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Information on EC 3.6.1.29 - bis(5'-adenosyl)-triphosphatase
for references in articles please use BRENDA:EC3.6.1.29
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.29 bis(5'-adenosyl)-triphosphatase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.6.1.29
- carcinogenesis
-
heterozygosity
-
clinicopathological
- metastasis
-
microsatellite
- tumorigenesis
- adenocarcinoma
-
hypermethylation
-
methylation-specific
- neoplasia
-
precancerous
-
paraffin-embedded
-
intraepithelial
- papillomavirus
- polyphosphate
-
tumor-suppressor
-
preneoplastic
- p16ink4a
-
normal-sized
-
rassf1a
-
fra16d
- hippel-lindau
-
3.6.1.17
-
caretaker
showSynonyms
fhit protein, fragile histidine triad, fragile histidine triad protein, dinucleoside triphosphatase, ap3a hydrolase, diadenosine triphosphatase, ap3aase, bis(5'-adenosyl)-triphosphatase, dinucleosidetriphosphatase, p1,p3-bis(5'-adenosyl)-triphosphate adenylohydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ap3A hydrolase
Ap3Aase
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-
-
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Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
-
-
-
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diadenosine 5,5-P1,P3-triphosphatase
-
-
-
-
diadenosine triphosphatase
dinucleoside triphosphatase
dinucleoside-triphosphatase
dinucleosidetriphosphatase
-
-
-
-
Fhit
Fhit protein
FHIT protein/dinucleoside triphosphatase
fragile histidine triad
Fragile histidine triad protein
HIT-45 protein
Ap3A hydrolase
-
-
-
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Fragile histidine triad protein
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP
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-
-
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P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP
two-step reaction mechanism via a fragile histidine triad Fhit-AMP intermediate and release of MgADP-, kinetic of the reaction steps, overview
-
P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP
the dimeric enzyme contains a catalytic histidine triad with H96 forming a covalent intermediate at the alpha-phosphate of P1,P3-bis(5'-adenosyl)triphosphate, S128, H96 and H98 are essential for the reaction, structure overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis
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-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
P1,P3-bis(5'-adenosyl)-triphosphate adenylohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
63951-94-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine 5'-phosphoimidazolide + UDP
imidazole + dA(5')p3(5')U
-
Substrates: H96G mutant
Products: -
Products: -
?
7-benzylguanosine(5')triphospho(5')adenosine + H2O
7-benzylguanosine(5')monophosphate + 7-benzylguanosine(5')diphosphate
-
Substrates: -
Products: -
Products: -
?
7-ethylguanosine(5')triphospho(5')adenosine + H2O
7-ethylguanosine(5')monophosphate + 7-ethylguanosine(5')diphosphate
-
Substrates: -
Products: -
Products: -
?
7-methylguanosine(5')triphospho(5')7-methylguanosine + H2O
7-methylguanosine(5')monophosphate + 7-methylguanosine(5')diphosphate
-
Substrates: -
Products: -
Products: -
?
7-methylguanosine(5')triphospho(5')adenosine + H2O
7-methylguanosine(5')monophosphate + ADP + AMP + 7-methylguanosine(5')diphosphate
7-methylguanosine(5')triphospho(5')cytosine + H2O
7-methylguanosine(5')monophosphate + CDP + CMP + 7-methylguanosine(5')diphosphate
-
Substrates: -
Products: -
Products: -
?
7-methylguanosine(5')triphospho(5')guanosine + H2O
7-methylguanosine(5')monophosphate + GDP + 7-methylguanosine(5')diphosphate + GMP
7-methylguanosine(5')triphospho(5')uracil + H2O
7-methylguanosine(5')monophosphate + UDP + UMP + 7-methylguanosine(5')diphosphate
-
Substrates: -
Products: -
Products: -
?
adenosine 5'-phosphoimidazolide + ADP
imidazole + A(5')p3(5')A
-
Substrates: H96G mutant
Products: -
Products: -
?
adenosine 5'-phosphoimidazolide + ATP
imidazole + A(5')p4(5')A
-
Substrates: H96G mutant
Products: -
Products: -
?
adenosine 5'-phosphoimidazolide + CDP
imidazole + A(5')p3(5')C
-
Substrates: H96G mutant
Products: -
Products: -
?
adenosine 5'-phosphoimidazolide + GDP
imidazole + A(5')p3(5')G
-
Substrates: H96G mutant
Products: -
Products: -
?
adenosine 5'-phosphoimidazolide + TDP
imidazole + A(5')p3(5')T
-
Substrates: H96G mutant
Products: -
Products: -
?
adenosine 5'-phosphoimidazolide + UDP
imidazole + A(5')p3(5')U
-
Substrates: H96G mutant
Products: -
Products: -
?
adenosine 5'-phosphoimidazolide + UTP
imidazole + A(5')p4(5')U
-
Substrates: H96G mutant
Products: -
Products: -
?
adenosyl-ribose triphosphate + H2O
AMP + ribose diphosphate
-
Substrates: -
Products: -
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?
adenylylfluoride + H2O
AMP + fluoride
Q9LVM4
Substrates: -
Products: -
Products: -
?
Appp-S-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacine-3-yl) methylaminoacetyl + H2O
AMP + diphospho-S-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacine-3-yl) methylaminoacetyl
-
Substrates: -
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?
Appp-S-(7-diethylamino-4-methyl-3-(4-succinimidylphenyl)) coumarin + H2O
AMP + diphospho-S-(7-diethylamino-4-methyl-3-(4-succinimidylphenyl)) coumarin
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Substrates: -
Products: -
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?
cytosine 5'-phosphoimidazolide + UDP
imidazole + C(5')p3(5')U
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Substrates: H96G mutant
Products: -
Products: -
?
gamma-fluoro-ATP + H2O
AMP + fluorodiphosphoric acid
Q9LVM4
Substrates: -
Products: -
Products: -
?
Gppp-S-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacine-3-yl) methylaminoacetyl + H2O
GMP + diphospho-S-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacine-3-yl) methylaminoacetyl
-
Substrates: -
Products: -
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?
m27,2'OGpppG + H2O
ppm27,2'OG + guanosine monophosphate
-
Substrates: -
Products: -
Products: -
?
m2N2,7GpppG + H2O
pm2N2,7G + guanosine diphosphate
-
Substrates: -
Products: -
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?
m3N2,N2,7GpppA + H2O
ppm3N2,N2,7G + adenosine monophosphate
-
Substrates: -
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?
m3N2,N2,7GpppG + H2O
ppm3N2,N2,7G + guanosine monophosphate
-
Substrates: -
Products: -
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?
m7Gpppm3N6,N6,2'OA + H2O
pm7G + ppm3N6,N6,2'OA
-
Substrates: -
Products: -
Products: -
?
m7Gpppm7G + H2O
N7-methyl-GMP + N7-methyl-GDP
-
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
AMP + ADP
Substrates: major substrate
Products: -
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?
P1-5'-O-adenosine-P3-5'-O-adenosine triphosphate + H2O
AMP + ADP
-
Substrates: -
Products: -
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r
P1-P5-bis(5'-adenosyl) pentaphosphate + H2O
adenosine monophosphate + adenosine tetraphosphate
-
Substrates: -
Products: -
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?
thymidine 5'-monophosphate p-nitrophenylester + H2O
?
-
Substrates: -
Products: -
Products: -
?
thymidine 5'-phosphoimidazolide + UDP
imidazole + T(5')p3(5')U
-
Substrates: H96G mutant
Products: -
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?
5'-O-[amino(hydroxy)phosphoryl]adenosine + H2O
?
-
Substrates: 64% initial velocity of degradation
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?
5'-O-[amino(hydroxy)phosphoryl]adenosine + H2O
?
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Substrates: 100% initial velocity of degradationin 0.1 M potassium phosphate (pH 6.8), 5 mM MgCl2, at 30°C
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?
5'-O-[amino(hydroxy)phosphoryl]adenosine + H2O
?
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Substrates: 96% initial velocity of degradation
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?
5'-O-[fluoro(hydroxy)phosphoryl]adenosine + H2O
?
-
Substrates: 19% initial velocity of degradation
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?
5'-O-[fluoro(hydroxy)phosphoryl]adenosine + H2O
?
-
Substrates: 25% initial velocity of degradation
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?
5'-O-[fluoro(hydroxy)phosphoryl]adenosine + H2O
?
-
Substrates: 97% initial velocity of degradation
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?
5'-O-[hydroxy(sulfooxy)phosphoryl]adenosine + H2O
?
-
Substrates: 48% initial velocity of degradation
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?
5'-O-[hydroxy(sulfooxy)phosphoryl]adenosine + H2O
?
-
Substrates: 65% initial velocity of degradation
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?
5'-O-[hydroxy(sulfooxy)phosphoryl]adenosine + H2O
?
-
Substrates: 100% initial velocity of degradation
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?
7-methylguanosine(5')triphospho(5')adenosine + H2O
7-methylguanosine(5')monophosphate + ADP + AMP + 7-methylguanosine(5')diphosphate
-
Substrates: -
Products: -
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?
7-methylguanosine(5')triphospho(5')adenosine + H2O
7-methylguanosine(5')monophosphate + ADP + AMP + 7-methylguanosine(5')diphosphate
-
Substrates: -
Products: -
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?
7-methylguanosine(5')triphospho(5')guanosine + H2O
7-methylguanosine(5')monophosphate + GDP + 7-methylguanosine(5')diphosphate + GMP
-
Substrates: -
Products: -
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?
7-methylguanosine(5')triphospho(5')guanosine + H2O
7-methylguanosine(5')monophosphate + GDP + 7-methylguanosine(5')diphosphate + GMP
-
Substrates: -
Products: -
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?
adenosine 5'-phosphoramidate + H2O
AMP + NH3
Q9LVM4
Substrates: no requirement for Mg2+
Products: -
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?
adenosine 5'-phosphoramidate + H2O
AMP + NH3
Q9LVM4
Substrates: preferred substrate
Products: -
Products: -
?
adenosine 5'-phosphoramidate + H2O
AMP + NH3
-
Substrates: preferred substrate
Products: -
Products: -
?
adenosine 5'-phosphosulfate + H2O
AMP + sulfate
Q9LVM4
Substrates: no requirement for Mg2+, reaction of EC 3.6.2.1, adenylylsulfatase
Products: -
Products: -
?
adenosine 5'-phosphosulfate + H2O
AMP + sulfate
Q9LVM4
Substrates: reaction of EC 3.6.2.1, adenylylsulfatase
Products: -
Products: -
?
adenosine 5'-phosphosulfate + H2O
AMP + sulfate
-
Substrates: reaction of EC 3.6.2.1, adenylylsulfatase
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?
adenosyl-cytosinyl triphosphate + H2O
CDP + AMP
-
Substrates: -
Products: -
Products: -
?
adenosyl-guanosine triphosphate + H2O
GDP + AMP
-
Substrates: -
Products: -
Products: -
?
adenosyl-guanosine triphosphate + H2O
GDP + AMP
-
Substrates: -
Products: -
Products: -
?
adenosyl-guanosine triphosphate + H2O
GDP + AMP
-
Substrates: -
Products: -
Products: -
?
di(7-methylguanosine) 50,50 0 0-P1,P3-triphosphate + H2O
?
-
Substrates: 100% initial velocity of degradation
Products: -
Products: -
?
di(7-methylguanosine) 50,50 0 0-P1,P3-triphosphate + H2O
?
-
Substrates: 8% initial velocity of degradation
Products: -
Products: -
?
di(7-methylguanosine) 50,50 0 0-P1,P3-triphosphate + H2O
?
-
Substrates: 1% initial velocity of degradation
Products: -
Products: -
?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
AMP + ATP
-
Substrates: -
Products: -
Products: -
?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
AMP + ATP
-
Substrates: -
Products: -
Products: -
?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
AMP + ATP
-
Substrates: -
Products: -
Products: -
?
diadenosine 5',5''-P1,P5-pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
Substrates: -
Products: -
Products: -
?
diadenosine 5',5''-P1,P5-pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
Substrates: -
Products: -
Products: -
?
diadenosine 5',5''-P1,P5-pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
Substrates: -
Products: -
Products: -
?
inosine 5'-phosphoramidate + H2O
IMP + NH3
Q9LVM4
Substrates: -
Products: -
Products: -
?
m7GpppA + H2O
N7-methyl-GMP + ADP + N7-methyl-GDP + AMP
-
Substrates: -
Products: -
Products: -
?
m7GpppA + H2O
N7-methyl-GMP + ADP + N7-methyl-GDP + AMP
-
Substrates: -
Products: -
Products: -
?
m7GpppG + H2O
pm7G + guanosine diphosphate
-
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-(7-methylguanosyl))triphosphate + H2O
?
-
Substrates: 100% initial velocities of degradation
Products: -
Products: -
?
P1,P3-bis(5'-(7-methylguanosyl))triphosphate + H2O
?
-
Substrates: 8% initial velocities of degradation
Products: -
Products: -
?
P1,P3-bis(5'-(7-methylguanosyl))triphosphate + H2O
?
-
Substrates: 1% initial velocities of degradation
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
Q9LVM4
Substrates: requirement for Mg2+
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
Q9LVM4
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: 27% initial velocity of degradation
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Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: FHIT protein has been shown to function as a dinucleoside 5',5'''-P1,P3-triphosphate hydrolase, forming ADP and AMP from the Ap3A substrate. Tumor suppression by FHIT occurs in lung, gastric, and renal carcinoma-derived cell lines, with Ap3A hydrolysis by FHIT being not necessary for the tumor suppressive activity
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P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
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?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: 58% initial velocity of degradation
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
ADP + AMP
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
ADP + AMP
-
Substrates: 72% initial velocity of degradation
Products: -
Products: -
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
-
Substrates: 27% initial velocities of degradation
Products: -
Products: -
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
Substrates: major substrate
Products: -
Products: -
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
-
Substrates: 58% initial velocities of degradation
Products: -
Products: -
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
-
Substrates: 72% initial velocities of degradation
Products: -
Products: -
?
P1-bis(5'-adenosyl) monophosphate + H2O
?
Q9LVM4
Substrates: requirement for Mg2+
Products: -
Products: -
?
P1-bis(5'-adenosyl) monophosphate + H2O
?
Q9LVM4
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: hydrolysis of Ap3A
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?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
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Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: highest specificity
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?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: highest specificity
Products: -
Products: -
?
P1-P3-bis(5'-guanosyl) triphosphate + H2O
GDP + GMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-guanosyl) triphosphate + H2O
GDP + GMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-guanosyl) triphosphate + H2O
GDP + GMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-guanosyl) triphosphate + H2O
GDP + GMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-guanosyl) triphosphate + H2O
GDP + GMP
-
Substrates: -
Products: -
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?
P1-P3-bis(5'-guanosyl) triphosphate + H2O
GDP + GMP
-
Substrates: -
Products: -
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?
P1-P3-bis(5'-uracyl) triphosphate + H2O
UDP + UMP
-
Substrates: -
Products: -
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?
additional information
?
-
Q9LVM4
Substrates: Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5'-monophosphates from such natural metabolites as adenosine 5'-phosphosulfate and adenosine 5'-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 5'-O-phosphorofluoridate and adenosine 5'-O-(gamma-fluorotriphosphate), and release AMP from them, the enzyme is involved in controlling the cellular level of NpnN0', overview
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additional information
?
-
Q9LVM4
Substrates: the dinucleoside triphosphatase preferentially hydrolyzes NpppN' to an NMP and N'DP
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?
additional information
?
-
-
Substrates: Fhit protein inhibits cell growth by attenuating the signaling mediated by nuclear factor-kappaB in colon cancer cell lines
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additional information
?
-
-
Substrates: Fhit is a tumor suppressor protein
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additional information
?
-
-
Substrates: Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5'-monophosphates from such natural metabolites as adenosine 5'-phosphosulfate and adenosine 5'-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 50-O-phosphorofluoridate and adenosine 5'-O-(gamma-fluorotriphosphate), and release AMP from them, the enzyme is involved in controlling the cellular level of NpnN0', overview
Products: -
Products: -
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additional information
?
-
-
Substrates: diadenosine oligophosphates, ApnA, have emerged as putative extra- and intracellular signaling molecules implicated in the maintenance and regulation of vital cellular functions and are now considered as a new class of signal transducers. FHIT induction protects from tumor necrosis factor-related apoptosis inducing ligand-induced cell death downstream TRAIL-receptors and likely requires its dinucleoside-triphosphate hydrolase activity, overview
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additional information
?
-
-
Substrates: the dinucleoside triphosphatase preferentially hydrolyzes NpppN' to an NMP and N'DP
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additional information
?
-
-
Substrates: the enzyme does not hydrolyze Cap 4 m7Gpppm3N6,N6,2'O, Apm2'OApm2'OCpm2N3,2'OU, m7GpppApApCpU, m7GpCH2ppG, and m7Gpppm3N6,N6,2'OApm29OA
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not hydrolyze Cap 4 m7Gpppm3N6,N6,2'O, Apm2'OApm2'OCpm2N3,2'OU, m7GpppApApCpU, m7GpCH2ppG, and m7Gpppm3N6,N6,2'OApm29OA
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenylylfluoride + H2O
AMP + fluoride
Q9LVM4
Substrates: -
Products: -
Products: -
?
gamma-fluoro-ATP + H2O
AMP + fluorodiphosphoric acid
Q9LVM4
Substrates: -
Products: -
Products: -
?
P1-5'-O-adenosine-P3-5'-O-adenosine triphosphate + H2O
AMP + ADP
-
Substrates: -
Products: -
Products: -
r
P1-bis(5'-adenosyl) monophosphate + H2O
?
Q9LVM4
Substrates: requirement for Mg2+
Products: -
Products: -
?
adenosine 5'-phosphoramidate + H2O
AMP + NH3
Q9LVM4
Substrates: no requirement for Mg2+
Products: -
Products: -
?
adenosine 5'-phosphosulfate + H2O
AMP + sulfate
Q9LVM4
Substrates: no requirement for Mg2+, reaction of EC 3.6.2.1, adenylylsulfatase
Products: -
Products: -
?
adenosine 5'-phosphosulfate + H2O
AMP + sulfate
-
Substrates: reaction of EC 3.6.2.1, adenylylsulfatase
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
Q9LVM4
Substrates: requirement for Mg2+
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: FHIT protein has been shown to function as a dinucleoside 5',5'''-P1,P3-triphosphate hydrolase, forming ADP and AMP from the Ap3A substrate. Tumor suppression by FHIT occurs in lung, gastric, and renal carcinoma-derived cell lines, with Ap3A hydrolysis by FHIT being not necessary for the tumor suppressive activity
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
ADP + AMP
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
P1-P3-bis(5'-adenosyl) triphosphate + H2O
ADP + AMP
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Q9LVM4
Substrates: Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5'-monophosphates from such natural metabolites as adenosine 5'-phosphosulfate and adenosine 5'-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 5'-O-phosphorofluoridate and adenosine 5'-O-(gamma-fluorotriphosphate), and release AMP from them, the enzyme is involved in controlling the cellular level of NpnN0', overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: Fhit protein inhibits cell growth by attenuating the signaling mediated by nuclear factor-kappaB in colon cancer cell lines
Products: -
Products: -
?
additional information
?
-
-
Substrates: Fhit is a tumor suppressor protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5'-monophosphates from such natural metabolites as adenosine 5'-phosphosulfate and adenosine 5'-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 50-O-phosphorofluoridate and adenosine 5'-O-(gamma-fluorotriphosphate), and release AMP from them, the enzyme is involved in controlling the cellular level of NpnN0', overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: diadenosine oligophosphates, ApnA, have emerged as putative extra- and intracellular signaling molecules implicated in the maintenance and regulation of vital cellular functions and are now considered as a new class of signal transducers. FHIT induction protects from tumor necrosis factor-related apoptosis inducing ligand-induced cell death downstream TRAIL-receptors and likely requires its dinucleoside-triphosphate hydrolase activity, overview
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Mg2+
-
required for the synthesis of dinucleoside tri- and tetraphosphates by H96G mutant
Mg2+
-
dependent on, formation of an MgADP- intermediate during catalytic reaction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O,O',O''-tris[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl] O,O',O''-propane-1,2,3-triyl tris[hydrogen (phosphorothioate)]
-
O,O'-bis[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl] O,O'-(2-hydroxypropane-1,3-diyl) bis[hydrogen (phosphorothioate)]
-
O-[1,11-bis[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]-3,9-dioxido-3,9-disulfanyl-2,4,8,10-tetraoxa-3l5,9l5-diphosphaundecan-6-yl] dihydrogen phosphorothioate
-
O-[3-[[[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy](sulfanyl)phosphoryl]oxy]-2,2-bis([[[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy](sulfanyl)phosphoryl]oxy]methyl)propyl] dihydrogen phosphorothioate
-
O-[3-[[[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy](sulfanyl)phosphoryl]oxy]-2,2-bis([[[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy](sulfanyl)phosphoryl]oxy]methyl)propyl] O-[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl] hydrogen phosphorothioate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady state kinetics of the phosphorylated enzyme form
-
0.003
5'-O-[amino(hydroxy)phosphoryl]adenosine
-
in 0.1 M potassium phosphate (pH 6.8), 5 mM MgCl2, at 30°C
0.003
5'-O-[amino(hydroxy)phosphoryl]adenosine
-
in 0.1 M potassium phosphate (pH 6.8), 5 mM MgCl2, at 30°C
0.015
5'-O-[amino(hydroxy)phosphoryl]adenosine
-
in 0.1 M potassium phosphate (pH 6.8), 5 mM MgCl2, at 30°C
0.22
Ap4A
capillary electrophoresis assay, pH not specified in the publication, 37°C
0.00066
P1,P3-bis(5'-adenosyl)triphosphate
diphosphorylated recombinant enzyme, pH 6.8, 37°C
0.00067
P1,P3-bis(5'-adenosyl)triphosphate
monophosphorylated recombinant enzyme, pH 6.8, 37°C
0.0016
P1,P3-bis(5'-adenosyl)triphosphate
nonphosphorylated recombinant enzyme, pH 6.8, 37°C
0.0029
P1-5'-O-adenosine-P3-5'-O-adenosine triphosphate
-
wild-type enzyme, pH 7.3
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.46
Ap4A
capillary electrophoresis assay, pH not specified in the publication, 37°C
0.02
P1,P3-bis(5'-adenosyl)triphosphate
diphosphorylated recombinant enzyme, pH 6.8, 37°C
0.38
P1,P3-bis(5'-adenosyl)triphosphate
monophosphorylated recombinant enzyme, pH 6.8, 37°C
2.74
P1,P3-bis(5'-adenosyl)triphosphate
nonphosphorylated recombinant enzyme, pH 6.8, 37°C
3 - 6
P1,P3-bis(5'-adenosyl)triphosphate
nonphosphorylated recombinant enzyme, pH 6.8, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.08
Ap4A
capillary electrophoresis assay, pH not specified in the publication, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.235
adenosine 5'-O-(gamma-fluoromonophosphate)
Q9LVM4
pH 6.8, 30°C, in presence of Mg2+
0.0021
P1,P3-bis(5'-adenosyl) triphosphate
Q9LVM4
pH 6.8, 30°C, in presence of Mg2+
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Q9LVM4
relative velocities of hydrolysis with different substrates, overview
additional information
-
relative velocities of hydrolysis with different substrates, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
7.3
-
optimal pH for hydrolysis of P1-5'-O-adenosine-P3-5'-O-adenosine triphosphate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
a human SV40-immortalized normal bronchial epithelial cell line
brenda
-
FHIT expression level and distribution in neoplastic, hyperplastic, and healthy endometrium, overview
brenda
cell line has lost the ability to express the Ap3A-hydrolase. Ap3A levels in H1299 cells are 30times higher than in HEK-293T cells
brenda
additional information
additional information
-
FHIT expression analysis of wild-type and mutant enzyme in colonic cancer cell lines, overview
brenda
additional information
-
detailed FHIT expression analysis in human tissues, the expression is reduced about 30-100% in cancer cells compared to healthy cells in diverse tissue types, no expression in lymphoma cells, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
a loss of FHIT expression associated with poor prognosis and beta-catenin expression
physiological function
physiological function
the FHIT protein is a tumor suppressor. FHIT/ferrodoxin reductase complex generates reactive oxygen species and increases calcium uptake into the mitochondria to potentiate the effects of apoptotic agents
physiological function
formation of Fhit-substrate complex results in an apoptosis initiation signal while subsequent hydrolysis of ApnA terminates this action
Show AA Sequence and Transmembrane Helices (3610 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
41000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
Fhit is phosphorylated in vivo, and is phosphorylated in vitro by Src kinase
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H96G
H355N
additional information
-
FHIT-specific small interference RNA transfection of SV40-immortalized normal bronchial BEAS cells that show levels of FHIT protein comparable to those of normal bronchial cells, results in a significant increase of TRAIL-induced apoptosis
H96G
-
mutant Fhit can not hydrolyse phosphoanhydrides, but can synthetise dinucleoside tri- and tetraphosphates
H96G
-
site-directed mutagenesis in the fragile histidine triad, leads to reduced activity and reduced hydrolysis of reaction intermediates
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM HEPES-NaOH buffer, pH 7.0, 100 mM NaCl, 25% glycerol, at least 18 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of Fhit with the elk tyrosine kinase in Escherichia coli strain TBK1 by ion exchange chromatography, gel filtration, and another step of ion exchange chromatography
native enzyme from blood platelets and leukocytes, 19000fold, by anion exchange chromatography and N6-5'-AMP affinity chromatography to homogeneity
-
native enzyme from brain cytosolic fraction by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, and N6-5'-AMP affinity chromatography to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of Fhit with the elk tyrosine kinase in Escherichia coli strain TBK1, expression of nonphosphorylized enzyme in Escherichia coli strain SG100
constitutive expression of FHIT in Calu-1 cells, endogenously lacking FHIT protein, FHIT re-expression does not affect cell survival, but a Calu-1 cell clone in which the expression of FHIT is under the control of a CMV promoter, is more resistant to TRAIL-induced, i.e. tumor necrosis factor-related apoptosis inducing ligand-induced, apoptosis than the mock transfected Calu-1 clones
-
expression in Escherichia coli
FHIT expression analysis of wild-type and mutant enzyme in colon cancer cell lines, overview
-
gene At5g58240, DNA and amino acid sequence determination and analysis
Q9LVM4
gene fhit maps to chromosome 3q14.2, expression analysis in human tissues, overview
-
gene FHIT, DNA sequence determination and analysis, comparative mapping study, the gene locates to BTA22q24prox
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
FHIT is absent or reduced in many types of human tumors including lung, esophagus, stomach, kidney and cervical carcinomas
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
enzyme assay using diadenosine tetraphosphate as a substrate. The reaction product ATP is quantified by luciferin-luciferase reaction in a 96-well plate format. The method displays a limit of detection of 14.6 nM
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jakubowski, H.; Guranowski, A.
Enzymes hydrolyzing ApppA and/or AppppA in higher plants. Purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds
J. Biol. Chem.
258
9982-9989
1983
Lupinus luteus
brenda
Luthje, J.; Ogilvie, A.
Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity
Eur. J. Biochem.
149
119-127
1985
Homo sapiens
brenda
Costas, M.J.; Cameselle, J.C.; Sillero, A.
Mitochondrial location of rat liver dinucleoside triphosphatase
J. Biol. Chem.
261
2064-2067
1986
Rattus norvegicus
brenda
Gunther Sillero, M.A.; Villalba, R.; Moreno, A.; Quintanilla, M.; Lobaton, C.D.; Sillero, A.
Dinucleosidetriphosphatase from rat liver
Eur. J. Biochem.
76
331-337
1977
Rattus norvegicus
brenda
Michels, W.; Schlimme, E.
Catabolism of capped (3'-5')- and (2'-5')-adenylates in rat liver nuclei
FEBS Lett.
166
57-61
1984
Rattus norvegicus
brenda
Costas, M.J.; MOntero, J.M.; Cameselle, J.C.; Gunther Sillero, M.A.; Sillero, A.
Dinucleosidetriphosphatase from rat brain
Int. J. Biochem.
16
757-762
1984
Rattus norvegicus
brenda
Costas, M.J.; Cameselle, J.C.; Gunther Sillero, M.A.; Sillero, A.
Occurence of nucleosidetriphosphatase in the cytosol and particulate fractions from rat liver
Int. J. Biochem.
17
903-909
1985
Rattus norvegicus
brenda
Montero, J.M.; Garcia-Agndez, J.A.; Costas, M.J.; Cameselle, J.C.; Gunther Sillero, M.A.; Sillero, A.
Hydrolytic activities on diadenosine 5',5'''-P1,P3-triphosphate in the 27000 x g supernatants and precipitates from rat brain, muscle, kidney and liver
Cienc. Biol.
11
1-6
1986
Rattus norvegicus
-
brenda
Hurtado, C.; Ruiz, A.; Sillero, A.; Gunther Sillero, M.A.
Specific magnesium-dependent diadenosine 5',5'''-P1,P3-triphosphate pyrophosphohydrolase in Escherichia coli
J. Bacteriol.
169
1718-1723
1987
Escherichia coli
brenda
Barnes, L.D.; Garrison, P.N.; Siprashvili, Z.; Guranowski, A.; Robinson, A.K.; Ingram, S.W.; Croce, C.M.; Ohta, M.; Huebner, K.
Fhit, a putative tumor supressor in humans, is a dinucleoside 5',5'''-P1,P3-triphosphate hydrolase
Biochemistry
35
11529-11535
1996
Homo sapiens
brenda
Pawelczyk, T.; Kowara, R.; Golebiowski, F.; Matecki, A.
Expression in Escherichia coli and simple purification of human Fhit protein
Protein Expr. Purif.
18
320-326
2000
Homo sapiens (P49789), Homo sapiens
brenda
Prescott, M.; Thorne, N.M.H.; Milne, A.D.; McLennan, A.G.
Characterization of a bis(5'-nucleosidyl) triphosphate pyrophosphohydrolase from encysted embryos of the brine shrimp Artemia
Int. J. Biochem.
24
565-571
1992
Artemia sp.
brenda
Guranowski, A.; Starzynska, E.; Gzik, L.; Langston, S.P.; Brown, P.; Blackburn, G.M.
Methylene and halomethylene analogues of diadenosine 5'5'''-P1,P3-triphosphate (ApppA) as substrates or inhibitors of ApppA-degrading enzymes
Nucleosides Nucleotides
14
731-734
1995
Lupinus luteus
-
brenda
Pace, H.C.; Garrison, P.N.; Robinson, A.K.; Barnes, L.D.; Draganescu, A.; Rsler, A.; Blackburn, G.M.; Siprashvilli, Z.; Croce, C.M.; Huebner, K.; Brenner, C.
Genetic, biochemical and crystallographic characterization of Fith-substrate complexes as the active signalling form of Fith
Proc. Natl. Acad. Sci. USA
95
5484-5489
1998
Homo sapiens
brenda
Draganescu, A.; Hodawadekar, S.C.; Gee, K.R.; Brenner, C.
Fith-nucleotide specificity probed with novel fluorescent and fluorogenic substrates
J. Biol. Chem.
275
4555-4560
2000
Homo sapiens
brenda
Brevet, A.; Chen, J.; Fromant, M.; Blanquet, S.; Plateau, P.
Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae
J. Bacteriol.
173
5275-5279
1991
Saccharomyces cerevisiae
brenda
Rotllan, P.; Rodriguez-Ferrer, C.R.; Asensio, A.C.; Oaknin, S.
Potent inhibition of specific diadenosine polyphosphate hydrolases by suramin
FEBS Lett.
429
143-146
1998
Rattus norvegicus
brenda
Garcia-Agndez, J.A.; Cameselle, J.C.; Costas, M.J.; Gunther Sillero, M.A.; Sillero, A.
Particulate diadenosine 5',5'''-P1,P3-triphosphate hydrolases in rat brain: two specific dinucleoside triphosphatases and two phosphodiesterase I-like hydrolases
Biochim. Biophys. Acta
1073
402-409
1991
Rattus norvegicus
brenda
Guranowski, A.; Starzynska, E.; Bojarska, E.; Stepinski, J.; Darzynkiewicz, E.
Dinucleoside 5',5'''-P1,P3-triphosphate hydrolase from yellow lupin (Lupinus luteus) seeds: purification to homogeneity and hydrolysis of mRNA 5'-cap analogs
Protein Expr. Purif.
8
416-422
1996
Lupinus luteus
brenda
Bernet, D.; Pinto, R.M.; Sillero, A.; Cameselle, J.C.
Location of dinucleoside triphosphatase in the matrix space of rat liver mitochondria
FEBS Lett.
283
286-288
1991
Rattus norvegicus
brenda
Huang, K.; Frey, P.A.
Engineering human Fhit, a diadenosine triphosphate hydrolase, into an efficient dinucleoside polyphosphate synthase
J. Am. Chem. Soc.
126
9548-9549
2004
Homo sapiens
brenda
Di Meo, G.P.; Perucatti, A.; Uboldi, C.; Roperto, S.; Incarnato, D.; Roperto, F.; Williams, J.; Eggen, A.; Ferretti, L.; Iannuzzi, L.
Comparative mapping of the fragile histidine triad (FHIT) gene in cattle, river buffalo, sheep and goat by FISH and assignment to BTA22 by RH-mapping: A comparison with HSA3
Anim. Genet.
36
363-365
2005
Bos taurus (Q4KTA6), Bos taurus
brenda
Huang, K.; Arabshahi, A.; Wei, Y.; Frey, P.A.
The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit
Biochemistry
43
7637-7642
2004
Homo sapiens
brenda
Garrison, P.N.; Robinson, A.K.; Pekarsky, Y.; Croce, C.M.; Barnes, L.D.
Phosphorylation of the human Fhit tumor suppressor on tyrosine 114 in Escherichia coli and unexpected steady state kinetics of the phosphorylated forms
Biochemistry
44
6286-6292
2005
Homo sapiens (P49789)
brenda
Asensio, A.C.; Rodriguez-Ferrer, C.R.; Oaknin, S.; Rotllan, P.
Biochemical and immunochemical characterisation of human diadenosine triphosphatase provides evidence for its identification with the tumour suppressor Fhit protein
Biochimie
88
461-471
2006
Homo sapiens, Rattus norvegicus
brenda
Nakagawa, Y.; Akao, Y.
Fhit protein inhibits cell growth by attenuating the signaling mediated by nuclear factor-kappaB in colon cancer cell lines
Exp. Cell Res.
312
2433-2442
2006
Homo sapiens
brenda
Zhao, P.; Hou, N.; Lu, Y.
Fhit protein is preferentially expressed in the nucleus of monocyte-derived cells and its possible biological significance
Histol. Histopathol.
21
915-923
2006
Homo sapiens
brenda
Oezkara, S.K.; Corakci, A.
FHIT expression in neoplastic, hyperplastic, and normal endometrium
Int. J. Gynecol. Cancer
15
1081-1088
2005
Homo sapiens
brenda
Guranowski, A.; Wojdyla, A.M.; Pietrowska-Borek, M.; Bieganowski, P.; Khurs, E.N.; Cliff, M.J.; Blackburn, G.M.; Blaziak, D.; Stec, W.J.
Fhit proteins can also recognize substrates other than dinucleoside polyphosphates
FEBS Lett.
582
3152-3158
2008
Arabidopsis thaliana (Q9LVM4), Homo sapiens
brenda
Mirandola, P.; Gobbi, G.; Sponzilli, I.; Malinverno, C.; Cavazzoni, A.; Alfieri, R.; Petronini, P.G.; Vitale, M.
TRAIL-induced apoptosis of FHIT-negative lung cancer cells is inhibited by FHIT re-expression
J. Cell. Physiol.
220
493-498
2009
Homo sapiens
brenda
Banerjee, H.; Palenchar, J.B.; Lukaszewicz, M.; Bojarska, E.; Stepinski, J.; Jemielity, J.; Guranowski, A.; Ng, S.; Wah, D.A.; Darzynkiewicz, E.; Bellofatto, V.
Identification of the HIT-45 protein from Trypanosoma brucei as an FHIT protein/dinucleoside triphosphatase: substrate specificity studies on the recombinant and endogenous proteins
RNA
15
1554-1564
2009
Trypanosoma brucei, Trypanosoma brucei 427
brenda
Martin, J.; St-Pierre, M.V.; Dufour, J.F.
Hit proteins, mitochondria and cancer
Biochim. Biophys. Acta
1807
626-632
2011
Homo sapiens (P49789)
brenda
Krakowiak, A.; Pecherzewska, R.; Kaczmarek, R.; Tomaszewska, A.; Nawrot, B.; Stec, W.J.
Evaluation of influence of Ap4A analogues on Fhit-positive HEK293T cells; cytotoxicity and ability to induce apoptosis
Bioorg. Med. Chem.
19
5053-5060
2011
Homo sapiens (P49789)
brenda
Guranowski, A.; Wojdyla, A.; Zimny, J.; Wypijewska, A.; Kowalska, J.; Lukaszewicz, M.; Jemielity, J.; Darzynkiewicz, E.; Jagiello, A.; Bieganowski, P.
Recognition of different nucleotidyl-derivatives as substrates of reactions catalyzed by various HIT-proteins
New J. Chem.
34
888-893
2010
Trypanosoma brucei, Homo sapiens, Arabidopsis thaliana
-
brenda
Lopez, V.; Lee, S.Y.; Stephan, H.; Mueller, C.E.
Recombinant expression of ecto-nucleotide pyrophosphatase/phosphodiesterase 4 (NPP4) and development of a luminescence-based assay to identify inhibitors
Anal. Biochem.
603
113774
2020
Homo sapiens (Q9Y6X5)
brenda
Albrecht, C.J.; Stumpf, F.M.; Krueger, L.; Niedermeier, M.L.; Stengel, F.; Marx, A.
Chemical proteomics reveals interactors of the alarmone diadenosine triphosphate in the cancer cell line H1299
J. Pept. Sci.
29
e3458
2023
Homo sapiens (P49789)
brenda
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