BRENDA - Enzyme Database
show all sequences of 3.6.1.17

Characterisation of a bis(5-nucleosyl)-tetraphosphatase (asymmetrical) from Drosophila melanogaster

Winward, L.; Whitfield, W.G.; Woodman, T.J.; McLennan, A.G.; Safrany, S.T.; Int. J. Biochem. Cell Biol. 39, 943-954 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, sequence comparison, expression of His-tagged Apf in Spodoptera frugiperda Sf21 cells, expression of EGFP-tagged enzyme in Drosophila melanbogaster Mel-2 cells
Drosophila melanogaster
Inhibitors
Inhibitors
Commentary
Organism
Structure
fluoride
fluoride potently inhibits diadenosine tetraphosphate hydrolysis in the presence of Mg2+, whereas it is ineffective in the presence of Zn2+, because inhibition involves a specific, MgF3--containing transition state analogue complex, overview
Drosophila melanogaster
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics strongly depend on pH and cation, overview
Drosophila melanogaster
0.009
-
5',5'-diadenosine tetraphosphate
pH 6.5, 1 mm Zn2+
Drosophila melanogaster
0.012
-
5',5'-diadenosine tetraphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
0.015
-
5',5'-diadenosine hexaphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
nucleus
association with euchromatin and facultative heterochromatin
Drosophila melanogaster
5634
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
the enzyme is dependent on divalent cations
Drosophila melanogaster
Mg2+
the enzyme is dependent on divalent cations, preferred cation, best at 3-10 mM
Drosophila melanogaster
Mn2+
the enzyme is dependent on divalent cations
Drosophila melanogaster
additional information
no activation by Cu2+, Fe2+, Ni2+ or Ca2+
Drosophila melanogaster
Zn2+
the enzyme is dependent on divalent cations, high activity
Drosophila melanogaster
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5',5'-diadenosine tetraphosphate + H2O
Drosophila melanogaster
-
ATP + AMP
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Drosophila melanogaster
Q4V6M1
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged Apf from Spodoptera frugiperda Sf21 cells by nickel affinity chromatography with removal of the His-tag
Drosophila melanogaster
Source Tissue
Source Tissue
Commentary
Organism
Textmining
additional information
patterns of Apf expression in Drosophila melanogaster tissues, semi-quantitative RT-PCR, highest expression levels in embryos and adult females, overview
Drosophila melanogaster
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Drosophila melanogaster
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5',5'-diadenosine hexaphosphate + H2O
diadenosine hexaphosphate is efficiently hydrolysed to ATP only at pH 7.5 with 20 mM Mg2+
687119
Drosophila melanogaster
2 ATP
-
-
-
?
5',5'-diadenosine pentaphosphate + H2O
-
687119
Drosophila melanogaster
ATP + ADP
-
-
-
?
5',5'-diadenosine tetraphosphate + H2O
-
687119
Drosophila melanogaster
ATP + AMP
-
-
-
?
5',5'-diadenosine tetraphosphate + H2O
best substrate
687119
Drosophila melanogaster
ATP + AMP
-
-
-
?
adenosine-5'-pentaphospho-5'-guanosine + H2O
-
687119
Drosophila melanogaster
?
-
-
-
?
adenosine-5'-tetraphospho-5'-guanosine + H2O
-
687119
Drosophila melanogaster
?
-
-
-
?
additional information
Apf always produces an NTP product, with substrate preference depending on pH and divalent ion
687119
Drosophila melanogaster
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
the enzyme contains a Nudix motif
Drosophila melanogaster
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
40
broad optimum
Drosophila melanogaster
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
60
65% of maximal activity at 52°C
Drosophila melanogaster
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
-
20 min, 55% remaining activity
Drosophila melanogaster
95
-
20 min, 1 mM Mn2+, a little amount of activity is remaining
Drosophila melanogaster
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4
-
5',5'-diadenosine hexaphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
13
-
5',5'-diadenosine tetraphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
43
-
5',5'-diadenosine tetraphosphate
pH 6.5, 1 mM Zn2+
Drosophila melanogaster
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7.5
activity depends on the substrate and the divalent cation
Drosophila melanogaster
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.02
-
in presence of Mg2+
Drosophila melanogaster
fluoride
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, sequence comparison, expression of His-tagged Apf in Spodoptera frugiperda Sf21 cells, expression of EGFP-tagged enzyme in Drosophila melanbogaster Mel-2 cells
Drosophila melanogaster
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.02
-
in presence of Mg2+
Drosophila melanogaster
fluoride
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
fluoride
fluoride potently inhibits diadenosine tetraphosphate hydrolysis in the presence of Mg2+, whereas it is ineffective in the presence of Zn2+, because inhibition involves a specific, MgF3--containing transition state analogue complex, overview
Drosophila melanogaster
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics strongly depend on pH and cation, overview
Drosophila melanogaster
0.009
-
5',5'-diadenosine tetraphosphate
pH 6.5, 1 mm Zn2+
Drosophila melanogaster
0.012
-
5',5'-diadenosine tetraphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
0.015
-
5',5'-diadenosine hexaphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
nucleus
association with euchromatin and facultative heterochromatin
Drosophila melanogaster
5634
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
the enzyme is dependent on divalent cations
Drosophila melanogaster
Mg2+
the enzyme is dependent on divalent cations, preferred cation, best at 3-10 mM
Drosophila melanogaster
Mn2+
the enzyme is dependent on divalent cations
Drosophila melanogaster
additional information
no activation by Cu2+, Fe2+, Ni2+ or Ca2+
Drosophila melanogaster
Zn2+
the enzyme is dependent on divalent cations, high activity
Drosophila melanogaster
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5',5'-diadenosine tetraphosphate + H2O
Drosophila melanogaster
-
ATP + AMP
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged Apf from Spodoptera frugiperda Sf21 cells by nickel affinity chromatography with removal of the His-tag
Drosophila melanogaster
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
additional information
patterns of Apf expression in Drosophila melanogaster tissues, semi-quantitative RT-PCR, highest expression levels in embryos and adult females, overview
Drosophila melanogaster
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Drosophila melanogaster
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5',5'-diadenosine hexaphosphate + H2O
diadenosine hexaphosphate is efficiently hydrolysed to ATP only at pH 7.5 with 20 mM Mg2+
687119
Drosophila melanogaster
2 ATP
-
-
-
?
5',5'-diadenosine pentaphosphate + H2O
-
687119
Drosophila melanogaster
ATP + ADP
-
-
-
?
5',5'-diadenosine tetraphosphate + H2O
-
687119
Drosophila melanogaster
ATP + AMP
-
-
-
?
5',5'-diadenosine tetraphosphate + H2O
best substrate
687119
Drosophila melanogaster
ATP + AMP
-
-
-
?
adenosine-5'-pentaphospho-5'-guanosine + H2O
-
687119
Drosophila melanogaster
?
-
-
-
?
adenosine-5'-tetraphospho-5'-guanosine + H2O
-
687119
Drosophila melanogaster
?
-
-
-
?
additional information
Apf always produces an NTP product, with substrate preference depending on pH and divalent ion
687119
Drosophila melanogaster
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme contains a Nudix motif
Drosophila melanogaster
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
40
broad optimum
Drosophila melanogaster
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
60
65% of maximal activity at 52°C
Drosophila melanogaster
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
-
20 min, 55% remaining activity
Drosophila melanogaster
95
-
20 min, 1 mM Mn2+, a little amount of activity is remaining
Drosophila melanogaster
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4
-
5',5'-diadenosine hexaphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
13
-
5',5'-diadenosine tetraphosphate
pH 7.5, 20 mM Mg2+
Drosophila melanogaster
43
-
5',5'-diadenosine tetraphosphate
pH 6.5, 1 mM Zn2+
Drosophila melanogaster
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7.5
activity depends on the substrate and the divalent cation
Drosophila melanogaster
Other publictions for EC 3.6.1.17
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733091
Wu
Elucidating diphosphoinositol ...
Homo sapiens
Angew. Chem. Int. Ed. Engl.
53
7192-7197
2014
-
-
-
-
-
-
3
-
-
-
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-
-
1
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2
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3
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3
3
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-
2
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
733346
Barta
Chlamydia trachomatis CT771 (n ...
Chlamydia trachomatis
Biochemistry
53
214-224
2014
-
-
-
1
-
-
-
6
-
2
-
-
-
6
-
-
-
-
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-
-
-
1
-
-
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6
-
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1
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6
-
2
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-
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-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
6
6
733872
Sasaki
Enzymatic characteristics of a ...
Myxococcus xanthus, Myxococcus xanthus DK 1622
FEBS Lett.
588
3395-3402
2014
-
-
-
-
-
-
5
2
-
2
-
-
-
2
-
-
-
-
-
-
-
-
6
-
-
-
-
2
-
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-
-
-
-
-
5
-
2
-
2
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
2
-
-
-
-
-
-
-
-
2
2
733257
Ge
Crystal structure of wild-type ...
Homo sapiens
Biochem. Biophys. Res. Commun.
432
16-21
2013
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733450
Osman
Molecular characterization and ...
Plasmodium falciparum
Biol. Pharm. Bull.
35
1191-1196
2012
-
-
1
-
2
-
-
3
-
5
1
-
-
1
-
-
-
-
-
-
-
-
2
1
1
-
1
3
1
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
3
-
5
1
-
-
-
-
-
-
-
-
-
2
1
1
-
1
3
1
-
-
-
-
-
-
-
-
-
733563
Albright
NPP4 is a procoagulant enzyme ...
Homo sapiens
Blood
120
4432-4440
2012
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
719339
Arczewska
Caenorhabditis elegans NDX-4 i ...
Caenorhabditis elegans, Caenorhabditis elegans Bristol N2
DNA Repair
10
176-187
2011
-
-
1
-
-
-
-
5
-
-
-
-
-
6
-
-
1
-
-
-
-
-
10
-
-
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
1
-
-
-
-
10
-
-
-
-
5
-
-
-
-
-
2
2
-
5
5
710715
Jeyakanthan
Free and ATP-bound structures ...
Aquifex aeolicus
Acta Crystallogr. Sect. D
66
116-124
2010
-
-
1
1
-
-
-
3
-
-
-
-
-
3
-
-
1
-
-
-
-
-
3
-
-
-
-
3
-
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-
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-
1
-
1
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3
-
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-
1
-
-
-
-
3
-
-
-
-
3
-
-
-
-
-
-
-
-
3
3
713580
Vasilenko
SARS coronavirus protein 7a in ...
Homo sapiens
Virol. J.
7
31
2010
-
-
-
-
-
-
-
-
1
-
-
1
-
4
-
-
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-
-
1
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1
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1
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1
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-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
697896
Guranowski
Novel diadenosine polyphosphat ...
Homo sapiens, Lupinus angustifolius
FEBS J.
276
1546-1553
2009
-
-
-
-
-
-
4
2
-
2
-
2
-
2
-
-
1
-
-
-
-
-
6
-
2
-
-
-
2
-
-
-
4
-
-
-
-
-
-
-
-
-
-
4
4
2
-
2
-
2
-
-
-
1
-
-
-
-
6
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
711209
Branson
Discovery of inhibitors of lup ...
Lupinus angustifolius
Biochemistry
48
7614-7620
2009
-
-
-
-
-
-
7
-
-
-
-
-
-
1
-
-
-
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-
-
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1
-
-
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-
-
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3
-
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7
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
695301
Szurmak
A diadenosine 5',5''-P1P4 tetr ...
Arabidopsis thaliana
Acta Biochim. Pol.
55
151-160
2008
-
-
1
-
-
-
-
-
-
5
1
4
-
3
-
-
1
-
-
-
6
-
4
-
-
-
-
-
1
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
5
1
4
-
-
-
1
-
-
6
-
4
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
687119
Winward
Characterisation of a bis(5-nu ...
Drosophila melanogaster
Int. J. Biochem. Cell Biol.
39
943-954
2007
-
-
1
-
-
-
1
4
1
5
-
1
-
3
-
-
1
-
-
1
1
-
7
1
1
1
2
3
1
-
-
-
-
-
1
-
-
1
-
-
-
-
1
1
-
4
1
5
-
1
-
-
-
1
-
1
1
-
7
1
1
1
2
3
1
-
-
-
-
-
-
-
-
-
669427
Swarbrick
Structure and substrate-bindin ...
Homo sapiens
J. Biol. Chem.
280
8471-8481
2005
-
-
1
1
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
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Minelli
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Swarbrick
1H, 13C and 15N backbone of th ...
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Maksel
Cloning and expression of diad ...
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Nuclear location of a diadenos ...
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Diadenosine 5',5'''-P1,P4-tetr ...
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Lanterns of firefly Photinus p ...
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Guranowski
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Lazewska
Human placental (asymmetrical) ...
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Robinson
Isolation and charcterization ...
Saccharomyces cerevisiae
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Pinto
Dinucleoside tetraphosphatase ...
Homo sapiens, Rattus norvegicus
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Guranowski
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Costas
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Costas
Mitochondrial location of rat ...
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Cameselle
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Cameselle
Dinucleosidetetraphosphatase i ...
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Moreno
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Cameselle
Bis-(5-guanosyl) tetraphosphat ...
Rattus norvegicus
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Vallejo
Dinucleosidasetetraphosphatase ...
Artemia salina, Rattus norvegicus
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Vallejo
Diguanosinetetraphosphate guan ...
Artemia salina
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Warner
Isolation, purification, and c ...
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