BRENDA - Enzyme Database
show all sequences of 3.6.1.17

Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus

Sasaki, M.; Takegawa, K.; Kimura, Y.; FEBS Lett. 588, 3395-3402 (2014)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
5 mM, 13.2% residual activity
Myxococcus xanthus
glycerol phosphate
20 mM, 46.1% residual activity
Myxococcus xanthus
iodoacetic acid
10 mM, 58.8% residual activity
Myxococcus xanthus
N-ethylmaleimide
1 mM, 73.8% residual activity
Myxococcus xanthus
trisodium phosphate
20 mM, 24.8% residual activity
Myxococcus xanthus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.14
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
0.19
-
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
about 50% of the activity with Mn2+. In the presence of Mn2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate mainly into AMP and ATP, whereas in the presence of Co2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17
Myxococcus xanthus
Mn2+
best activator. In the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17
Myxococcus xanthus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Myxococcus xanthus
Q1DC62
-
-
Myxococcus xanthus DK 1622
Q1DC62
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
PrpA exhibits a phosphatase activity towards p-nitrophenyl phosphate, tyrosine phosphopeptide and tyrosine-phosphorylated protein and a weak hydrolase activity towards ATP
733872
Myxococcus xanthus
?
-
-
-
-
additional information
PrpA exhibits a phosphatase activity towards p-nitrophenyl phosphate, tyrosine phosphopeptide and tyrosine-phosphorylated protein and a weak hydrolase activity towards ATP
733872
Myxococcus xanthus DK 1622
?
-
-
-
-
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
733872
Myxococcus xanthus
AMP + ATP
in the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes Ap4A into two molecules of ADP, reaction of EC 3.6.1.41
-
-
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
733872
Myxococcus xanthus DK 1622
AMP + ATP
in the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes Ap4A into two molecules of ADP, reaction of EC 3.6.1.41
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
-
733872
Myxococcus xanthus
AMP + adenosine 5'-tetraphosphate
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
-
733872
Myxococcus xanthus DK 1622
AMP + adenosine 5'-tetraphosphate
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.035
-
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
0.055
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
5 mM, 13.2% residual activity
Myxococcus xanthus
glycerol phosphate
20 mM, 46.1% residual activity
Myxococcus xanthus
iodoacetic acid
10 mM, 58.8% residual activity
Myxococcus xanthus
N-ethylmaleimide
1 mM, 73.8% residual activity
Myxococcus xanthus
trisodium phosphate
20 mM, 24.8% residual activity
Myxococcus xanthus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.14
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
0.19
-
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
about 50% of the activity with Mn2+. In the presence of Mn2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate mainly into AMP and ATP, whereas in the presence of Co2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17
Myxococcus xanthus
Mn2+
best activator. In the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17
Myxococcus xanthus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
PrpA exhibits a phosphatase activity towards p-nitrophenyl phosphate, tyrosine phosphopeptide and tyrosine-phosphorylated protein and a weak hydrolase activity towards ATP
733872
Myxococcus xanthus
?
-
-
-
-
additional information
PrpA exhibits a phosphatase activity towards p-nitrophenyl phosphate, tyrosine phosphopeptide and tyrosine-phosphorylated protein and a weak hydrolase activity towards ATP
733872
Myxococcus xanthus DK 1622
?
-
-
-
-
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
733872
Myxococcus xanthus
AMP + ATP
in the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes Ap4A into two molecules of ADP, reaction of EC 3.6.1.41
-
-
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
733872
Myxococcus xanthus DK 1622
AMP + ATP
in the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes Ap4A into two molecules of ADP, reaction of EC 3.6.1.41
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
-
733872
Myxococcus xanthus
AMP + adenosine 5'-tetraphosphate
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
-
733872
Myxococcus xanthus DK 1622
AMP + adenosine 5'-tetraphosphate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.035
-
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
0.055
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.18
-
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
0.4
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.18
-
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
0.4
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
Myxococcus xanthus
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
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733346
Barta
Chlamydia trachomatis CT771 (n ...
Chlamydia trachomatis
Biochemistry
53
214-224
2014
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1
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6
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2
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6
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6
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6
6
733872
Sasaki
Enzymatic characteristics of a ...
Myxococcus xanthus, Myxococcus xanthus DK 1622
FEBS Lett.
588
3395-3402
2014
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5
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2
2
733257
Ge
Crystal structure of wild-type ...
Homo sapiens
Biochem. Biophys. Res. Commun.
432
16-21
2013
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733450
Osman
Molecular characterization and ...
Plasmodium falciparum
Biol. Pharm. Bull.
35
1191-1196
2012
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1
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2
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3
-
5
1
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1
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2
1
1
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3
1
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1
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2
1
1
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1
3
1
-
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733563
Albright
NPP4 is a procoagulant enzyme ...
Homo sapiens
Blood
120
4432-4440
2012
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1
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1
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1
1
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719339
Arczewska
Caenorhabditis elegans NDX-4 i ...
Caenorhabditis elegans, Caenorhabditis elegans Bristol N2
DNA Repair
10
176-187
2011
-
-
1
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-
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5
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6
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1
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10
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5
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1
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1
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10
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5
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2
2
-
5
5
710715
Jeyakanthan
Free and ATP-bound structures ...
Aquifex aeolicus
Acta Crystallogr. Sect. D
66
116-124
2010
-
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1
1
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3
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3
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3
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3
3
713580
Vasilenko
SARS coronavirus protein 7a in ...
Homo sapiens
Virol. J.
7
31
2010
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1
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4
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1
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1
1
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697896
Guranowski
Novel diadenosine polyphosphat ...
Homo sapiens, Lupinus angustifolius
FEBS J.
276
1546-1553
2009
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4
2
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2
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2
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1
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4
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4
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6
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2
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711209
Branson
Discovery of inhibitors of lup ...
Lupinus angustifolius
Biochemistry
48
7614-7620
2009
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7
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1
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1
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3
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1
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695301
Szurmak
A diadenosine 5',5''-P1P4 tetr ...
Arabidopsis thaliana
Acta Biochim. Pol.
55
151-160
2008
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1
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1
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6
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4
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1
1
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1
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687119
Winward
Characterisation of a bis(5-nu ...
Drosophila melanogaster
Int. J. Biochem. Cell Biol.
39
943-954
2007
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1
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1
4
1
5
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3
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7
1
1
1
2
3
1
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1
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1
1
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4
1
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1
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7
1
1
1
2
3
1
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669427
Swarbrick
Structure and substrate-bindin ...
Homo sapiens
J. Biol. Chem.
280
8471-8481
2005
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1
1
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654523
Guranowski
Adenosine-5'-O-phosphorylated ...
Homo sapiens, Lupinus angustifolius
Biochem. J.
373
635-640
2003
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14
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2
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2
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14
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14
14
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2
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656173
Abdelghany
Analysis of the catalytic and ...
Caenorhabditis elegans
J. Biol. Chem.
278
4435-4439
2003
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1
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16
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16
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2
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1
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15
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1
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16
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16
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1
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15
-
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657213
Minelli
Ecto-diadenosine polyphosphate ...
Homo sapiens
Prostate
51
1-9
2002
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2
3
1
3
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1
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1
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1
3
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Maksel
Cloning and expression of diad ...
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Nuclear location of a diadenos ...
Solanum lycopersicum
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Diadenosine 5',5'''-P1,P4-tetr ...
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McLennan
Lanterns of firefly Photinus p ...
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The green alga Scenedesmus obl ...
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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 ...
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Guranowski
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Costas
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Costas
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Cameselle
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Cameselle
Dinucleosidetetraphosphatase i ...
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Moreno
Dinucleosidetetraphosphatase f ...
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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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Lobaton
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Vallejo
Diguanosinetetraphosphate guan ...
Artemia salina
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Warner
Isolation, purification, and c ...
Artemia salina
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