BRENDA - Enzyme Database
show all sequences of 3.6.1.13

Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies

Zha, M.; Guo, Q.; Zhang, Y.; Yu, B.; Ou, Y.; Zhong, C.; Ding, J.; J. Mol. Biol. 379, 568-578 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
; overexpression of wild-type and mutant enzymes
Homo sapiens
Crystallization (Commentary)
Crystallization
Organism
in complex with alpha,beta-methyleneadenosine diphosphoribose and 3 Mg2+ ions, hanging drop vapor diffusion method, using 250 mM sodium acetate, 100 mM Tris-HCl, pH 8.0, and 29% (w/v) polyethylene glycol 4000; purified recombinant wild-type and truncated mutant NUDT5 in complex with a non-hydrolyzable ADPR analogue, alpha,beta-methyleneadenosine diphosphoribose, and three Mg2+ ions representing the transition state of the enzyme during catalysis, 20 mg/ml protein is incubated with 5 mM AMPCPR and 10 mM MgCl2 at 4 °C overnight, followed by hanging drop vapour diffusion method, wild-type enzyme in complex with AMPCPR, and truncation mutant DELTAhNUDT5 in complex with AMPCPR and Mg2+, 4 °C, mixing of equal volumes of the protein solution and the reservoir solution containing 250 mM NaAc, 100 mM Tris-HCl, pH 8.0, and 29% PEG 4000, ingle crystals of the plate-shape morphology grow after 1 month, X-ray diffraction structure determination and anaylsis at 2.0 A resolution, molecular modelling
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
C139A
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D133A
site-directed mutagenesis, mutation causes a 4.0fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D133N
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D164A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D164N
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Homo sapiens
E112Q
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E115Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E116Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E166Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E93Q
site-directed mutagenesis, mutation causes a 1.8fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
L98A
site-directed mutagenesis, mutation of Leu98 to Ala causes a 5.8fold increase in Km but has no effect on kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
additional information
construction of a truncation mutant DELTAhNUDT5
Homo sapiens
Q82A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R111Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R196Q
site-directed mutagenesis, mutation causes a 5.5fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R51Q
site-directed mutagenesis, the mutant shows a 14.6fold increased Km and a 17fold decreased kcat for ADP-ribose compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R84Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
W28A
site-directed mutagenesis, the mutant shows 8.4fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
W28A/W46A
site-directed mutagenesis, the mutant shows 53.7fold increased Km and a 219fold decreased kcat for ADP-ribose compared to the wild-type enzyme; the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
W46A
site-directed mutagenesis, the mutant shows 5.7fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme; the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis, Trp28 and Trp46 function synergistically in substrate binding and catalysis, overview
Homo sapiens
0.0209
-
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
Homo sapiens
0.0223
-
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
Homo sapiens
0.0223
-
ADP-ribose
pH 7.0, 37°C, wild-type enzyme
Homo sapiens
0.0231
-
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
Homo sapiens
0.0257
-
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
Homo sapiens
0.0279
-
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
Homo sapiens
0.0389
-
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
Homo sapiens
0.0402
-
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
Homo sapiens
0.0434
-
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
Homo sapiens
0.0456
-
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
Homo sapiens
0.0463
-
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
Homo sapiens
0.0702
-
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
Homo sapiens
0.0879
-
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
Homo sapiens
0.1084
-
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
Homo sapiens
0.1197
-
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
Homo sapiens
0.1265
-
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
Homo sapiens
0.1271
-
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
Homo sapiens
0.1283
-
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
Homo sapiens
0.1497
-
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
Homo sapiens
0.184
-
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
Homo sapiens
0.3213
-
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ADP-D-ribose + H2O
Homo sapiens
-
AMP + D-ribose 5-phosphate
-
-
?
ADP-ribose + H2O
Homo sapiens
the enzyme plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5?-phosphate
AMP + D-ribose 5-phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Homo sapiens
Q9UKK9
-
-
Purification (Commentary)
Commentary
Organism
-
Homo sapiens
Reaction
Reaction
Commentary
Organism
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
molecular catalytic mechanism involving Arg51, Arg111, Glu112, and Glu116, active site structure, substrate binding involving Arg51, Leu98, Trp28 and Trp46 and transition-state structure, structure-function relationship, and kinetic analysis
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP-D-ribose + H2O
-
688413
Homo sapiens
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
preferred substrate
688413
Homo sapiens
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
the enzyme plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5?-phosphate
688413
Homo sapiens
AMP + D-ribose 5-phosphate
-
-
-
?
additional information
hNUDT5 can utilize a variety of ADP-sugar conjugates as substrate, with a preference for ADPR
688413
Homo sapiens
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
homodimer
Homo sapiens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0019
-
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
Homo sapiens
0.0069
-
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
Homo sapiens
0.058
-
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
Homo sapiens
0.1
-
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
Homo sapiens
0.18
-
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
Homo sapiens
0.32
-
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
Homo sapiens
0.41
-
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
Homo sapiens
2.7
-
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
Homo sapiens
4.5
-
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
Homo sapiens
6
-
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
Homo sapiens
7.3
-
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
Homo sapiens
10.3
-
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
Homo sapiens
10.4
-
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
Homo sapiens
11.3
-
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
Homo sapiens
11.4
-
ADP-ribose
pH 7.0, 37°C, wild-type enzyme
Homo sapiens
11.8
-
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
Homo sapiens
12.2
-
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
Homo sapiens
12.4
-
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
Homo sapiens
13.1
-
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
Homo sapiens
13.3
-
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
Homo sapiens
13.7
-
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
overexpression of wild-type and mutant enzymes
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
in complex with alpha,beta-methyleneadenosine diphosphoribose and 3 Mg2+ ions, hanging drop vapor diffusion method, using 250 mM sodium acetate, 100 mM Tris-HCl, pH 8.0, and 29% (w/v) polyethylene glycol 4000
Homo sapiens
purified recombinant wild-type and truncated mutant NUDT5 in complex with a non-hydrolyzable ADPR analogue, alpha,beta-methyleneadenosine diphosphoribose, and three Mg2+ ions representing the transition state of the enzyme during catalysis, 20 mg/ml protein is incubated with 5 mM AMPCPR and 10 mM MgCl2 at 4 °C overnight, followed by hanging drop vapour diffusion method, wild-type enzyme in complex with AMPCPR, and truncation mutant DELTAhNUDT5 in complex with AMPCPR and Mg2+, 4 °C, mixing of equal volumes of the protein solution and the reservoir solution containing 250 mM NaAc, 100 mM Tris-HCl, pH 8.0, and 29% PEG 4000, ingle crystals of the plate-shape morphology grow after 1 month, X-ray diffraction structure determination and anaylsis at 2.0 A resolution, molecular modelling
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C139A
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
Homo sapiens
C139A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D133A
site-directed mutagenesis, mutation causes a 4.0fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
Homo sapiens
D133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D133N
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
Homo sapiens
D133N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D164A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
D164N
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Homo sapiens
E112Q
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E115Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E116Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E166Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
E93Q
site-directed mutagenesis, mutation causes a 1.8fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
Homo sapiens
E93Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
L98A
site-directed mutagenesis, mutation of Leu98 to Ala causes a 5.8fold increase in Km but has no effect on kcat compared to the wild-type enzyme
Homo sapiens
L98A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
additional information
construction of a truncation mutant DELTAhNUDT5
Homo sapiens
Q82A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R111Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R196Q
site-directed mutagenesis, mutation causes a 5.5fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
Homo sapiens
R196Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R51Q
site-directed mutagenesis, the mutant shows a 14.6fold increased Km and a 17fold decreased kcat for ADP-ribose compared to the wild-type enzyme
Homo sapiens
R51Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
R84Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
W28A
site-directed mutagenesis, the mutant shows 8.4fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme
Homo sapiens
W28A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
W28A/W46A
site-directed mutagenesis, the mutant shows 53.7fold increased Km and a 219fold decreased kcat for ADP-ribose compared to the wild-type enzyme
Homo sapiens
W28A/W46A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
W46A
site-directed mutagenesis, the mutant shows 5.7fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme
Homo sapiens
W46A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis, Trp28 and Trp46 function synergistically in substrate binding and catalysis, overview
Homo sapiens
0.0209
-
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
Homo sapiens
0.0223
-
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
Homo sapiens
0.0223
-
ADP-ribose
pH 7.0, 37°C, wild-type enzyme
Homo sapiens
0.0231
-
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
Homo sapiens
0.0257
-
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
Homo sapiens
0.0279
-
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
Homo sapiens
0.0389
-
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
Homo sapiens
0.0402
-
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
Homo sapiens
0.0434
-
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
Homo sapiens
0.0456
-
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
Homo sapiens
0.0463
-
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
Homo sapiens
0.0702
-
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
Homo sapiens
0.0879
-
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
Homo sapiens
0.1084
-
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
Homo sapiens
0.1197
-
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
Homo sapiens
0.1265
-
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
Homo sapiens
0.1271
-
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
Homo sapiens
0.1283
-
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
Homo sapiens
0.1497
-
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
Homo sapiens
0.184
-
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
Homo sapiens
0.3213
-
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ADP-D-ribose + H2O
Homo sapiens
-
AMP + D-ribose 5-phosphate
-
-
?
ADP-ribose + H2O
Homo sapiens
the enzyme plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5?-phosphate
AMP + D-ribose 5-phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP-D-ribose + H2O
-
688413
Homo sapiens
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
preferred substrate
688413
Homo sapiens
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
the enzyme plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5?-phosphate
688413
Homo sapiens
AMP + D-ribose 5-phosphate
-
-
-
?
additional information
hNUDT5 can utilize a variety of ADP-sugar conjugates as substrate, with a preference for ADPR
688413
Homo sapiens
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
homodimer
Homo sapiens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0019
-
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
Homo sapiens
0.0069
-
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
Homo sapiens
0.058
-
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
Homo sapiens
0.1
-
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
Homo sapiens
0.18
-
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
Homo sapiens
0.32
-
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
Homo sapiens
0.41
-
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
Homo sapiens
2.7
-
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
Homo sapiens
4.5
-
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
Homo sapiens
6
-
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
Homo sapiens
7.3
-
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
Homo sapiens
10.3
-
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
Homo sapiens
10.4
-
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
Homo sapiens
11.3
-
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
Homo sapiens
11.4
-
ADP-ribose
pH 7.0, 37°C, wild-type enzyme
Homo sapiens
11.8
-
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
Homo sapiens
12.2
-
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
Homo sapiens
12.4
-
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
Homo sapiens
13.1
-
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
Homo sapiens
13.3
-
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
Homo sapiens
13.7
-
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Homo sapiens
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0027
-
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
Homo sapiens
0.005
-
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
Homo sapiens
0.23
-
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
Homo sapiens
1.2
-
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
Homo sapiens
1.7
-
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
Homo sapiens
4.3
-
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
Homo sapiens
13
-
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
Homo sapiens
50
-
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
Homo sapiens
67
-
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
Homo sapiens
72
-
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
Homo sapiens
81
-
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
Homo sapiens
83
-
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
Homo sapiens
89
-
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
Homo sapiens
97
-
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
Homo sapiens
120
-
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
Homo sapiens
230
-
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
Homo sapiens
300
-
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
Homo sapiens
390
-
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
Homo sapiens
530
-
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
Homo sapiens
630
-
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
Homo sapiens
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0027
-
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
Homo sapiens
0.005
-
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
Homo sapiens
0.23
-
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
Homo sapiens
1.2
-
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
Homo sapiens
1.7
-
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
Homo sapiens
4.3
-
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
Homo sapiens
13
-
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
Homo sapiens
50
-
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
Homo sapiens
67
-
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
Homo sapiens
72
-
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
Homo sapiens
81
-
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
Homo sapiens
83
-
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
Homo sapiens
89
-
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
Homo sapiens
97
-
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
Homo sapiens
120
-
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
Homo sapiens
230
-
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
Homo sapiens
300
-
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
Homo sapiens
390
-
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
Homo sapiens
530
-
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
Homo sapiens
630
-
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
Homo sapiens
Other publictions for EC 3.6.1.13
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)
735009
Cabezas
Molecular bases of catalysis a ...
Homo sapiens
PLoS ONE
10
e0118680
2015
-
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1
13
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42
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7
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4
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44
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13
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42
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4
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44
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54
54
734285
Karuppiah
Structure and mechanism of the ...
Thermus thermophilus, Thermus thermophilus DSM 579
J. Biol. Chem.
289
33187-33197
2014
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718517
Okazaki
Crystallization and preliminar ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Acta Crystallogr. Sect. F
68
49-52
2012
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1
1
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2
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5
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735057
Rodrigues
Characterization of Danio reri ...
Danio rerio
PLoS ONE
7
e42249
2012
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1
1
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13
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1
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4
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8
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8
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13
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13
13
715407
Ito
Cleavage of oxidized guanine n ...
Homo sapiens
J. Biochem.
149
731-738
2011
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1
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5
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1
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1
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3
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2
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-
741073
Arimori
Diverse substrate recognition ...
Homo sapiens
Nucleic Acids Res.
39
8972-8983
2011
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1
1
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1
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1
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1
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3
-
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-
-
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-
720769
Ishikawa
Distinct regulation of Arabido ...
Arabidopsis thaliana
Plant Signal. Behav.
5
839-841
2010
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1
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1
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-
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1
1
1
1
-
-
700755
Ogawa
Overexpression of an ADP-ribos ...
Arabidopsis thaliana
Plant J.
57
289-301
2009
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1
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1
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2
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-
-
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710725
Goncalves
Structure of an N-terminally t ...
Deinococcus radiodurans
Acta Crystallogr. Sect. F
65
1083-1087
2009
-
-
1
1
-
-
-
-
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1
-
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2
-
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1
-
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1
-
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1
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1
-
1
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1
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-
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1
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
687404
Wakamatsu
Structural basis for different ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Bacteriol.
190
1108-1117
2008
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1
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6
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-
1
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-
-
-
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8
-
1
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4
1
1
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-
-
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1
-
1
-
-
-
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4
-
1
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4
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1
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-
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-
8
-
1
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4
1
1
-
-
-
-
-
-
-
-
688413
Zha
Molecular mechanism of ADP-rib ...
Homo sapiens
J. Mol. Biol.
379
568-578
2008
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-
1
1
20
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22
1
1
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1
1
-
-
-
-
4
1
1
-
-
21
1
-
-
-
-
-
-
-
-
2
-
2
30
-
-
-
-
22
1
1
-
2
-
-
-
1
-
-
-
-
4
1
1
-
-
21
1
-
-
-
-
-
-
-
20
20
690090
Huang
Bifunctional NMN adenylyltrans ...
Francisella tularensis, Synechocystis sp.
Structure
16
196-209
2008
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2
2
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-
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2
-
2
-
6
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2
2
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-
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6
2
2
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-
-
2
-
-
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-
-
-
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2
-
2
-
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2
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2
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2
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-
6
2
2
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2
-
-
-
-
-
-
-
-
-
684834
Yu
Activation of NUDT5, an ADP-ri ...
Homo sapiens
Biochem. Biophys. Res. Commun.
354
764-768
2007
1
-
1
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1
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1
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2
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1
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2
-
1
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1
-
1
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-
-
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1
-
1
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1
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-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
690189
Ge
AcMNPV ORF38 protein has the a ...
Autographa californica multiple nucleopolyhedrovirus
Virology
361
204-211
2007
-
-
1
-
-
-
-
1
-
1
-
1
-
3
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-
1
-
-
-
-
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1
-
-
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-
1
1
-
-
-
-
-
-
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-
1
-
-
-
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-
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-
1
-
1
-
1
-
-
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1
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-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
667823
Carloto
The specific, submicromolar-K( ...
Homo sapiens
Biochim. Biophys. Acta
1760
1545-1551
2006
-
-
-
-
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2
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4
1
1
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2
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1
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2
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2
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1
1
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1
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2
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2
-
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-
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-
-
-
-
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670632
Jambunathan
Analysis of Arabidopsis growth ...
Arabidopsis sp.
Planta
224
1-11
2006
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1
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1
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1
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1
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-
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715902
Zha
Crystal structures of human NU ...
Homo sapiens
J. Mol. Biol.
364
1021-1033
2006
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1
1
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1
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1
1
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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
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-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667690
Ooga
Molecular mechanism of the The ...
Thermus thermophilus
Biochemistry
44
9320-9329
2005
-
-
-
1
21
-
1
22
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-
-
-
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3
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1
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-
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4
-
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29
-
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2
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-
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1
21
-
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1
2
22
-
-
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1
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-
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4
-
-
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29
-
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-
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669102
Okuda
Systematic characterization of ...
Synechocystis sp.
J. Bacteriol.
187
4984-4991
2005
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1
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-
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1
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4
-
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3
-
-
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1
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3
-
1
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1
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1
-
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-
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4
-
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3
-
-
-
-
-
-
-
-
-
-
669355
Ogawa
Comprehensive analysis of cyto ...
Arabidopsis thaliana
J. Biol. Chem.
280
25277-25283
2005
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1
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4
1
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7
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1
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3
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4
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3
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1
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4
1
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1
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3
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4
-
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3
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-
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-
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-
654895
Okuda
Identification and characteriz ...
Synechococcus sp.
Biochim. Biophys. Acta
1699
245-252
2004
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1
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1
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3
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1
-
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2
1
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1
1
1
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1
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1
-
-
-
-
-
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-
1
-
3
3
-
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-
-
1
-
-
-
-
2
1
-
-
-
1
1
1
-
1
-
-
-
-
-
-
656238
Yoshiba
Structural insights into the T ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biol. Chem.
279
37163-37174
2004
-
-
-
1
6
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Canales
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The hydrolysis of adenosine di ...
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