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2',3'-cyclic-AMP + H2O
adenosine + phosphate
2'-AMP + H2O
adenosine + phosphate
2'-UMP + H2O
deoxyuridine + phosphate
2-glycerophosphate + H2O
glycerol + phosphate
2-naphthol phosphate + H2O
2-naphthol + phosphate
3'-AMP + H2O
adenosine + phosphate
3'-CMP + H2O
cytidine + phosphate
3'-CMP + H2O
cytosine + phosphate
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
3'-dCMP + H2O
deoxycytidine + phosphate
3'-dTMP + H2O
deoxythymidine + phosphate
3'-dUMP + H2O
deoxyuridine + phosphate
3'-GMP + H2O
adenosine + phosphate
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
3'-UMP + H2O
uridine + phosphate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
5'-AMP + H2O
adenosine + phosphate
5'-AMP + H2O
guanosine + phosphate
-
-
-
?
5'-ATP + H2O
5'-ADP + phosphate
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
5'-dAMP + H2O
deoxyadenosine + phosphate
5'-dATP + H2O
?
-
i.e. 2'-deoxyadenosine 5'-triphosphate
-
-
?
5'-dCMP + H2O
2'-deoxycytidine + phosphate
-
-
-
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
5'-dCTP + H2O
?
-
i.e. 2'-deoxycytidine 5'-triphosphate
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
5'-dGTP + H2O
?
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
5'-dIMP + H2O
hypoxanthine + phosphate
-
YfbR
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
5'-dUMP + H2O
deoxyuridine + phosphate
5'-GMP + H2O
adenosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
5'-IMP + H2O
inosine + phosphate
5'-TMP + H2O
thymidine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
7-methylguanosine diphosphate + H2O
7-methylguanosine monophosphate + phosphate
-
less efficient substrate
-
-
?
7-methylguanosine monophosphate + H2O
7-methylguanosine + phosphate
-
preferred substrate
-
-
?
a nucleotide + H2O
a nucleoside + phosphate
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
Golgi-resident gPAPP protein has 3'-phosphoadenosine 5'-phosphate-phosphatase activity, functional role of gPAPP protein in the formation of skeletal elements through endochondral ossification in mice
-
-
?
ADP + H2O
adenosine + diphosphate
low activity
-
-
?
ADP + H2O
AMP + phosphate
AMP + H2O
adenosine + phosphate
ATP + H2O
ADP + phosphate
ATP + H2O
AMP + diphosphate
low activity
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CMP + H2O
cytosine + phosphate
CTP + H2O
CDP + phosphate
-
-
-
-
?
cyclic 3',5'-dTMP
?
-
lysosomal enzyme
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
?
dAMP + H2O
deoxyadenosine + phosphate
-
66% activity compared to AMP
-
-
?
dCMP + H2O
deoxycytosine + phosphate
-
12.1% activity compared to AMP
-
-
?
dGMP + H2O
deoxyguanosine + phosphate
-
49.9% activity compared to AMP
-
-
?
dIMP + H2O
deoxyinosine + phosphate
-
60.9% activity compared to AMP
-
-
?
dsDNA 3' phosphate + H2O
dsDNA + phosphate
GDP + H2O
GMP + phosphate
GMP + H2O
guanosine + phosphate
GTP + H2O
GDP + phosphate
IDP + H2O
IMP + phosphate
IMP + H2O
inosine + phosphate
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
polyphosphate + H2O
phosphate
-
SurE
-
-
?
TMP + H2O
thymidine + phosphate
-
15.2% activity compared to AMP
-
-
?
UDP + H2O
UMP + phosphate
UDP + H2O
uridine + diphosphate
best substrate, the enzyme shows some specificity for uridine nucleotides
-
-
?
UMP + H2O
uridine + phosphate
UTP + H2O
UDP + phosphate
UTP + H2O
UMP + diphosphate
the enzyme shows some specificity for uridine nucleotides
-
-
?
additional information
?
-
2',3'-cyclic-AMP + H2O

adenosine + phosphate
-
isozyme NSP-I: 3% of the activity with 5'-AMP, isozyme NSP-II: 1% of the activity with 5'-AMP
-
?
2',3'-cyclic-AMP + H2O
adenosine + phosphate
-
5% of the activity of 3'-AMP, cytosolic enzyme
-
?
2'-AMP + H2O

adenosine + phosphate
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
isozyme NSP-I: 52% of the activity with 5'-AMP, isozyme NSP-II: 54% of the activity with 5'-AMP
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
lysosomal enzyme
-
?
2'-AMP + H2O
adenosine + phosphate
-
68% of the activity of 3'-AMP, cytosolic enzyme
-
?
2'-UMP + H2O

deoxyuridine + phosphate
-
-
-
?
2'-UMP + H2O
deoxyuridine + phosphate
-
-
-
?
2-glycerophosphate + H2O

glycerol + phosphate
-
lysosomal enzyme
-
?
2-glycerophosphate + H2O
glycerol + phosphate
-
cytosolic enzyme
-
?
2-naphthol phosphate + H2O

2-naphthol + phosphate
-
-
-
?
2-naphthol phosphate + H2O
2-naphthol + phosphate
-
lysosomal enzyme
-
?
3'-AMP + H2O

adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
isozyme NSP-I: 59% of the activity with 5'-AMP, isozyme NSP-II: 54% of the activity with 5'-AMP
-
?
3'-AMP + H2O
adenosine + phosphate
-
most efficient substrate
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
3.2% of the activity with 5'-dUMP
-
-
-
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-CMP + H2O

cytidine + phosphate
-
-
-
?
3'-CMP + H2O
cytidine + phosphate
-
-
-
?
3'-CMP + H2O
cytidine + phosphate
-
2% of the activity with 5'-dUMP
-
?
3'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
3'-CMP + H2O

cytosine + phosphate
-
-
-
?
3'-CMP + H2O
cytosine + phosphate
-
-
-
-
?
3'-dAMP + H2O

3'-deoxyadenosine + phosphate
-
9.1% of the activity with 5'-dUMP
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
131% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 3'-phosphate
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 3'-phosphate
-
?
3'-dCMP + H2O

deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 3'-phosphate
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
6.5% of the activity with 5'-dUMP
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
101% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 3'-phosphate
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 3'-phosphate
-
?
3'-dTMP + H2O

deoxythymidine + phosphate
-
113.7% of the activity with 5'-dUMP
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
77% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dUMP + H2O

deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
-
-
-
-
3'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
153.5% of the activity with 5'-dUMP
-
?
3'-GMP + H2O

guanosine + phosphate
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
-
49% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
?
3'-UMP + H2O

uridine + phosphate
-
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
122.8% of the activity with 5'-dUMP
-
?
3'-UMP + H2O
uridine + phosphate
-
14% of the activity of 3'-AMP, cytosolic enzyme
-
?
4-nitrophenyl phosphate + H2O

4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
112% activity compared to IMP
-
-
?
5'-AMP + H2O

adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
hydrolyzed by both isozymes NSP-I and NSP-II
-
?
5'-AMP + H2O
adenosine + phosphate
-
least efficient substrate
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
49% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-CMP + H2O

cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
97% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-dAMP + H2O

deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
-
-
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
isozyme NSP-I: 90% of the activity with 5'-AMP, isozyme NSP-II: 101% of the activity with 5'-AMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
128% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dCMP + H2O

deoxycytidine + phosphate
-
7.8% of the activity with 5'-dUMP
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 5'-phosphate
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 5'-phosphate
-
?
5'-dGMP + H2O

deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
-
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
142% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dIMP + H2O

deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
46% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dTMP + H2O

deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
-
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
-
-
-
-
5'-dTMP + H2O
deoxythymidine + phosphate
-
77.7% of the activity with 5'-dUMP
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
60% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dUMP + H2O

deoxyuridine + phosphate
-
-
-
-
-
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
28% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-GMP + H2O

guanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
31% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
5'-IMP + H2O

inosine + phosphate
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
-
-
-
?
5'-IMP + H2O
inosine + phosphate
-
28% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-IMP + H2O
inosine + phosphate
-
13% of the activity with 5'-dUMP
-
?
5'-IMP + H2O
inosine + phosphate
-
-
-
?
5'-UMP + H2O

uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
isozyme NSP-I: 156% of the activity with 5'-AMP, isozyme NSP-II: 205% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
8.2% of the activity with 5'-dUMP
-
?
5'-UMP + H2O
uridine + phosphate
-
22% of the activity of 3'-AMP, cytosolic enzyme
-
?
a nucleotide + H2O

a nucleoside + phosphate
-
-
-
-
?
a nucleotide + H2O
a nucleoside + phosphate
-
-
-
-
?
ADP + H2O

?
-
isozyme NSP-I: 58% of the activity with 5'-AMP, isozyme NSP-II: 51% of the activity with 5'-AMP
-
-
?
ADP + H2O

AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
low activity
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
AMP + H2O

adenosine + phosphate
-
100% activity, 15fold preference for AMP over IMP
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
60% activity compared to IMP
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
no inhibitory effects by fluoxetine and nortriptyline on AMP hydrolysis in cerebral cortex and hippocampus
-
-
?
AMP + H2O
adenosine + phosphate
-
no inhibitory effects by fluoxetine and nortriptyline on AMP hydrolysis in cerebral cortex and hippocampus
-
-
?
ATP + H2O

?
-
isozyme NSP-I: 17% of the activity with 5'-AMP, isozyme NSP-II: 1% of the activity with 5'-AMP
-
-
?
ATP + H2O
?
-
40% of the activity of 3'-AMP, cytosolic enzyme
-
-
?
ATP + H2O
?
-
influence of tricyclic antidepressant on hydrolysis of ATP, affection of the ecto-nucleotidase pathway by fluoxetine and nortriptyline, extracellular adenosine levels can be modulated
-
-
?
ATP + H2O
?
-
influence of tricyclic antidepressant on hydrolysis of ATP, affection of the ecto-nucleotidase pathway by fluoxetine and nortriptyline, extracellular adenosine levels can be modulated
-
-
?
ATP + H2O

ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
18.2% compared to the activity with to ATP
-
-
?
ATP + H2O
ADP + phosphate
a model is proposed in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling
-
-
?
ATP + H2O
ADP + phosphate
18.2% compared to the activity with to ATP
-
-
?
ATP + H2O
ADP + phosphate
a model is proposed in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
best substrate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
CMP + H2O

cytosine + phosphate
-
61.7% activity compared to AMP
-
-
?
CMP + H2O
cytosine + phosphate
-
88% activity compared to IMP
-
-
?
dsDNA 3' phosphate + H2O

dsDNA + phosphate
-
-
-
-
?
dsDNA 3' phosphate + H2O
dsDNA + phosphate
-
repair of DNA-damage
-
-
?
GDP + H2O

GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
low activity
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
-
GDP + H2O
GMP + phosphate
-
-
-
-
?
GMP + H2O

guanosine + phosphate
-
33.5% activity compared to AMP
-
-
?
GMP + H2O
guanosine + phosphate
-
98% activity compared to IMP
-
-
?
GTP + H2O

GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
24% compared to the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
24% compared to the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
IDP + H2O

IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
-
IDP + H2O
IMP + phosphate
-
-
-
-
?
IMP + H2O

inosine + phosphate
-
33.1% activity compared to AMP
-
-
?
IMP + H2O
inosine + phosphate
-
100% activity
-
-
?
p-nitrophenyl phosphate + H2O

p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
isozyme NSP-I: 51% of the activity with 5'-AMP, isozyme NSP-II: 33% of the activity with 5'-AMP
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
140% of the activity of 3'-AMP, cytosolic enzyme
-
?
UDP + H2O

UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
low activity
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UMP + H2O

uridine + phosphate
-
49.5% activity compared to AMP
-
-
?
UMP + H2O
uridine + phosphate
-
-
-
-
?
UMP + H2O
uridine + phosphate
-
-
-
-
?
UMP + H2O
uridine + phosphate
-
92% activity compared to IMP
-
-
?
UTP + H2O

UDP + phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
-
?
additional information

?
-
-
phosphotransferase activity
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
Bothrops pradoi
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
does not use AMP as a substrate
-
-
-
additional information
?
-
-
very low rates of dephosphorylation with beta-glycerophosphate, D-ribose 5-phosphate and 4-nitrophenyl phosphate, while 3',5'-cyclic AMP is not hydrolysed significantly
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
substrate specificities of SurE, YfbR, and YjjG, overview
-
-
-
additional information
?
-
-
the enzyme prefers nucleoside triphosphates, no activity with AMP and diphosphate
-
-
-
additional information
?
-
-
poor hydrolysis of AMP
-
-
-
additional information
?
-
-
the wild type enzyme does not efficiently hydrolyze ADP
-
-
-
additional information
?
-
-
the wild type enzyme hydrolyzes ADP poorly
-
-
-
additional information
?
-
nucleotidase activity of ER-targeted NTPDase3 decreases the efficiency of protein folding in ER
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
the enzyme exhibits a preference for RNA as substrate compared to single stranded DNA, while activity on double stranded DNA reaches about 8% of the single stranded DNA activity. The enzyme does not show 5'-nucleotidase or phospholipase activities
-
-
-
additional information
?
-
the enzyme exhibits a preference for RNA as substrate compared to single stranded DNA, while activity on double stranded DNA reaches about 8% of the single stranded DNA activity. The enzyme does not show 5'-nucleotidase or phospholipase activities
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
physiological significance for spleen cytoplasm in the reutilization of nucleotides, especially for thymidine and uridine nucleotides
-
-
-
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1-amino-4-[phenanthrene-9-yl-amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
PSB-16131, most potent inhibitor, 90% inhibition at 0.03 mM
-
4-nitrophenyl phosphate
-
49.9% inhibition at 10 mM
5'-deoxy-5'-isobutylthioadenosine
-
21.1% inhibition at 3 mM
5'-deoxy-5'-isobutylthioinosine
-
54.8% inhibition at 7 mM
6-N,N-diethyl-beta-gamma-dibromomethylene-D-adenosine-5-triphosphate
-
i.e. ARL67156, concentrations of 100-300 microM
ADP
-
inhibits SurE slightly, YfbR, not YjjG, competitive
beta,gamma-imidoATP
-
the inhibitory respond is blocked by 8-phenyltheophylline and superfusion with adenosine deaminase
Cibacron blue 3GA
-
45% inhibition at 0.03 mM
citrate
-
lysosomal enzyme
CMP
-
55.4% inhibition at 10 mM
CTP
-
inhibits SurE, YfbR, not YjjG, competitive
D-ribose 5-phosphate
-
14.2% inhibition at 10 mM
dAMP
-
66.1% inhibition at 10 mM
dATP
-
inhibits SurE, YfbR, not YjjG, competitive
dCTP
-
inhibits SurE, YfbR, not YjjG, competitive
deoxyuridine
-
hydrolysis of 5'-dUMP
dGTP
-
inhibits SurE, YfbR, not YjjG, competitive
dTTP
-
inhibits SurE, YfbR, not YjjG, competitive
fluoxetine
-
tricyclic antidepressant, acute and chronic treatment, concentrations of 100, 250, and 500 microM, decreases ATP (17.8%) hydrolysis in hippocampus, decreases ATP (25.5%) hydrolysis in the cerebral cortex, no inhibitory effects on AMP hydrolysis in cerebral cortex and hippocampus
GMP
-
42.7% inhibition at 10 mM
GTP
-
inhibits SurE, YfbR, not YjjG, competitive
IMP
-
36% inhibition at 10 mM
ITP
-
inhibits SurE, YfbR, not YjjG, competitive
LiCl
-
uncompetitive mode of inhibition
malate
-
lysosomal enzyme
Mg2+
-
inhibitory at 10 mM and above
NaN3
-
inhibits the enzyme from digestive gland by 36% at 0.01 mM, no inhibition of the enzyme from nervous ganglia
NEM
-
inhibits the enzyme from digestive gland by 45%, no inhibition of the enzyme from nervous ganglia
nortriptyline
-
tricyclic antidepressant, acute and chronic treatment, concentrations of 100, 250, and 500 microM, decreases ATP (16.3%) hydrolysis in the hippocampus, increases ATP (32.3%) hydrolysis in the cerebral cortex, no inhibitory effects on AMP hydrolysis in cerebral cortex and hippocampus
oxalate
-
lysosomal enzyme
p-hydroxymercuribenzoate
-
lysosomal enzyme
p-Hydroxymercuriphenylsulfonate
-
lysosomal enzyme
PO43-
-
hydrolysis of 5'-dUMP
POM-1
-
i.e. Na6[H2W12O40]*21H2O
-
POM-6
-
i.e (NH4)18[NaSb9W21O86]*14H2O
-
Reactive blue 2
-
non-selective inhibitor, 75% inhibition at 0.03 mM
Reactive Blue 4
-
8% inhibition at 0.03 mM
sodium 4-amino-1-(2-ethylanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-(2-methylanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-(3-bromoanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-(3-methylanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-(3-nitroanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-(4-chloroanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-(cyclohexylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-anilino-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-[(2-methylnaphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-[(6-carboxynaphthalen-2-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-[(naphthalen-2-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-1-[4-(2-methoxyphenoxy)anilino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-9,10-dioxo-1-(2,4,6-trimethylanilino)-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-9,10-dioxo-1-[(5-sulfonaphthalen-1-yl)amino]-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-9,10-dioxo-1-[(6-sulfonaphthalen-1-yl)amino]-9,10-dihydroanthracene-2-sulfonate
-
-
sodium 4-amino-9,10-dioxo-1-[(phenanthren-9-yl)amino]-9,10-dihydroanthracene-2-sulfonate
-
-
-
TTP
-
inhibits SurE, YfbR, not YjjG, competitive
UMP
-
74.5% inhibition at 10 mM
UTP
-
inhibits SurE, YfbR, and slightly YjjG, competitive
adenosine

IC50: 0.16 mM
ATP

-
inhibits SurE, YfbR, not YjjG, competitive
ATP
-
the inhibitory respond is blocked by 8-phenyltheophylline and superfusion with adenosine deaminase
Hg2+

-
-
KF

-
lysosomal enzyme
phosphate

-
31.7% inhibition at 20 mM
Tartrate

IC50: 7 mM
Tartrate
-
lysosomal enzyme
Tartrate
-
cytosolic enzyme
Zn2+

-
additional information

-
not inhibited by [alpha,beta-methylene]ADP
-
additional information
-
inhibitory potency of nucleotides, overview, AMP is a poor inhibitor for SurE, YfbR, and YjjG, YjjG is not inhibitable by nucleotides
-
additional information
-
the nervous ganglia enzyme is not significantly affected by vanadate, levamisole, NaN3, the digestive gland enzyme is not affected by vanadate, levamisole, ouabain, and oligomycin
-
additional information
-
no effect of p-chloromercuribenzoate
-
additional information
-
not inhibited by Sodium 1-amino-9,10-dioxo-4-(2-fluorophenylamino)-9,10-dihydro-anthracene-2-sulfonate and sodium 1-amino-9,10-dioxo-4-(propylamino)-9,10-dihydroanthracene-2-sulfonate
-
additional information
-
not inhibited by molybdate
-
additional information
-
the organoselenium compounds 2-phenyl-1,2-benzisoselenazol-3(2H)-one (i.e. ebselen) or diphenyl diselenide counteract the glutamate-induced stimulation of ecto-nucleotide activities, concentrations of 0.3-3 microM
-
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0.17
-
crude enzyme from supernatant, at pH 6.5 and 37°C
1.37
-
substrate p-nitrophenyl phosphate, lysosomal enzyme
2.3
-
recombinant mutant, DELTA55 gPAPP protein
35.83
-
after 211fold purification, at pH 6.5 and 37°C
9.5
-
recombinant gPAPP protein, full-lenght
additional information

characterization of mutants of the inositol polyphosphate 1-phosphatase SAL1, alx8 mutant, fry1-1 mutant and T-DNA insertional knockout mutant have markedly increased resistance to drought when water is withheld from soil-grown intact plants, effect of mutations in SAL1 by microarray and metabolom analysis, biomass at maturity, plant water use efficiency, stomatal index, morphology or aperture unaffected under well-water conditions, inactivation of SAL1 protein results in altered osmoprotectants, higher leaf relative water content and maintenance of viable tissues during prolonged water stress
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, pyrophosphate assay reveals highest nucleotidase activity among tested venoms, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, nucleotidase activity determined by pyrophosphate assay, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, most intense bands in 5'-nucleotidase gels among the tested venoms, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, most intense bands in 5'-nucleotidase gels among the tested venoms
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
Bothrops pradoi
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comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
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comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
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comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
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comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
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comparative analysis of nucleotidase activities of crude venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, nucleotidase activities tested by pyrophosphate assay, no or minimal bands in zymographic analyses; comparative analysis of nucleotidase activities of crude venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, no or minimal bands in zymographic analyses of 5'-nucleotidase activities, lowest 5'-nucleotidase activity among Crotales; comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, minimal bands in zymographic analyses
additional information
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comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, minimal bands in zymographic analyses
additional information
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additional information
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mechanism and subcellular location of NTPDase activation, block of the secretory transport with monensin or brefeldin A, or by targeting to the endoplasmic reticulum (ER) with a signal peptide, cell surface biotinylation, glycosidase sensitivity, fluorescence microscopy, results in contrast to previous report on CD39, NTPDase3 catalytically active in the ER or in the ER-Golgi intermediate compartment, terminal glycosylation in Golgi not essential for activity, wild-type NTPDase3 has probably ATPase activity in a post-ER but pre-Golgi compartment, ER-targeted NTPDase3 as potential tool to study the effects of ATP depletion on ER function under normal and stress conditions
additional information
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comparative analysis of nucleotidase activities of crude venoms, nucleotidase activities tested by pyrophosphate assay and by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
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comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, low activity levels, no banding in zymographic analyses
additional information
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inactivation of gPAPP protein leads to neonatal lethality, lung abnormalities resembling atelectasis, and dwarfism characterized by aberrant cartilage morphology, undersulfated chondroitin in the absence of functional enzyme, loss of enzyme function leads to perturbations in the levels of heparan sulfate species in lung tissue and whole embryos, clearance of the nucleotide product of sulfotransferases within the Golgi plays an important role in glycosaminoglycan sulfation, unique genetic basis for chondrodysplasia
additional information
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extracellular nucleotidase activity and ATP release upon deoxygenation, extracellular ATP determined with the luciferin-luciferase technique, increase of extracellular ATP in the presence of ectonucleotidase inhibitor reveals presence of ectonucleotidase activity, ATP release of erythrocytes not influenced by oxygenation degree
additional information
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glutamate stimulates ecto-nucleotidase activities in cerebellar granule cells, increase of extracellular adenosine levels, the analyzed organoselenium compounds do not modify basal enzyme activities but they counteract the increase in the nucleotide hydrolysis produced by neurotoxic agents likely via their antioxidant properties
additional information
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significant changes in NTPDase activities when the tricyclic antidepressants fluoxetine and nortriptyline are tested in vitro, affection of the ecto-nucleotidase pathway by modulating changes of extracellular adenosine levels
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