Data extracted from this reference:
Cloned(Commentary)
expressed in Escherichia coli Rosetta2 (DE3) cells
Escherichia coli
Crystallization (Commentary)
sitting drop vapor diffusion method. Wild type enzyme in complex with ADP-D-ribose using 0.2 M potassium sodium tartrate tetrahydrate, 20% w/v polyethylene glycol 3350, double mutant N25A/D35A complexed with 2''-O-acetyl-ADP-D-ribose using 2 M ammonium sulfate, 0.1 M Bis-Tris pH 5.5, and mutant Y126A in complex with ADP-D-ribose using 2 M ammonium sulfate, 0.1 M Bis-Tris pH 5.5
Escherichia coli
Engineering
D35A
the mutant shows strongly reduced activity compared to the wild type enzyme
Escherichia coli
N25A
the mutant shows strongly reduced activity compared to the wild type enzyme
Escherichia coli
N25A/D35A
inactive
Escherichia coli
Y126A
inactive
Escherichia coli
KM Value [mM]
0.4306
2''-O-acetyl-ADP-D-ribose
wild type enzyme, at pH 7.5 and 25°C
Escherichia coli
1.358
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
Escherichia coli
2.74
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
Escherichia coli
Natural Substrates/ Products (Substrates)
2''-O-acetyl-ADP-D-ribose + H2O
Escherichia coli
specific substrate
ADP-D-ribose + acetate
?
Organism
Purification (Commentary)
Ni-NTA resin column chromatography and Superdex S200 gel filtration
Escherichia coli
Substrates and Products (Substrate)
2''-O-acetyl-ADP-D-ribose + H2O
751419
Escherichia coli
ADP-D-ribose + acetate
?
2''-O-acetyl-ADP-D-ribose + H2O
specific substrate
751419
Escherichia coli
ADP-D-ribose + acetate
?
Synonyms
O-acetyl-ADP-ribose deacetylase
Escherichia coli
Turnover Number [1/s]
0.2
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
Escherichia coli
0.814
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
Escherichia coli
1.31
2''-O-acetyl-ADP-D-ribose
wild type enzyme, at pH 7.5 and 25°C
Escherichia coli
Cloned(Commentary) (protein specific)
expressed in Escherichia coli Rosetta2 (DE3) cells
Escherichia coli
Crystallization (Commentary) (protein specific)
sitting drop vapor diffusion method. Wild type enzyme in complex with ADP-D-ribose using 0.2 M potassium sodium tartrate tetrahydrate, 20% w/v polyethylene glycol 3350, double mutant N25A/D35A complexed with 2''-O-acetyl-ADP-D-ribose using 2 M ammonium sulfate, 0.1 M Bis-Tris pH 5.5, and mutant Y126A in complex with ADP-D-ribose using 2 M ammonium sulfate, 0.1 M Bis-Tris pH 5.5
Escherichia coli
Engineering (protein specific)
D35A
the mutant shows strongly reduced activity compared to the wild type enzyme
Escherichia coli
N25A
the mutant shows strongly reduced activity compared to the wild type enzyme
Escherichia coli
N25A/D35A
inactive
Escherichia coli
Y126A
inactive
Escherichia coli
KM Value [mM] (protein specific)
0.4306
2''-O-acetyl-ADP-D-ribose
wild type enzyme, at pH 7.5 and 25°C
Escherichia coli
1.358
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
Escherichia coli
2.74
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
2''-O-acetyl-ADP-D-ribose + H2O
Escherichia coli
specific substrate
ADP-D-ribose + acetate
?
Purification (Commentary) (protein specific)
Ni-NTA resin column chromatography and Superdex S200 gel filtration
Escherichia coli
Substrates and Products (Substrate) (protein specific)
2''-O-acetyl-ADP-D-ribose + H2O
751419
Escherichia coli
ADP-D-ribose + acetate
?
2''-O-acetyl-ADP-D-ribose + H2O
specific substrate
751419
Escherichia coli
ADP-D-ribose + acetate
?
Turnover Number [1/s] (protein specific)
0.2
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
Escherichia coli
0.814
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
Escherichia coli
1.31
2''-O-acetyl-ADP-D-ribose
wild type enzyme, at pH 7.5 and 25°C
Escherichia coli
KCat/KM [mM/s]
0.073
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
Escherichia coli
0.599
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
Escherichia coli
3.042
2''-O-acetyl-ADP-D-ribose
wild type enzyme, at pH 7.5 and 25°C
Escherichia coli
KCat/KM [mM/s] (protein specific)
0.073
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
Escherichia coli
0.599
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
Escherichia coli
3.042
2''-O-acetyl-ADP-D-ribose
wild type enzyme, at pH 7.5 and 25°C
Escherichia coli
Other publictions for EC 3.1.1.106
750645
Agnew
MacroD1 is a promiscuous ADP- ...
Homo sapiens, Mus musculus
Front. Microbiol.
9
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2
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752262
Haikarainen
Development of an inhibitor s ...
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SLAS Discov.
23
255-263
2018
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1
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5
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3
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3
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1
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3
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1
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1
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5
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1
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3
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-
752189
Haikarainen
Proximal ADP-ribose hydrolysi ...
Trypanosoma brucei gambiense, Trypanosoma cruzi, Trypanosoma cruzi CL Brener
Sci. Rep.
6
24213
2016
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2
2
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9
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11
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2
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9
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6
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2
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2
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9
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2
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9
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-
751419
Zhang
Structural insights into the ...
Escherichia coli
J. Struct. Biol.
192
478-486
2015
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1
1
4
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3
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1
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1
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1
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2
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3
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1
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1
4
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3
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1
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1
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2
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3
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3
3
749471
Hirsch
Transition-state analysis of ...
Homo sapiens
ACS Chem. Biol.
9
2255-2262
2014
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1
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2
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2
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4
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2
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2
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1
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2
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2
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2
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2
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2
2
751688
Rosenthal
Macrodomain-containing protei ...
Homo sapiens
Nat. Struct. Mol. Biol.
20
502-507
2013
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3
-
1
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6
-
7
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3
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-
13
-
6
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-
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-
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3
-
-
1
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-
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6
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-
3
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13
-
-
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3
3
-
-
-
751029
Chen
Identification of macrodomain ...
Escherichia coli, Staphylococcus aureus, Homo sapiens
J. Biol. Chem.
286
13261-13271
2011
-
-
1
1
15
-
3
4
-
-
-
8
-
11
-
-
1
-
-
2
-
-
12
-
13
-
-
-
19
-
-
-
-
1
-
-
-
-
1
-
1
15
-
-
4
1
4
-
-
-
8
-
-
-
1
-
2
-
-
12
-
-
-
-
19
-
-
-
-
-
-
-
-
4
4
751030
Kasamatsu
Hydrolysis of O-acetyl-ADP-ri ...
Homo sapiens
J. Biol. Chem.
286
21110-21117
2011
-
-
-
-
-
-
4
1
-
1
-
1
-
1
-
-
-
-
-
-
-
-
6
1
3
-
-
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
3
4
-
1
-
1
-
1
-
-
-
-
-
-
-
-
6
1
-
-
-
-
1
-
-
-
-
-
-
-
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-
752026
Ono
The 39-kDa poly(ADP-ribose) g ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
103
16687-16691
2006
1
-
-
-
3
-
2
-
-
1
-
2
-
1
-
-
-
-
-
-
-
-
2
1
3
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
3
-
-
2
1
-
-
1
-
2
-
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-
-
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2
1
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-
751012
Rafty
-
Analysis of O-acetyl-ADP-ribo ...
Saccharomyces cerevisiae, Homo sapiens
J. Biol. Chem.
277
47114-47122
2002
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2
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4
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2
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3
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