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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.1.1.106
751029
Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases
J. Biol. Chem.
286
13261-13271
2011
Escherichia coli
21257746
3.1.1.106
751029
Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases
J. Biol. Chem.
286
13261-13271
2011
Staphylococcus aureus
21257746
3.1.1.106
751029
Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases
J. Biol. Chem.
286
13261-13271
2011
Homo sapiens
21257746
3.1.1.106
752026
The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
Proc. Natl. Acad. Sci. USA
103
16687-16691
2006
Homo sapiens
17075046
3.1.1.106
750645
MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria
Front. Microbiol.
9
20
2018
Homo sapiens
29410655
3.1.1.106
750645
MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria
Front. Microbiol.
9
20
2018
Mus musculus
29410655
3.1.1.106
751030
Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3
J. Biol. Chem.
286
21110-21117
2011
Homo sapiens
21498885
3.1.1.106
749471
Transition-state analysis of 2-O-acetyl-ADP-ribose hydrolysis by human macrodomain 1
ACS Chem. Biol.
9
2255-2262
2014
Homo sapiens
25051211
3.1.1.106
752189
Proximal ADP-ribose hydrolysis in Trypanosomatids is catalyzed by a macrodomain
Sci. Rep.
6
24213
2016
Trypanosoma brucei gambiense
27064071
3.1.1.106
752189
Proximal ADP-ribose hydrolysis in Trypanosomatids is catalyzed by a macrodomain
Sci. Rep.
6
24213
2016
Trypanosoma cruzi
27064071
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