroanthracene-2-sulfonate
-
-
0.00307
tetrasodium 4-[[4-([4-[(4-amino-9,10-dioxo-3-sulfonato-9,10-dihydroanthracen-1-yl)amino]-2-sulfonatophenyl]amino)-6-chloro-1,3,5-triazin-2-yl]amino]benzene-1,2-disulfonate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00729
1-pentyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Rattus norvegicus
at pH 7.5 and 37°C
0.00543
1-tert-butyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Rattus norvegicus
at pH 7.5 and 37°C
0.1
1-tert-butyl-5-chloro-6-(2-hydroxy-5-methylphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
1-tert-butyl-5-chloro-6-(2-hydroxyphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
2-(3-methyl-1,5-diphenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0235
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Rattus norvegicus
at pH 7.5 and 37°C
0.00203
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
Rattus norvegicus
at pH 7.5 and 37°C
0.1
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0111
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
Rattus norvegicus
at pH 7.5 and 37°C
0.1
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00067
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
Rattus norvegicus
at pH 7.5 and 37°C
0.1
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
3,8-dimethyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
3,8-dimethyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
3-methyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00645
3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
at pH 7.5 and 37°C
0.1
5-chloro-3-methyl-1-phenyl-6-(2-propoxyphenyl)-1H-pyrazolo[3,4-b]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-(heptyloxy)phenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-hydroxy-5-methylphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-hydroxyphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-methoxyphenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00352
6-chloro-7-(2-hydroxy-5-methylphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Rattus norvegicus
at pH 7.5 and 37°C
0.00214
6-chloro-7-(2-hydroxyphenyl)-1-methylpyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Rattus norvegicus
at pH 7.5 and 37°C
0.1
6-chloro-7-(2-hydroxyphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
7-methoxy-3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0773
sulfamic acid
Rattus norvegicus
at pH 7.5 and 37°C
0.027
1-amino-4-bromo-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.0443
4-(3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzenesulfonic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.0104
6-amino-4-hydroxynaphthalene-2-sulfonic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.0773
sulfamic acid
Rattus norvegicus
-
at pH 7.4 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17
-
substrate 5'-IMP, liver cytosol
175
-
pH 7.4, 37°C
60.5
-
synaptic plasma membrane
7.48
-
cytosolic enzyme from brain
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
brain, cytosolic enzyme
7.4
-
assay at
7.8 - 8.1
-
enzyme from glioblastoma cells
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
spinal cord astrocyte
Manually annotated by BRENDA team
-
from submandibular salivary glands
Manually annotated by BRENDA team
-
endothelial cell in choroid and ciliary body
Manually annotated by BRENDA team
-
ectonucleotidases are differentially expressed along the nephron
Manually annotated by BRENDA team
-
cell culture from submandibular salivary glands
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the key and rate-limiting enzyme in the ectonucleotidase pathway is ecto-5'-nucleotidase, which catalyzes the final step of dephosphorylation of AMP to adenosine
physiological function
-
the enzyme plays a role in the generation of extracellular adenosine, a key modulator of male fertility
additional information
-
unilateral cortical stab injury causes a rapid and irreversible loss of the enzyme from neurons, accounting for a decrease in the overall enzyme expression, accompanied with a gradual increase in e-5NT-positive astrocytes, accounting for upregulation of the enzyme levels in the injured area. CSI induces dynamic changes in the expression pattern of e-5NT that modify the ATP/adenosine ratio and the extent of P1 and P2 receptors activation and, therefore, outcome of the pathological processes after cortical stab injury
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
5NTD_RAT
576
1
63969
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
131000
-
x * 131000, brain cytosol, SDS-PAGE
135000
-
enzyme from glioblastoma cells, gel filtration in presence of 0.6% sodium deoxycholate
140000
-
gel filtration in absence of detergent
147000
-
heart, membrane-bound, SDS-PAGE after cross-linkage with dimethylsuberimidate
182000
-
liver cytosol, absence of ATP, allosteric protein, binding of adenine nucleotides induces a more compact and stable conformation, calculation from Stokes radius and partial specific volume
191000
-
liver cytosol, SDS-PAGE after cross-linkage with dimethylsuberimidate
197000
-
liver cytosol, presence of 3 mM ATP, allosteric protein, binding of adenine nucleotides induces a more compact and stable conformation, calculation from Stokes radius and partial specific volume
230000
-
brain cytoplasm, gel filtration
260000
-
liver microsomes, gel filtration in presence of detergents
268000
286000
-
enzyme from synaptic plasma membrane, gel filtration
54300
-
4 * 54300, brain cytoplasm, SDS-PAGE
70000
-
SDS-PAGE
72000
74000
85000
-
x * 92000, glycosylated enzyme form, x * 85000 deglycosylated enzyme form, SDS-PAGE
92000
-
x * 92000, glycosylated enzyme form, x * 85000 deglycosylated enzyme form, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70000, SDS-PAGE
dimer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
side-chain modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
-
enzyme from glioblastoma cells, stable up to
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme from glioblastoma cells, 40 mM Tris-HCl buffer, pH 7.4, 0.1 M NaCl, 0.1% Triton X-100, several months stable
-
0°C, 0.1 M Tris-HCl, pH 7.5, 1 mM MgCl2, 1 mM 5'-AMP, stable for 3 months
-
4°C, 50 mM Tris-HCl, pH 7.5, 50 mM sodium cholate, 1 M NaCl
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
agarose-coupled GSH affinity chromatography
-
brain cytosol
-
brain cytosol and synaptic plasma membrane
-
glioblastoma cells, membrane-bound
-
glutathione-S-transferase fusion protein: affinity chromatography
-
heart, membrane-bound
-
liver cytosol
-
liver, membrane-bound
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS-7 cells
catalytically active recombinant soluble glutathione-S transferase/ecto-5'-NT fusion protein is expressed in insect cells using the baculovirus system
-
expression in Sf9 cells
-
glutathione-S-transferase fusion protein expressed in insect cells using a baculovirus system
-
glutathione-S-transferase fusion protein expressed in Sf9 insect cells
-
recombinant expression in COS-7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
fibroblast growth factor 2 upregulates protein expression of the enzyme in spinal cord astrocytes
in carotid bodies obtained from rats reared under chronic hypobaric hypoxia there is a significant upregulation of enzyme mRNA relative to normoxic controls
after scratch wounding, the abundance of enzyme mRNA increases more than 2fold
-
an infection with Fasciola hepatica leads to 68% higher enzyme activity 87 days after infection in serum and tissue
-
unilateral cortical stab injury causes a rapid and irreversible loss of the enzyme from neurons, accounting for a decrease in the overall enzyme expression, accompanied with a gradual increase in e-5NT-positive astrocytes, accounting for upregulation of the enzyme levels in the injured area. CSI induces dynamic changes in the expression pattern of e-5NT that modify the ATP/adenosine ratio and the extent of P1 and P2 receptors activation and, therefore, outcome of the pathological processes after cortical stab injury
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
-
tool for drug screening
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wada, I.; Eto, S.; Himeno, M.; Kato, K.
5'-Nucleotidase in rat liver lysosomes
J. Biochem.
101
1077-1085
1987
Rattus norvegicus
Manually annotated by BRENDA team
Lamers, J.M.J.; Heyliger, C.E.; Panagia, V.; Dhalla, N.S.
Properties of 5-nucleotidase in rat heart sarcolemma
Biochim. Biophys. Acta
742
568-575
1983
Rattus norvegicus
Manually annotated by BRENDA team
Itoh, R.
Studies on some molecular properties of cytosol 5'-nucleotidase from rat liver
Biochim. Biophys. Acta
716
110-113
1982
Rattus norvegicus
Manually annotated by BRENDA team
Naito, Y.; Lowenstein, J.M.
5'-Nucleotidase from rat heart
Biochemistry
20
5188-5194
1981
Rattus norvegicus
Manually annotated by BRENDA team
Itoh, R.
Purification and some properties of cytosol 5'-nucleotidase from rat liver
Biochim. Biophys. Acta
657
402-410
1981
Rattus norvegicus
Manually annotated by BRENDA team
Newby, A.; Luzio, P.; Hales, C.N.
The properties and extracellular location of 5'-nucleotidase of the rat fat-cell plasma membrane
Biochem. J.
146
625-633
1975
Rattus norvegicus
Manually annotated by BRENDA team
Widnell, C.C.
Purification of rat liver 5'-nucleotidase as a complex with sphingomyelin
Methods Enzymol.
32
368-374
1974
Rattus norvegicus
Manually annotated by BRENDA team
Gibson, W.B.; Drummond, G.I.
Properties of 5'-nucleotidase from avian heart
Biochemistry
11
223-229
1972
Gallus gallus, Columba livia, Rattus norvegicus, Sturnus vulgaris
Manually annotated by BRENDA team
Turnay, J.; Olmo, N.; Navarro, J.M.; Gavilanes, J.G.; Lizarbe, M.A.
Isolation and characterization of the ecto-5'-nucleotidase from a rat glioblastoma cell line
Mol. Cell. Biol.
117
23-33
1992
Rattus norvegicus
Manually annotated by BRENDA team
Yegutkin, G.G.
Effects of Triton X-100 and concanavalin A on the properties of 5'-nucleotidase in rat liver and adipose plasma membranes: a role of membrane structure in the regulation of enzyme activity
Membr. Cell Biol.
10
631-638
1997
Rattus norvegicus
Manually annotated by BRENDA team
Servos, J.; Reilnder, H.; Zimmermann, H.
Catalytically active soluble ecto-5'-nucleotidase purified after heterologous expression as a tool for drug screening
Drug Develop. Res.
45
269-276
1998
Rattus norvegicus
-
Manually annotated by BRENDA team
Orford, M.R.; Saggerson, E.D.
A low-Km 5'-nucleotidase from rat brain cytosolic fraction: purification, kinetic properties, and description of regulation by a novel factor that increases sensitivity to inhibition by ATP and ADP
J. Neurochem.
67
795-804
1996
Rattus norvegicus
Manually annotated by BRENDA team
Lai, K.M.; Wong, P.C.L.
A comparison of the properties of 5'-nucleotidase purified from the cytosolic and synaptic plasma membrane fractions of rat forebrain
Int. J. Biochem.
23
1123-1130
1991
Rattus norvegicus
Manually annotated by BRENDA team
Rajput, A.; Chakravarthy, B.R.; DSouza, C.J.M.
Isolation and characterization of 5'-nucleotidase inhibitor from rat liver
Indian J. Biochem. Biophys.
29
204-208
1992
Rattus norvegicus
Manually annotated by BRENDA team
Garvey, E.P.; Prus, K.L.
A specific inhibitor of heart cytosolic 5'-nucleotidase I attenuates hydrolysis of adenosine 5'-monophosphate in primary rat myocytes
Arch. Biochem. Biophys.
364
235-240
1999
Rattus norvegicus
Manually annotated by BRENDA team
Kocic, G.; Pavlovic, D.; Jevtovic, T.; Kocic, R.; Bojic, A.; Vlahovic, P.; Djordjevic, V.; Sokolovic, D.; Djindjic, B.
Oxidative modification of rat liver 5'-nucleotidase: the mechanisms for protection and re-activation
Arch. Physiol. Biochem.
109
323-330
2001
Rattus norvegicus
Manually annotated by BRENDA team
Balz, D.; de Souza Wyse, A.T.; Morsch, V.M.; da Silva, A.C.; Vieira, V.L.; Morsch, A.L.; Schetinger, M.R.
In vitro effects of L-arginine and guanidino compounds on NTPDase1 and 5'-nucleotidase activities from rat brain synaptosomes
Int. J. Dev. Neurosci.
21
75-82
2003
Rattus norvegicus
Manually annotated by BRENDA team
Vekaria, R.M.; Shirley, D.G.; Sevigny, J.; Unwin, R.J.
Immunolocalization of ectonucleotidases along the rat nephron
Am. J. Physiol.
290
F550-F560
2006
Rattus norvegicus
Manually annotated by BRENDA team
Henz, S.L.; Ribeiro, C.G.; Rosa, A.; Chiarelli, R.A.; Casali, E.A.; Sarkis, J.J.
Kinetic characterization of ATP diphosphohydrolase and 5'-nucleotidase activities in cells cultured from submandibular salivary glands of rats
Cell Biol. Int.
30
214-220
2006
Rattus norvegicus
Manually annotated by BRENDA team
Barsotti, C.; Pesi, R.; Giannecchini, M.; Ipata, P.L.
Evidence for the involvement of cytosolic 5'-nucleotidase (cN-II) in the synthesis of guanine nucleotides from xanthosine
J. Biol. Chem.
280
13465-13469
2005
Rattus norvegicus
Manually annotated by BRENDA team
Satriano, J.; Wead, L.; Cardus, A.; Deng, A.; Boss, G.R.; Thomson, S.C.; Blantz, R.C.
Regulation of ecto-5'-nucleotidase by NaCl and nitric oxide: potential roles in tubuloglomerular feedback and adaptation
Am. J. Physiol. Renal Physiol.
291
F1078-F1082
2006
Rattus norvegicus
Manually annotated by BRENDA team
Boeck, C.R.; Kroth, E.H.; Bronzatto, M.J.; Vendite, D.
Effect of the L- or D-aspartate on ecto-5'nucleotidase activity and on cellular viability in cultured neurons: participation of the adenosine A(2A) receptors
Amino Acids
33
439-444
2007
Rattus norvegicus
Manually annotated by BRENDA team
Iqbal, J.; Jirovsky, D.; Lee, S.Y.; Zimmermann, H.; Mueller, C.E.
Capillary electrophoresis-based nanoscale assays for monitoring ecto-5'-nucleotidase activity and inhibition in preparations of recombinant enzyme and melanoma cell membranes
Anal. Biochem.
373
129-140
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Babiychuk, E.B.; Draeger, A.
Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?
Biochem. Soc. Trans.
34
374-376
2006
Rattus norvegicus
Manually annotated by BRENDA team
Nedeljkovic, N.; Bjelobaba, I.; Subasic, S.; Lavrnja, I.; Pekovic, S.; Stojkov, D.; Vjestica, A.; Rakic, L.; Stojiljkovic, M.
Up-regulation of ectonucleotidase activity after cortical stab injury in rats
Cell Biol. Int.
30
541-546
2006
Rattus norvegicus
Manually annotated by BRENDA team
Bernardi, A.; Bavaresco, L.; Wink, M.R.; Jacques-Silva, M.C.; Delgado-Canedo, A.; Lenz, G.; Battastini, A.M.
Indomethacin stimulates activity and expression of ecto-5'-nucleotidase/CD73 in glioma cell lines
Eur. J. Pharmacol.
569
8-15
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kittel, A.; Sperlagh, B.; Pelletier, J.; Sevigny, J.; Kirley, T.L.
Transient changes in the localization and activity of ecto-nucleotidases in rat hippocampus following lipopolysaccharide treatment
Int. J. Dev. Neurosci.
25
275-282
2007
Rattus norvegicus
Manually annotated by BRENDA team
Pedrazza, E.L.; Senger, M.R.; Rico, E.P.; Zimmermann, F.F.; Pedrazza, L.; de Freitas Sarkis, J.J.; Bonan, C.D.
Fluoxetine and nortriptyline affect NTPDase and 5'-nucleotidase activities in rat blood serum
Life Sci.
81
1205-1210
2007
Rattus norvegicus
Manually annotated by BRENDA team
Tamajusuku, A.S.; Carrillo-Sepulveda, M.A.; Braganhol, E.; Wink, M.R.; Sarkis, J.J.; Barreto-Chaves, M.L.; Battastini, A.M.
Activity and expression of ecto-5-nucleotidase/CD73 are increased by thyroid hormones in vascular smooth muscle cells
Mol. Cell. Biochem.
289
65-72
2006
Rattus norvegicus
Manually annotated by BRENDA team
Miron, V.R.; Bauermann, L.; Morsch, A.L.; Zanin, R.F.; Correa, M.; da Silva, A.C.; Mazzanti, C.; Morsch, V.M.; Lunkes, G.I.; Schetinger, M.R.
Enhanced NTPDase and 5'-nucleotidase activities in diabetes mellitus and iron-overload model
Mol. Cell. Biochem.
298
101-107
2007
Rattus norvegicus
Manually annotated by BRENDA team
Spanevello, R.M.; Mazzanti, C.M.; Kaizer, R.; Zanin, R.; Cargnelutti, D.; Hannel, L.; Correa, M.; Mazzanti, A.; Festugatto, R.; Graca, D.; Schetinger, M.R.; Morsch, V.M.
Apyrase and 5'-nucleotidase activities in synaptosomes from the cerebral cortex of rats experimentally demyelinated with ethidium bromide and treated with interferon-beta
Neurochem. Res.
31
455-462
2006
Rattus norvegicus
Manually annotated by BRENDA team
Delwing, D.; Delwing, D.; Goncalves, M.C.; Sarkis, J.J.; Wyse, A.T.
NTPDase and 5'-nucleotidase activities of synaptosomes from hippocampus of rats subjected to hyperargininemia
Neurochem. Res.
32
1209-1216
2007
Rattus norvegicus
Manually annotated by BRENDA team
Pochmann, D.; Innocente, A.M.; Cotomacci, G.; Barreto-Chaves, M.L.; Sarkis, J.J.
AMP hydrolysis in soluble and microsomal rat cardiac cell fractions: kinetic characterization and molecular identification of 5'-nucleotidase
Biosci. Rep.
28
267-273
2008
Rattus norvegicus
Manually annotated by BRENDA team
Pedrazza, E.L.; Rico, E.P.; Senger, M.R.; Pedrazza, L.; Zimmermann, F.F.; Sarkis, J.J.; Bogo, M.R.; Bonan, C.D.
Ecto-nucleotidase pathway is altered by different treatments with fluoxetine and nortriptyline
Eur. J. Pharmacol.
583
18-25
2008
Rattus norvegicus
Manually annotated by BRENDA team
Ruecker, B.; Almeida, M.E.; Libermann, T.A.; Zerbini, L.F.; Wink, M.R.; Sarkis, J.J.
E-NTPDases and ecto-5'-nucleotidase expression profile in rat heart left ventricle and the extracellular nucleotide hydrolysis by their nerve terminal endings
Life Sci.
82
477-486
2008
Rattus norvegicus
Manually annotated by BRENDA team
Bavaresco, L.; Bernardi, A.; Braganhol, E.; Cappellari, A.R.; Rockenbach, L.; Farias, P.F.; Wink, M.R.; Delgado-Canedo, A.; Battastini, A.M.
The role of ecto-5'-nucleotidase/CD73 in glioma cell line proliferation
Mol. Cell. Biochem.
319
61-68
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Fuerstenau, C.R.; Trentin, D.d.a..S.; Gossenheimer, A.N.; Ramos, D.B.; Casali, E.A.; Barreto-Chaves, M.L.; Sarkis, J.J.
Ectonucleotidase activities are altered in serum and platelets of L-NAME-treated rats
Blood Cells Mol. Dis.
41
223-229
2008
Rattus norvegicus
Manually annotated by BRENDA team
Braun, J.S.
Ecto-5'-nucleotidase-positive cells in the choroid and ciliary body of the rat eye
Anat. Rec. (Hoboken)
293
379-382
2010
Rattus norvegicus
Manually annotated by BRENDA team
Schmatz, R.; Mazzanti, C.M.; Spanevello, R.; Stefanello, N.; Gutierres, J.; Maldonado, P.A.; Correa, M.; da Rosa, C.S.; Becker, L.; Bagatini, M.; Goncalves, J.F.; Jaques, J.d.o.s..S.; Schetinger, M.R.; Morsch, V.M.
Ectonucleotidase and acetylcholinesterase activities in synaptosomes from the cerebral cortex of streptozotocin-induced diabetic rats and treated with resveratrol
Brain Res. Bull.
80
371-376
2009
Rattus norvegicus
Manually annotated by BRENDA team
Bjelobaba, I.; Stojiljkovic, M.; Lavrnja, I.; Stojkov, D.; Pekovic, S.; Dacic, S.; Laketa, D.; Rakic, L.; Nedeljkovic, N.
Regional changes in ectonucleotidase activity after cortical stab injury in rat
Gen. Physiol. Biophys.
28 Spec No
62-68
2009
Rattus norvegicus
Manually annotated by BRENDA team
El-Tayeb, A.; Iqbal, J.; Behrenswerth, A.; Romio, M.; Schneider, M.; Zimmermann, H.; Schrader, J.; Mueller, C.E.
Nucleoside-5'-monophosphates as prodrugs of adenosine A2A receptor agonists activated by ecto-5-nucleotidase
J. Med. Chem.
52
7669-7677
2009
Rattus norvegicus
Manually annotated by BRENDA team
Baqi, Y.; Lee, S.Y.; Iqbal, J.; Ripphausen, P.; Lehr, A.; Scheiff, A.B.; Zimmermann, H.; Bajorath, J.; Mueller, C.E.
Development of potent and selective inhibitors of ecto-5-nucleotidase based on an anthraquinone scaffold
J. Med. Chem.
53
2076-2086
2010
Rattus norvegicus
Manually annotated by BRENDA team
Shirley, D.G.; Vekaria, R.M.; Sevigny, J.
Ectonucleotidases in the kidney
Purinergic Signal.
5
501-511
2009
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Martin-Satue, M.; Lavoie, E.G.; Fausther, M.; Lecka, J.; Aliagas, E.; Kukulski, F.; Sevigny, J.
High expression and activity of ecto-5'-nucleotidase/CD73 in the male murine reproductive tract
Histochem. Cell Biol.
133
659-668
2010
Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
Manually annotated by BRENDA team
Bjelobaba, I.; Parabucki, A.; Lavrnja, I.; Stojkov, D.; Dacic, S.; Pekovic, S.; Rakic, L.; Stojiljkovic, M.; Nedeljkovic, N.
Dynamic changes in the expression pattern of ecto-5'-nucleotidase in the rat model of cortical stab injury
J. Neurosci. Res.
89
862-873
2011
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Iqbal, J.; Saeed, A.; Raza, R.; Matin, A.; Hameed, A.; Furtmann, N.; Lecka, J.; Sevigny, J.; Bajorath, J.
Identification of sulfonic acids as efficient ecto-5-nucleotidase inhibitors
Eur. J. Med. Chem.
70
685-691
2013
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Salman, S.; Vollmer, C.; McClelland, G.B.; Nurse, C.A.
Characterization of ectonucleotidase expression in the rat carotid body regulation by chronic hypoxia
Am. J. Physiol. Cell Physiol.
313
C274-C284
2017
Rattus norvegicus (P21588)
Manually annotated by BRENDA team
Adzic, M.; Nedeljkovic, N.
Unveiling the role of ecto-5'-nucleotidase/CD73 in astrocyte migration by using pharmacological tools
Front. Pharmacol.
9
153
2018
Rattus norvegicus
Manually annotated by BRENDA team
Eguchi, R.; Yamaguchi, S.; Otsuguro, K.I.
Fibroblast growth factor 2 modulates extracellular purine metabolism by upregulating ecto-5'-nucleotidase and adenosine deaminase in cultured rat spinal cord astrocytes
J. Pharmacol. Sci.
139
98-104
2018
Rattus norvegicus (P21588)
Manually annotated by BRENDA team
Miliutina, M.; Janke, J.; Hassan, S.; Zaib, S.; Iqbal, J.; Lecka, J.; Sevigny, J.; Villinger, A.; Friedrich, A.; Lochbrunner, S.; Langer, P.
A domino reaction of 3-chlorochromones with aminoheterocycles. Synthesis of pyrazolopyridines and benzofuropyridines and their optical and ecto-5'-nucleotidase inhibitory effects
Org. Biomol. Chem.
16
717-732
2018
Rattus norvegicus (P21588), Homo sapiens (P21589)
Manually annotated by BRENDA team
Doleski, P.H.; Mendes, R.E.; Leal, D.B.; Bottari, N.B.; Piva, M.M.; Da Silva, E.S.; Gabriel, M.E.; Lucca, N.J.; Schwertz, C.I.; Giacomim, P.; Morsch, V.M.; Schetinger, M.R.; Baldissera, M.D.; Da Silva, A.S.
Seric and hepatic NTPDase and 5'nucleotidase activities of rats experimentally infected by Fasciola hepatica
Parasitology
143
551-556
2016
Rattus norvegicus
Manually annotated by BRENDA team
Saeed, A.; Ejaz, S.; Shehzad, M.; Hassan, S.; Al-Rashida, M.; Lecka, J.; Sevigny, J.; Iqbal, J.
3-(5-(Benzylideneamino)thiazol-3-yl)-2H-chromen-2-ones A new class of alkaline phosphatase and ecto-5'-nucleotidase inhibitors
RSC Adv.
6
21026-21036
2016
Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team