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Information on EC 3.1.3.5 - 5'-nucleotidase and Organism(s) Homo sapiens and UniProt Accession P49902

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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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P49902
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
cytosolic 5'-nucleotidase II
-
type II cytosolic 5'-nucleotidase
-
5'-adenylic phosphatase
-
-
-
-
5'-AMP nucleotidase
-
-
-
-
5'-AMPase
-
-
-
-
5'-ectonucleotidase
-
-
5'-mononucleotidase
-
-
-
-
5'-nucleotidase
-
5'-nucleotidase I
-
5'-nucleotidase II
-
-
5'nucleotidase
-
-
-
-
adenosine 5'-monophosphatase
-
-
-
-
adenosine 5'-phosphatase
-
-
-
-
adenosine monophosphatase
-
-
-
-
AMP phosphatase
-
-
-
-
AMP phosphohydrolase
-
-
-
-
AMP-selective 5'-nucleotidase
-
-
AMPase
-
-
-
-
CD73 antigen
-
-
-
-
cN-III
-
-
cNIIIB nucleotidase
-
-
cytoplasmic 5'-nucleotidase II
-
-
cytoplasmic 5'-nucleotidase II (IMP-selective or GMP/IMP-selective)
-
-
cytoplasmic 5'-nucleotidase III
-
-
cytoplasmic 5'-nucleotidase-I (AMP-selective)
-
-
cytosolic 5'-nucleotidase
-
-
cytosolic 5'-nucleotidase II
-
-
E-5'-Nu
-
-
e5'-NT
-
-
e5'NT
ecto 5'-NT
-
-
ecto 5'-nucleotidase
-
-
ecto-5'-NT
ecto-5'-NT/CD73
-
-
ecto-5'-nucleotidase
ecto-5'-nucleotidase/CD73
-
-
ecto-5-NT
-
-
ecto-5-nucleotidase
-
-
ecto-nucleotidase
-
ectonucleotidase
-
ectonucleotidase CD73
-
-
high Km 5'-nucleotidase
-
-
high-Km 5'-NT
-
-
IMP 5'-nucleotidase
-
-
-
-
IMP-GMP specific nucleotidase
-
-
IMP-specific, high Km 5'-nucleotidase
-
-
IMP/GMP selective 5'-NT
-
-
membrane-bound 5'-nucleotidase
-
-
NT5C3A
-
-
P5'N-1
-
-
Phm8
-
-
Pho5
-
-
PN-1
-
-
PN-I
-
-
purine 5'-NT
-
-
purine 5'-nucleotidase
-
-
pyrimidine 5'-nucleotidase
-
-
Sdt1
-
-
snake venom 5'-nucleotidase
-
-
-
-
thymidine monophosphate nucleotidase
-
-
-
-
UMPase
-
-
-
-
UMPH-1
-
-
uridine 5'-nucleotidase
-
-
-
-
uridine monophosphate hydrolase-1
-
-
UshA
-
-
additional information
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
-
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
?
inosine + 5'-IMP
5'-IMP + inosine
show the reaction diagram
-
-
-
?
inosine + phosphate
5'-IMP + H2O
show the reaction diagram
-
-
-
r
ribavirin + 5'-IMP
?
show the reaction diagram
better substrate than viramidine
-
-
?
viramidine + 5'-IMP
?
show the reaction diagram
worse substrate than ribavirin
-
-
?
2'-chloro-2'-deoxyAMP + H2O
2'-chloro-2'-deoxyadenosine + phosphate
show the reaction diagram
-
cNII
-
-
?
2-chloro-2'-deoxyadenosine monophosphate + H2O
2-chloro-2'-deoxyadenosine + phosphate
show the reaction diagram
39% of the activity with 5'-AMP
-
?
3'-azido-3'deoxy-dTMP + H2O
3'-azido-3'-deoxythymidine + phosphate
show the reaction diagram
-
cNII
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
5'-dAMP + H2O
deoxyadenosine + phosphate
show the reaction diagram
5'-dCMP + H2O
2'-deoxycytidine + phosphate
show the reaction diagram
5'-dCMP + H2O
deoxycytidine + phosphate
show the reaction diagram
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
5'-dIMP + H2O
deoxyinosine + phosphate
show the reaction diagram
5'-dTMP + H2O
deoxythymidine + phosphate
show the reaction diagram
5'-dUMP + H2O
deoxyuridine + phosphate
show the reaction diagram
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
5'-TMP + H2O
thymidine + phosphate
show the reaction diagram
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
5'-XMP + H2O
xanthosine + phosphate
show the reaction diagram
5-fluoro-dUMP + H2O
5-fluoro-uridine + phosphate
show the reaction diagram
-
cNII
-
-
?
7-methylguanosine diphosphate + H2O
7-methylguanosine monophosphate + phosphate
show the reaction diagram
-
preferred substrate
-
-
?
7-methylguanosine monophosphate + H2O
7-methylguanosine + phosphate
show the reaction diagram
-
preferred substrate
-
-
?
9-beta-D-arabinosyl-2-fluoroadenine monophosphate + H2O
9-beta-D-arabinosyl-2-fluoroadenine + phosphate
show the reaction diagram
-
-
-
-
?
a 5'-ribonucleotide + H2O
a ribonucleoside + phosphate
show the reaction diagram
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
dAMP + H2O
deoxyadenosine + phosphate
show the reaction diagram
91% of the activity with 5'-AMP
-
?
dCMP + H2O
deoxycytidine + phosphate
show the reaction diagram
10% of the activity with 5'-AMP
-
?
dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
75% of the activity with 5'-AMP
-
?
dIMP + H2O
deoxyinosine + phosphate
show the reaction diagram
84% of the activity with 5'-AMP
-
?
dUMP + H2O
deoxyuridine + phosphate
show the reaction diagram
7% of the activity with 5'-AMP
-
?
FAD + H2O
?
show the reaction diagram
-
microsomal enzyme
-
-
?
IMP + H2O
inosine + phosphate
show the reaction diagram
-
-
-
-
?
methylthio-IMP + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
thio-GMP + H2o
6-thioguanosine + phosphate
show the reaction diagram
-
-
-
-
?
thio-IMP + H2O
6-thioinosine + 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
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dCMP + H2O
2'-deoxycytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
show the reaction diagram
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
5'-XMP + H2O
xanthosine + phosphate
show the reaction diagram
-
-
-
-
?
a 5'-ribonucleotide + H2O
a ribonucleoside + phosphate
show the reaction diagram
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
IMP + H2O
inosine + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
1 mM used in assay conditions
Mn2+
-
-
Zn2+
60% recovery of initial activity with EDTA-treated enzyme
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(6-deoxy-6-phosphono-beta-D-allofuranosyl)-5-(2-(E)-phenylvinyl)-cytosine
-
1-(6-deoxy-6-phosphono-beta-D-allofuranosyl)-5-phenyl-cytosine
-
1-(6-deoxy-6-phosphono-beta-D-allofuranosyl)-cytosine
-
beta-gamma-methylene-ATP
-
(2E)-5-(5-methylfuran-2-yl)-N-(2-methylphenyl)-3-oxo-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-2,3-dihydro-5H-[1,3]thiazolo[3,2-a]pyrimidine-6-carboxamide
67% inhibition at 0.005 mM
(2Z)-2-[[3-(3-fluoro-4-methoxyphenyl)-1-phenyl-1H-pyrazol-4-yl]methylidene]-6-[(4-methylphenyl)methyl]-7H-[1,3]thiazolo[3,2-b][1,2,4]triazine-3,7(2H)-dione
61% inhibition at 0.005 mM
1-amino-4-bromo-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
-
-
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
-
2,2'-(2-(2-((2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-carboxamido)ethylamino)-2-oxoethylazanediyl) diacetic acid
nucleotide-derived inhibitor
2,3,5-tri-O-benzyl-1-O-(4-nitrobenzoyl)-D-arabinofuranose
68% inhibition at 0.005 mM
2-((4'-cyano-4,4''-dimethoxy-[1,1':3',1''-terphenyl]-5'-yl)thio)-N-(3-cyano-4,5,6,7-tetrahydrobenzo[b]thiophen-2-yl)acetamide
73% inhibition at 0.005 mM
2-(3,4-dihydroisoquinolin-2(1H)-yl)-N-[4-[1-(4-methylbenzoyl)-2,3-dihydro-1H-indol-5-yl]-5-sulfanyl-1,3-thiazol-2-yl]acetamide
74% inhibition at 0.005 mM
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
-
2-chloro-N-(pyridin-4-yl)benzamide
-
2-fluoroadenine-9-beta-D-arabinofuranoside
1 mM, 70% inhibition with 5 mM 5'-AMP as substrate
2-methyl-N-(pyridin-4-yl)benzamide
-
2-nitro-N-(pyridin-4-yl)benzamide
-
2-phenyl-N-(pyridin-4-yl)acetamide
-
3,4,5-trimethoxy-N-(pyridin-4-yl)benzamide
-
3,5-dinitro-N-(pyridine-4-yl)benzamide
-
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-(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
-
-
3-chloro-N-(pyridin-4-yl)benzamide
-
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
-
3-methyl-N-(pyridin-4-yl)benzamide
-
3-nitro-N-(pyridin-4-yl)benzamide
-
3-[4,5-di([1,1'-biphenyl]-4-yl)-1H-imidazol-2-yl]-1H-indole
93% inhibition at 0.005 mM
4-(3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzenesulfonic acid
-
compound shows high cytotoxicity on H157 cells, with about 72% at 100 mM final concentration
4-(4-[1-[(3-chlorophenyl)methyl]-4-hydroxy-1H-[1,2,3]triazolo[4,5-c]pyridin-6-yl]piperidine-1-sulfonyl)-N-cycloheptylbenzene-1-sulfonamide
63% inhibition at 0.005 mM
4-(6-[[2-(4-aminophenyl)-1H-benzimidazol-5-yl]methyl]-1H-benzimidazol-2-yl)aniline
78% inhibition at 0.005 mM
4-chloro-N-(pyridin-4-yl)benzamide
-
4-methyl-N-(pyridin-4-yl)benzamide
-
4-nitro-N-(pyridin-4-yl)benzamide
-
5'-deoxy-5'-S-isobutylthioadenosine
-
-
5'-deoxy-7-methyl-5'-(4-phosphono-1H-pyrazol-1-yl)guanosine
-
moderately potent inhibitor
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
-
5-ethynyldideoxyuridine
-
selective inhibitor
6-(4-ethoxyphenyl)-3-(4-methylphenyl)-N-(2-phenylethyl)-1H-pyrazolo[3,4-b]pyridine-4-carboxamide
65% inhibition at 0.005 mM
6-amino-4-hydroxynaphthalene-2-sulfonic acid
-
most potent inhibitor of the screen
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
-
6-N,N-diethyl-D-beta-gamma-dibromomethylene adenosine triphosphate
originally named FPL 67156 or ARL 67156, 28% inhibition at 0.1 mM
6-Thiopurine
-
-
7-methoxy-3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
adenosine 5'-(alpha,beta-methylene)diphosphate
adenosine 5'-(alpha,beta-methylene)triphosphate
-
-
alpha,beta-methylene adenosine 5'-diphosphate
-
specific inhibitor
alpha,beta-methylene adenosine-5'-diphosphate
-
-
alpha,beta-methylene-ADP
alpha-beta-methylene-ADP
-
alpha/beta-methylene-ADP
-
a specific CD73 inhibitor
araCMP
1 mM, 25% inhibition with 5 mM 5'-AMP as substrate
concanavalin A
-
Cu2+
further inhibition of the residual activity in EDTA-treated enzyme
dADP
-
-
dATP
-
-
dCTP
-
-
dGDP
-
-
dGTP
-
-
dITP
-
-
dUTP
-
-
ethyl 4-(2-((4'-cyano-4''-methoxy-4-methyl-[1,1':3',1''-terphenyl]-5'-yl)thio)acetamido)benzoate
80% inhibition at 0.005 mM
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-sulfanylidene-1,2,3,4-tetrahydropyrimidine-5-carboxylate
monastrol
ethyl 4-[4-(dimethylamino)phenyl]-6-methyl-2-sulfanylidene-1,2,3,4-tetrahydropyrimidine-5-carboxylate
LaSOM 63
Fe2+
further inhibition of the residual activity in EDTA-treated enzyme
Ly-294002
-
0.01 mM LY-294002 abolishes lipopolysaccharide-induced ecto-5'-nucleotidase activity
MEDI9447
non-competitive inhibitor
-
myricetin
-
N-(4-(4-methoxyphenyl)thiazol-2-yl)acrylamide
-
selective inhibitor
N-(4-methylcyclohexyl)-1-(2-phenyl-1H-benzimidazole-5-sulfonyl)piperidine-3-carboxamide
17% inhibition at 0.005 mM
N-(pyridin-4-yl)furan-2-carboxamide
-
N-[4-[5-([2-[2-(4-methoxybenzoyl)hydrazinyl]-2-oxoethyl]sulfanyl)-4-(4-methoxyphenyl)-4H-1,2,4-triazol-3-yl]phenyl]-4-methylbenzene-1-sulfonamide
64% inhibition at 0.005 mM
NAD+
-
-
NADH
-
-
NADP+
-
-
NADPH
-
-
pentoxifillin
-
-
phosphate
-
-
quercetin
Reactive blue
-
Reactive blue 2
-
sodium 1-amino-4-(2-carboxy-4-fluoroanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
PSB-0952
sodium 1-amino-4-anilino-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
AB-25
sodium 1-amino-4-[(anthracen-2-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
PSB-0963
sulfamic acid
Sulfanilic acid
-
tenascin C
-
thio-IMP
-
substrate inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
diadenosine polyphosphate
allosteric activation
-
2,3-bisphosphoglycerate
2,3-diphosphoglycerate
-
activation
ammonium pyrrolidin dithiocarbamate
-
0.01 mM ammonium pyrrolidin dithiocarbamate increases the basal activity of ecto-5'-nucleotidase by 17% but has no effect on the lipopolysaccharide-induced increase in ecto-5'-nucleotidase activity
D-fructose
-
the activity of 5'-nucleotidase increases with increasing D-fructose concentrations (5-30 mM) in diabetic patients
D-glucose
-
the activity of 5'-nucleotidase increases with increasing D-glucose concentrations (5-30 mM) in diabetic patients
diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
Diadenosine tetraphosphate
-
activates cytosolic 5'-nucleotidase II by increase binding and dimer formation, interface binding structure modeling
indomethacin
-
0.1 mM, causes 62% increase of activity in vivo after 48 h
lipopolysaccharide
-
ecto-5'-nucleotidase activity increases after incubation with 10 ng/ml lipopolysaccharide for 24 h but is not changed after shorter incubation times
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8 - 2.17
Inosine
0.024 - 0.095
ribavirin
0.0038 - 2.96
5'-AMP
0.002 - 0.0564
5'-CMP
0.035 - 0.114
5'-dAMP
0.023
5'-dCMP
-
-
0.044
5'-dGMP
-
-
0.057
5'-dIMP
-
-
0.017
5'-dUMP
-
-
0.0065 - 0.017
5'-GMP
0.0071 - 12.11
5'-IMP
0.008
5'-TMP
37°C, pH not specified in the publication
0.014 - 0.0316
5'-UMP
0.065
5'-XMP
-
-
10
9-beta-D-arabinosyl-2-fluoroadenine monophosphate
-
pH 8.3, 25°C
0.0091
AMP
-
at pH 8.5
0.012 - 0.193
dCMP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19 - 22
Inosine
0.023 - 0.15
ribavirin
187
5'-AMP
37°C, pH not specified in the publication
202
5'-CMP
37°C, pH not specified in the publication
174
5'-dAMP
37°C, pH not specified in the publication
132
5'-GMP
37°C, pH not specified in the publication
104
5'-IMP
37°C, pH not specified in the publication
40
5'-TMP
37°C, pH not specified in the publication
289
5'-UMP
37°C, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48800
5'-AMP
37°C, pH not specified in the publication
3600
5'-CMP
37°C, pH not specified in the publication
1500
5'-dAMP
37°C, pH not specified in the publication
20300
5'-GMP
37°C, pH not specified in the publication
14700
5'-IMP
37°C, pH not specified in the publication
5000
5'-TMP
37°C, pH not specified in the publication
9100
5'-UMP
37°C, pH not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.14
1-(6-deoxy-6-phosphono-beta-D-allofuranosyl)-5-(2-(E)-phenylvinyl)-cytosine
pH 6.5, 37°C
2.01
1-(6-deoxy-6-phosphono-beta-D-allofuranosyl)-5-phenyl-cytosine
pH 6.5, 37°C
1.74
1-(6-deoxy-6-phosphono-beta-D-allofuranosyl)-cytosine
pH 6.5, 37°C
0.0013
(2E)-5-(5-methylfuran-2-yl)-N-(2-methylphenyl)-3-oxo-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-2,3-dihydro-5H-[1,3]thiazolo[3,2-a]pyrimidine-6-carboxamide
at pH 7.0 and 37°C
0.0172
2,3,5-tri-O-benzyl-1-O-(4-nitrobenzoyl)-D-arabinofuranose
at pH 7.0 and 37°C
0.0012
2-((4'-cyano-4,4''-dimethoxy-[1,1':3',1''-terphenyl]-5'-yl)thio)-N-(3-cyano-4,5,6,7-tetrahydrobenzo[b]thiophen-2-yl)acetamide
at pH 7.0 and 37°C
0.00122
2-(3,4-dihydroisoquinolin-2(1H)-yl)-N-[4-[1-(4-methylbenzoyl)-2,3-dihydro-1H-indol-5-yl]-5-sulfanyl-1,3-thiazol-2-yl]acetamide
at pH 7.0 and 37°C
0.00053
3-[4,5-di([1,1'-biphenyl]-4-yl)-1H-imidazol-2-yl]-1H-indole
at pH 7.0 and 37°C
0.00046
4-(4-[1-[(3-chlorophenyl)methyl]-4-hydroxy-1H-[1,2,3]triazolo[4,5-c]pyridin-6-yl]piperidine-1-sulfonyl)-N-cycloheptylbenzene-1-sulfonamide
at pH 7.0 and 37°C
0.0061
4-(6-[[2-(4-aminophenyl)-1H-benzimidazol-5-yl]methyl]-1H-benzimidazol-2-yl)aniline
at pH 7.0 and 37°C
0.0027
6-(4-ethoxyphenyl)-3-(4-methylphenyl)-N-(2-phenylethyl)-1H-pyrazolo[3,4-b]pyridine-4-carboxamide
at pH 7.0 and 37°C
0.00091
ADP
pH and temperature not specified in the publication
0.00051
alpha,beta-methylene-ADP
-
in 10 mM HEPES (pH 7.4), 2 mM MgCl2, and 1 mM CaCl2
0.00068
ethyl 4-(2-((4'-cyano-4''-methoxy-4-methyl-[1,1':3',1''-terphenyl]-5'-yl)thio)acetamido)benzoate
at pH 7.0 and 37°C
0.0011
myricetin
pH and temperature not specified in the publication
0.00939
N-(4-methylcyclohexyl)-1-(2-phenyl-1H-benzimidazole-5-sulfonyl)piperidine-3-carboxamide
at pH 7.0 and 37°C
0.0049
N-[4-[5-([2-[2-(4-methoxybenzoyl)hydrazinyl]-2-oxoethyl]sulfanyl)-4-(4-methoxyphenyl)-4H-1,2,4-triazol-3-yl]phenyl]-4-methylbenzene-1-sulfonamide
at pH 7.0 and 37°C
0.0014
quercetin
pH and temperature not specified in the publication
0.00026
sodium 1-amino-4-(2-carboxy-4-fluoroanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
pH and temperature not specified in the publication
0.00015
sodium 1-amino-4-[(anthracen-2-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
1-amino-4-bromo-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
Homo sapiens
-
pH 7.4, 37°C
0.0137
1-pentyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Homo sapiens
at pH 7.5 and 37°C
0.00921
1-tert-butyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Homo sapiens
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
Homo sapiens
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
Homo sapiens
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
Homo sapiens
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00326
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Homo sapiens
at pH 7.5 and 37°C
0.00263
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
Homo sapiens
at pH 7.5 and 37°C
0.00032
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Homo sapiens
at pH 7.5 and 37°C
0.00346
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
Homo sapiens
at pH 7.5 and 37°C
0.00573
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Homo sapiens
at pH 7.5 and 37°C
0.0105
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
Homo sapiens
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
Homo sapiens
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00077
2-chloro-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0112
2-methyl-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00038
2-nitro-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00041
2-phenyl-N-(pyridin-4-yl)acetamide
Homo sapiens
pH and temperature not specified in the publication
0.00307
3,4,5-trimethoxy-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00554
3,5-dinitro-N-(pyridine-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00463
3,8-dimethyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Homo sapiens
at pH 7.5 and 37°C
0.00566
3,8-dimethyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Homo sapiens
at pH 7.5 and 37°C
0.0102
3-(2-(3,4,5-trimethoxybenzylideneamino)thiazol-4-yl)-2Hchromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.00223
3-(2-(3-chlorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.00041
3-(2-(3-methoxy-4-phenoxybenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.00025
3-(2-(3-nitrobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.000438
3-(2-(4-bromobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.00028
3-(2-(4-chlorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.00515
3-(2-(4-fluorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.00092
3-(2-(furan-2-ylmethyleneamino)thiazol-4-yl)-2H-chromen-2-one
Homo sapiens
-
at pH 7.4 and 37°C
0.00411
3-chloro-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00732
3-methyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Homo sapiens
at pH 7.5 and 37°C
0.0111
3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Homo sapiens
at pH 7.5 and 37°C
0.00025
3-methyl-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00109
3-nitro-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0061
4-(3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzenesulfonic acid
Homo sapiens
-
pH 7.4, 37°C
0.00029
4-chloro-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00171
4-methyl-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00042
4-nitro-N-(pyridin-4-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0878
5'-deoxy-7-methyl-5'-(4-phosphono-1H-pyrazol-1-yl)guanosine
Homo sapiens
-
at pH 7.5 and 30°C
0.1
5-chloro-3-methyl-1-phenyl-6-(2-propoxyphenyl)-1H-pyrazolo[3,4-b]pyridine
Homo sapiens
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
Homo sapiens
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
Homo sapiens
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0103
5-chloro-6-(2-hydroxyphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
Homo sapiens
at pH 7.5 and 37°C
0.0184
5-chloro-6-(2-methoxyphenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
Homo sapiens
at pH 7.5 and 37°C
0.02
5-ethynyldideoxyuridine
Homo sapiens
-
-
0.00132
6-amino-4-hydroxynaphthalene-2-sulfonic acid
Homo sapiens
-
pH 7.4, 37°C
0.0171
6-chloro-7-(2-hydroxy-5-methylphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
at pH 7.5 and 37°C
0.00129
6-chloro-7-(2-hydroxyphenyl)-1-methylpyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
at pH 7.5 and 37°C
0.00521
6-chloro-7-(2-hydroxyphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
at pH 7.5 and 37°C
0.0124
7-methoxy-3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Homo sapiens
at pH 7.5 and 37°C
0.00792
N-(pyridin-4-yl)furan-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0453
quercetin
Homo sapiens
-
pH 7.4, 37°C
0.0421
sulfamic acid
0.0421
Sulfanilic acid
Homo sapiens
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17.1
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
microsomal enzyme
6.5
-
cytoplasmic enzyme, substrate 5'-IMP
7
-
substrate thio-IMP
7.5
-
substrates IMP, methylthio-IMP
8
-
substrate thio-GMP
8.5
-
substrates GMP, AMP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
bronchial epithelium, mucosal and serosal epithelial surface
Manually annotated by BRENDA team
-
patients with head and neck cancer
Manually annotated by BRENDA team
-
5'-nucleotidase activity is decreased in seminal plasma from varicocele patients
Manually annotated by BRENDA team
-
5'-nucleotidase activity is decreased in spermatozoa from varicocele patients
Manually annotated by BRENDA team
-
CD73
Manually annotated by BRENDA team
-
CD73 is a lymphocyte surface antigen
Manually annotated by BRENDA team
-
CD73
Manually annotated by BRENDA team
-
the enzyme contributes to function of endothelial cells by inhibiting platelet aggregation in cooperation with ATP diphosphohydrolase, which degrades ADP to AMP
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the nucleotide salvage pathway is regulated at a molecular level
physiological function
cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates and participates in the regulation of purine nucleotide pools within the cell
malfunction
metabolism
-
5'-nucleotidases are involved in the purine and pyrimidine nucleotide metabolic pathways, overview. CD73 enzymatic activity is implicated in two major extracellular metabolic pathways with distinct physiological roles, extracellular adenosine nucleotide and NAD+ metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
5NTC_HUMAN
561
0
64970
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
-
195000
-
gel filtration
210000
-
gel filtration
47700
x * 47700, calculation from nucleotide sequence
53000
-
4 * 53000, cytoplasmic enzyme, SDS-PAGE
56000
-
x * 56000, membrane-bound enzyme, deglycosylated, SDS-PAGE
57000
-
SDS-PAGE
57300
-
4 * 57300, calculated from amino acid sequence
58000
-
x * 67000, glycosylated enzyme form, x * 58000, deglycosylated enzyme form, SDS-PAGE
65000
x * 65000, truncated form of enzyme
67000
-
x * 67000, glycosylated enzyme form, x * 58000, deglycosylated enzyme form, SDS-PAGE
70000
-
SDS-PAGE
71000
-
homodimeric CD73
73000
-
x * 73000, membrane-bound enzyme, SDS-PAGE under reducing conditions
74000
-
x * 74000, microsomal enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
cN-II functions as a tetramer forming a dimer of dimers, structural basis for the allosteric regulation and substrate recognition of cytosolic 5-nucleotidase II, overview. The effector binding site, corresponding to effector site 1, is located close to one of the subunit interfaces where the effector takes part in subunit-subunit interactions by forming electrostatic interactions between the effector phosphates and the positively charged residues of each subunit
dimer
-
-
homodimer
-
CD73
homotetramer
-
4 * 57300, calculated from amino acid sequence
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structures of the inactive D52N mutant enzyme in apoform or in complexes with 1. 2,3-bisphosphoglycerate, 2. IMP/ATP, 3. IMP/2,3-bisphosphoglycerate, 4. GMP/diadenosine tetraphosphate, 5. dGMP/dATP, or 6. UMP/ATP, overview. Crystallization by sitting drop vapor diffusion method with sitting drops of 300 nl at a protein solution/reservoir solution ratio of 2:1, the reservoir solution contains 0.1 M bicine, pH 9.0, and 10% w/v PEG 6000, with 20 mM MgCl2, 10 mM dATP, and 10 mM dGMP added to the protein solution, 7.7 mg/ml protein, 1-2 weeks at 4°C, to obtain the enzyme complexes the crystals are soaked in 0.01 ml drops of reservoir solution supplemented with 10 mM of the corresponding substrate/activator and 20 mM MgCl2 for 90 min, X-ray diffraction structure determination and analysis at A resolution
molecular modeling study using inhibitor 1-(6-deoxy-6-phosphono-beta-D-allofuranosyl)-5-(2-(E)-phenylvinyl)-cytosine
in complex with adenosine, inhibitors 2,2'-(2-(2-((2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-carboxamido)ethylamino)-2-oxoethylazanediyl) diacetic acid, baicalin and ADP analog AMPCP. The dimeric enzyme undergoes an extensive 114° conformational switch between the open and closed forms. The dimerization interface is formed by the C-terminal domains and exhibits interchain motions of up to 13°. Structural control of the domain movement determines the selectivity for monophosphate nucleotides
sitting drop vapour diffusion method with 1.8 M of MgSO4 and 0.1 M of Tris, pH 8.5
-
soluble form of human soluble CD73 at 2.2 A resolution, a truncated form of CD73, residues 27–549, that retains ecto-5'-nucleotidase activity. Structure reveals a conserved loop that is directly involved in the dimer-dimer interaction showing that the two subunits of the dimer are not linked by disulfide bridges
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D52N
site-directed mutagenesis, catalytically inactive active site residue
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
-
30 min, 44% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose bead chromatography
recombinant enzyme
HisTrap column chromatography
HisTrap column chromatography and Superdex 75 gel filtration
-
Ni2+-charged His-Trap HP column chromatography and HiLoad 16/60 Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain Y187 and Escherichia coli BL21 (DE3) cells
expression of mutant D52N in Escherichia coli strain BL21(DE)-R3-pRARE2
expressed in COS-7 cells
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) RIL cells
-
expressed in Escherichia coli Rosetta2(DE) cells
-
expressed in Sf9 insect cells
expression in Sf9 insect cells
gene NT5E at 6q14-q21 encodes CD73
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the addition of ponasterone leads to overexpression of the enzyme assayed as phosphotransferase in an exposure time-dependent manner
CD73 is highly induced by ischemia and hypoxia, and increased expression in cardiac ischemia is mediated by a positive feedback loop involving adenosine. Though CD73 is mainly regulated transcriptionally, cross linking of CD38, a cell surface glycoprotein with cyclic ADP-ribose hydrolase activity, causes upregulation of CD73 via export of protein to the cell surface that is independent of new transcription
-
enzyme expression is higher in papillary thyroid carcinoma cells than in the adjacent non-malignant thyroid tissue
markedly increased in the ventricular myocardium in patients with chronic heart failure
-
the expression of the enzyme is high in breast cancer tissues and increases with advanced tumor grades and lympho-node status
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, R.S.F.; Ford, H.C.
5'-Nucleotidase of human placental trophoblastic microvilli possesses cobalt-stimulated FAD pyrophosphatase activity
J. Biol. Chem.
263
14878-14883
1988
Homo sapiens
Manually annotated by BRENDA team
Spychala, J.; Madrid-Marina, V.; Fox, I.H.
High Km soluble 5'-nucleotidase from human placenta. Properties and allosteric regulation by IMP and ATP
J. Biol. Chem.
263
18759-18765
1988
Homo sapiens
Manually annotated by BRENDA team
Madrid-Marina, V.; Fox, I.H.
Human placental cytoplasmic 5'-nucleotidase. Kinetic properties and inhibition
J. Biol. Chem.
261
444-452
1986
Homo sapiens
Manually annotated by BRENDA team
Klemens, M.R.; Sherman, W.R.; Holmberg, N.J.; Ruedi, J.M.; Low, M.G.; Thompson, L.F.
Characterization of soluble vs membrane-bound human placental 5'-nucleotidase
Biochem. Biophys. Res. Commun.
172
1371-1377
1990
Homo sapiens
Manually annotated by BRENDA team
Lee, R.S.F.; Ford, H.C.
Purification and characterization of 5'-nucleotidase/FAD pyrophosphatase from human placenta
Methods Enzymol.
280
424-436
1997
Homo sapiens
Manually annotated by BRENDA team
Flocke, K.; Mannherz, H.G.
Isolation and characterization of 5'-nucleotidase of a human pancreatic tumor cell line
Biochim. Biophys. Acta
1076
273-281
1991
Homo sapiens
Manually annotated by BRENDA team
Kalsi, K.K.; Lawson, C.; McCormack, A.; Kochan, Z.; Yacoub, M.H.; Smolenski, R.T.
TNF-a reduces the activity of ecto-5'-nucleotidase in human endothelial cells
Adv. Exp. Med. Biol.
486
149-152
2000
Homo sapiens
Manually annotated by BRENDA team
Trifilo, M.; Page, T.
NAPDD patients exhibit altered electrophoretic mobility of cytosolic 5' nucleotidase
Adv. Exp. Med. Biol.
486
87-90
2000
Homo sapiens
Manually annotated by BRENDA team
Kawashima, Y.; Nagasawa, T.; Ninomiya, H.
Contribution of ecto-5'-nucleotidase to the inhibition of platelet aggregation by human endothelial cells
Blood
96
2157-2162
2000
Homo sapiens
Manually annotated by BRENDA team
Hunsucker, S.A.; Spychala, J.; Mitchell, B.S.
Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance
J. Biol. Chem.
276
10498-10504
2001
Homo sapiens (Q9BXI3), Homo sapiens
Manually annotated by BRENDA team
Picher, M.; Burch, L.H.; Hirsh, A.J.; Spychala, J.; Boucher, R.C.
Ecto 5'-nucleotidase and nonspecific alkaline phosphatase. Two-AMP-hydrolyzing ectoenzymes with distinct roles in human airways
J. Biol. Chem.
278
13468-13479
2003
Homo sapiens
Manually annotated by BRENDA team
Wu, J.Z.; Larson, G.; Walker, H.; Shim, J.H.; Hong, Z.
Phosphorylation of ribavirin and viramidine by adenosine kinase and cytosolic 5'-nucleotidase II: Implications for ribavirin metabolism in erythrocytes
Antimicrob. Agents Chemother.
49
2164-2171
2005
Homo sapiens (P49902)
Manually annotated by BRENDA team
Hanisch, F.; Hellsten, Y.; Zierz, S.
Ecto- and cytosolic 5'-nucleotidases in normal and AMP deaminase-deficient human skeletal muscle
Biol. Chem.
387
53-58
2006
Homo sapiens
Manually annotated by BRENDA team
Brouwer, C.; Vogels-Mentink, T.M.; Keizer-Garritsen, J.J.; Trijbels, F.J.; Bokkerink, J.P.; Hoogerbrugge, P.M.; van Wering, E.R.; Veerman, A.J.; De Abreu, R.A.
Role of 5'-nucleotidase in thiopurine metabolism: enzyme kinetic profile and association with thio-GMP levels in patients with acute lymphoblastic leukemia during 6-mercaptopurine treatment
Clin. Chim. Acta
361
95-103
2005
Homo sapiens
Manually annotated by BRENDA team
Borowiec, A.; Lechward, K.; Tkacz-Stachowska, K.; Skladanowski, A.C.
Adenosine as a metabolic regulator of tissue function: production of adenosine by cytoplasmic 5'-nucleotidases
Acta Biochim. Pol.
53
269-278
2006
Homo sapiens
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
Braganhol, E.; Tamajusuku, A.S.; Bernardi, A.; Wink, M.R.; Battastini, A.M.
Ecto-5'-nucleotidase/CD73 inhibition by quercetin in the human U138MG glioma cell line
Biochim. Biophys. Acta
1770
1352-1359
2007
Homo sapiens
Manually annotated by BRENDA team
Levesque, S.A.; Lavoie, E.G.; Lecka, J.; Bigonnesse, F.; Sevigny, J.
Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases
Br. J. Pharmacol.
152
141-150
2007
Homo sapiens (Q53Z63), Homo sapiens
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
Wallden, K.; Stenmark, P.; Nyman, T.; Flodin, S.; Graeslund, S.; Loppnau, P.; Bianchi, V.; Nordlund, P.
Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition
J. Biol. Chem.
282
17828-17836
2007
Homo sapiens
Manually annotated by BRENDA team
Sadej, R.; Spychala, J.; Skladanowski, A.C.
Expression of ecto-5'-nucleotidase (eN, CD73) in cell lines from various stages of human melanoma
Melanoma Res.
16
213-222
2006
Homo sapiens
Manually annotated by BRENDA team
Jordheim, L.P.; Cros, E.; Galmarini, C.M.; Dumontet, C.; Bretonnet, A.; Krimm, I.; Lancelin, J.; Gagnieu, M.
F-ara-AMP is a substrate of cytoplasmic 5'-nucleotidase II (cN-II): HPLC and NMR studies of enzymatic dephosphorylation
Nucleosides Nucleotides Nucleic Acids
25
289-297
2006
Homo sapiens
Manually annotated by BRENDA team
Zhou, X.; Zhi, X.; Zhou, P.; Chen, S.; Zhao, F.; Shao, Z.; Ou, Z.; Yin, L.
Effects of ecto-5'-nucleotidase on human breast cancer cell growth in vitro and in vivo
Oncol. Rep.
17
1341-1346
2007
Homo sapiens
Manually annotated by BRENDA team
Li, R.W.; Man, R.Y.; Vanhoutte, P.M.; Leung, G.P.
Stimulation of ecto-5'-nucleotidase in human umbilical vein endothelial cells by lipopolysaccharide
Am. J. Physiol. Heart Circ. Physiol.
295
H1177-H1181
2008
Homo sapiens
Manually annotated by BRENDA team
Sadej, R.; Inai, K.; Rajfur, Z.; Ostapkowicz, A.; Kohler, J.; Skladanowski, A.C.; Mitchell, B.S.; Spychala, J.
Tenascin C interacts with Ecto-5-nucleotidase (eN) and regulates adenosine generation in cancer cells
Biochim. Biophys. Acta
1782
35-40
2008
Homo sapiens
Manually annotated by BRENDA team
Careddu, M.G.; Allegrini, S.; Pesi, R.; Camici, M.; Garcia-Gil, M.; Tozzi, M.G.
Knockdown of cytosolic 5'-nucleotidase II (cN-II) reveals that its activity is essential for survival in astrocytoma cells
Biochim. Biophys. Acta
1783
1529-1535
2008
Homo sapiens
Manually annotated by BRENDA team
Lunkes, G.I.; Lunkes, D.S.; Leal, D.; Araujo, M.d.o..C.; Correa, M.; Becker, L.; Rosa, C.S.; Morsch, V.M.; Schetinger, M.R.
Effect of high glucose levels in human platelet NTPDase and 5'-nucleotidase activities
Diabetes Res. Clin. Pract.
81
351-357
2008
Homo sapiens
Manually annotated by BRENDA team
Johnson, S.M.
The importance of B-cells and ecto-5'nucleotidase in Mycoplasma fermentans infection and the relevance to rheumatoid arthritis
Immunology
123
187-196
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, L.; Zhou, X.; Zhou, T.; Ma, D.; Chen, S.; Zhi, X.; Yin, L.; Shao, Z.; Ou, Z.; Zhou, P.
Ecto-5'-nucleotidase promotes invasion, migration and adhesion of human breast cancer cells
J. Cancer Res. Clin. Oncol.
134
365-372
2008
Homo sapiens
Manually annotated by BRENDA team
Fini, C.; Coli, M.; Angelini, A.; Brusco, G.; Pasqualucci, P.; Tiziani, F.
5'-Nucleotidase activity is decreased in seminal plasma and spermatozoa from varicocele patients
J. Endocrinol. Invest.
31
666-671
2008
Homo sapiens
Manually annotated by BRENDA team
Roszkowska, A.; Klimek, J.; Kaletha, K.
Expression patterns of AMP-deaminase and cytosolic 5'-nucleotidase genes in human term placenta
Mol. Cell. Biochem.
311
249-251
2008
Homo sapiens
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
Mandapathil, M.; Szczepanski, M.J.; Szajnik, M.; Ren, J.; Lenzner, D.E.; Jackson, E.K.; Gorelik, E.; Lang, S.; Johnson, J.T.; Whiteside, T.L.
Increased ectonucleotidase expression and activity in regulatory T cells of patients with head and neck cancer
Clin. Cancer Res.
15
6348-6357
2009
Homo sapiens
Manually annotated by BRENDA team
Fujita, M.; Asakura, M.; Sanada, S.; Funaya, H.; Tsukamoto, O.; Komamura, K.; Asanuma, H.; Taketani, S.; Isomura, T.; Nakamaru, K.; Furukawa, H.; Sawa, Y.; Hori, M.; Kitakaze, M.
Activation of ecto-5'-nucleotidase in the blood and hearts of patients with chronic heart failure
J. Card. Fail.
14
426-430
2008
Homo sapiens
Manually annotated by BRENDA team
Wallden, K.; Nordlund, P.
Structural basis for the allosteric regulation and substrate recognition of human cytosolic 5-nucleotidase II
J. Mol. Biol.
408
684-696
2011
Homo sapiens (P49902), Homo sapiens
Manually annotated by BRENDA team
Bogan, K.; Brenner, C.
5'-Nucleotidases and their new roles in NAD+ and phosphate metabolism
New J. Chem.
34
845-853
2010
Corynebacterium glutamicum, Saccharomyces cerevisiae, Homo sapiens
-
Manually annotated by BRENDA team
Sadej, R.; Skladanowski, A.C.
Dual, enzymatic and non-enzymatic, function of ecto-5-nucleotidase (eN, CD73) in migration and invasion of A375 melanoma cells
Acta Biochim. Pol.
59
647-652
2012
Homo sapiens
Manually annotated by BRENDA team
Heuts, D.P.; Weissenborn, M.J.; Olkhov, R.V.; Shaw, A.M.; Gummadova, J.; Levy, C.; Scrutton, N.S.
Crystal structure of a soluble form of human CD73 with ecto-5-nucleotidase activity
ChemBioChem
13
2384-2391
2012
Homo sapiens (Q6NZX3), Homo sapiens
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
Meurillon, M.; Marton, Z.; Hospital, A.; Jordheim, L.P.; Bejaud, J.; Lionne, C.; Dumontet, C.; Perigaud, C.; Chaloin, L.; Peyrottes, S.
Structure-activity relationships of beta-hydroxyphosphonate nucleoside analogues as cytosolic 5-nucleotidase II potential inhibitors: synthesis, in vitro evaluation and molecular modeling studies
Eur. J. Med. Chem.
77
18-37
2014
Homo sapiens (P49902)
Manually annotated by BRENDA team
Pettengill, M.; Robson, S.; Tresenriter, M.; Millan, J.L.; Usheva, A.; Bingham, T.; Belderbos, M.; Bergelson, I.; Burl, S.; Kampmann, B.; Gelinas, L.; Kollmann, T.; Bont, L.; Levy, O.
Soluble ecto-5-nucleotidase (5-NT), alkaline phosphatase, and adenosine deaminase (ADA1) activities in neonatal blood favor elevated extracellular adenosine
J. Biol. Chem.
288
27315-27326
2013
Homo sapiens
Manually annotated by BRENDA team
Knapp, K.; Zebisch, M.; Pippel, J.; El-Tayeb, A.; Mueller, C.E.; Straeter, N.
Crystal structure of the human ecto-5-nucleotidase (CD73): insights into the regulation of purinergic signaling
Structure
20
2161-2173
2012
Homo sapiens (P21589), Homo sapiens
Manually annotated by BRENDA team
Spychala, J.; Chen, V.; Oka, J.; Mitchell, B.S.
ATP and phosphate reciprocally affect subunit association of human recombinant High Km 5'-nucleotidase. Role for the C-terminal polyglutamic acid tract in subunit association and catalytic activity
Eur. J. Biochem.
259
851-858
1999
Homo sapiens
Manually annotated by BRENDA team
Cividini, F.; Filoni, D.N.; Pesi, R.; Allegrini, S.; Camici, M.; Tozzi, M.G.
IMP-GMP specific cytosolic 5'-nucleotidase regulates nucleotide pool and prodrug metabolism
Biochim. Biophys. Acta
1850
1354-1361
2015
Homo sapiens (P49902), Homo sapiens
Manually annotated by BRENDA team
Hassan, S.; Ejaz, S.A.; Saeed, A.; Shehzad, M.; Ullah Khan, S.; Lecka, J.; Sevigny, J.; Shabir, G.; Iqbal, J.
4-Aminopyridine based amide derivatives as dual inhibitors of tissue non-specific alkaline phosphatase and ecto-5'-nucleotidase with potential anticancer activity
Bioorg. Chem.
76
237-248
2018
Homo sapiens (P21589)
Manually annotated by BRENDA team
Kozarski, M.; Kubacka, D.; Wojtczak, B.A.; Kasprzyk, R.; Baranowski, M.R.; Kowalska, J.
7-Methylguanosine monophosphate analogues with 5-(1,2,3-triazoyl) moiety Synthesis and evaluation as the inhibitors of cNIIIB nucleotidase
Bioorg. Med. Chem.
26
191-199
2018
Homo sapiens
Manually annotated by BRENDA team
Villamonte, M.L.; Torrejon-Escribano, B.; Rodriguez-Martinez, A.; Trapero, C.; Vidal, A.; Gomez de Aranda, I.; Sevigny, J.; Matias-Guiu, X.; Martin-Satue, M.
Characterization of ecto-nucleotidases in human oviducts with an improved approach simultaneously identifying protein expression and in situ enzyme activity
Histochem. Cell Biol.
149
269-276
2018
Homo sapiens (P21589)
Manually annotated by BRENDA team
Yu, J.; Wang, X.; Lu, Q.; Wang, J.; Li, L.; Liao, X.; Zhu, W.; Lv, L.; Zhi, X.; Yu, J.; Jin, Y.; Zou, Q.; Ou, Z.; Liu, X.; Zhou, P.
Extracellular 5'-nucleotidase (CD73) promotes human breast cancer cells growth through AKT/GSK-3beta/beta-catenin/cyclinD1 signaling pathway
Int. J. Cancer
142
959-967
2018
Homo sapiens (P21589), Homo sapiens
Manually annotated by BRENDA team
Shali, S.; Yu, J.; Zhang, X.; Wang, X.; Jin, Y.; Su, M.; Liao, X.; Yu, J.; Zhi, X.; Zhou, P.
Ecto-5'-nucleotidase (CD73) is a potential target of hepatocellular carcinoma
J. Cell. Physiol.
234
10248-10259
2018
Homo sapiens (P21589), Homo sapiens
Manually annotated by BRENDA team
Baqi, Y.
Ecto-nucleotidase inhibitors recent developments in drug discovery
Mini Rev. Med. Chem.
15
21-33
2015
Homo sapiens (P21589)
Manually annotated by BRENDA team
Bertoni, A.P.S.; Bracco, P.A.; de Campos, R.P.; Lutz, B.S.; Assis-Brasil, B.M.; Meyer, E.L.S.; Saffi, J.; Braganhol, E.; Furlanetto, T.W.; Wink, M.R.
Activity of ecto-5'-nucleotidase (NT5E/CD73) is increased in papillary thyroid carcinoma and its expression is associated with metastatic lymph nodes
Mol. Cell. Endocrinol.
479
54-60
2019
Homo sapiens (P21589), Homo sapiens
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
Rahimova, R.; Fontanel, S.; Lionne, C.; Jordheim, L.P.; Peyrottes, S.; Chaloin, L.
Identification of allosteric inhibitors of the ecto-5'-nucleotidase (CD73) targeting the dimer interface
PLoS Comput. Biol.
14
e1005943
2018
Homo sapiens (P21589)
Manually annotated by BRENDA team
Cividini, F.; Tozzi, M.G.; Galli, A.; Pesi, R.; Camici, M.; Dumontet, C.; Jordheim, L.P.; Allegrini, S.
Cytosolic 5'-nucleotidase II interacts with the leucin rich repeat of NLR family member Ipaf
PLoS ONE
10
e0121525
2015
Homo sapiens (P49902), Homo sapiens
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
Al-Haj, L.; Khabar, K.S.A.
The intracellular pyrimidine 5'-nucleotidase NT5C3A is a negative epigenetic factor in interferon and cytokine signaling
Sci. Signal.
11
eaal2434
2018
Homo sapiens
Manually annotated by BRENDA team