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Information on EC 3.1.1.106 - O-acetyl-ADP-ribose deacetylase
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EC Tree
3.1.1.106 O-acetyl-ADP-ribose deacetylaseIUBMB Comments
The enzyme, characterized from the bacterium Escherichia coli and from human cells, removes the acetyl group from either the 2'' or 3'' position of O-acetyl-ADP-ribose, which are formed by the action of EC 2.3.1.286, protein acetyllysine N-acetyltransferase. The human enzyme can also remove ADP-D-ribose from phosphorylated double stranded DNA adducts.
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Word Map
- 3.1.1.106
-
adp-ribosylation
-
macrodomains
-
mono-adp-ribosylation
- mono-adp-ribosylhydrolase
-
pargs
-
macrodomain-containing
-
adp-ribosylhydrolase
-
poly-adp-ribosylation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
macrod2, macrod1, c6orf130, adp-ribosyl hydrolase, macrodomain 1, oaadpr hydrolase, o-acetyl-adp-ribose deacetylase, macrod-like protein, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-ribose hydrolase
ADP-ribosyl hydrolase
MacroD-like protein
MACROD1
MDO
Nudix hydrolase
O-acetyl-ADP-ribose deacetylase
OAADPr deacetylase
ymdB
MACROD1
-
-
-
-
ymdB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2''-O-acetyl-ADP-D-ribose + H2O = ADP-D-ribose + acetate
(2)
-
-
-
3''-O-acetyl-ADP-D-ribose + H2O = ADP-D-ribose + acetate
(1)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
O-acetyl-ADP-D-ribose carboxylesterase
The enzyme, characterized from the bacterium Escherichia coli and from human cells, removes the acetyl group from either the 2'' or 3'' position of O-acetyl-ADP-ribose, which are formed by the action of EC 2.3.1.286, protein acetyllysine N-acetyltransferase. The human enzyme can also remove ADP-D-ribose from phosphorylated double stranded DNA adducts.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
poly(ADP-D-ribose) + H2O
ADP-D-ribose
-
the linkage hydrolyzed by the enzyme in poly(ADP-D-ribose) is stereospecific at the C-1' position with the alpha-anomer present in the polymer
-
-
?
[ARTD10 protein]-ADP-D-ribose + H2O
[ARTD10 protein] + ADP-D-ribose
-
-
-
?
[glycogen synthase kinase 3beta]-ADP-D-ribose + H2O
[glycogen synthase kinase 3beta] + ADP-D-ribose
-
-
-
?
[SRPK2 protein]-ADP-D-ribose + H2O
[SRPK2 protein] + ADP-D-ribose
-
-
-
?
1''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
predominant substrate at pH 9.0
-
-
?
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
specific substrate
-
-
?
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
predominant substrate at pH 7.0
-
-
?
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
predominant substrate at pH 5.0 and 7.0
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
mono-ADP-ribosylated phosphorylated double stranded DNA ends + H2O
?
-
the enzyme can efficiently remove ADP-D-ribose from 5' and 3'-phosphorylated double stranded DNA adducts in vitro
-
-
?
mono-ADP-ribosylated phosphorylated double stranded DNA ends + H2O
?
the enzyme can efficiently remove ADP-D-ribose from 5' and 3'-phosphorylated double stranded DNA adducts in vitro
-
-
?
[protein]-ADP-D-ribose + H2O
[protein] + ADP-D-ribose
-
-
-
?
[protein]-ADP-D-ribose + H2O
[protein] + ADP-D-ribose
-
-
-
?
additional information
?
-
-
isoform MacroD1 is completely inactive toward poly-ADP-D-ribose synthesized by ADP-ribosyltransferase diphtheria toxin-like 1 in the presence of high NAD+ concentrations
-
-
?
additional information
?
-
isoform MacroD1 is completely inactive toward poly-ADP-D-ribose synthesized by ADP-ribosyltransferase diphtheria toxin-like 1 in the presence of high NAD+ concentrations
-
-
?
additional information
?
-
isoform MacroD1 is completely inactive toward poly-ADP-D-ribose synthesized by ADP-ribosyltransferase diphtheria toxin-like 1 in the presence of high NAD+ concentrations
-
-
?
additional information
?
-
-
isoform MacroD2 is a mono-ADP-ribosylhydrolase specific for acidic residues of aspartates and glutamates
-
-
?
additional information
?
-
isoform MacroD2 is a mono-ADP-ribosylhydrolase specific for acidic residues of aspartates and glutamates
-
-
?
additional information
?
-
isoform MacroD2 is a mono-ADP-ribosylhydrolase specific for acidic residues of aspartates and glutamates
-
-
?
additional information
?
-
-
isoform MacroD2 is completely inactive toward poly-ADP-D-ribose synthesized by ADP-ribosyltransferase diphtheria toxin-like 1 in the presence of high NAD+ concentrations. MacroD2 does not remove ADP-D-ribose modifications generated by the arginine-specific enzyme CDTa or TccC3
-
-
?
additional information
?
-
isoform MacroD2 is completely inactive toward poly-ADP-D-ribose synthesized by ADP-ribosyltransferase diphtheria toxin-like 1 in the presence of high NAD+ concentrations. MacroD2 does not remove ADP-D-ribose modifications generated by the arginine-specific enzyme CDTa or TccC3
-
-
?
additional information
?
-
isoform MacroD2 is completely inactive toward poly-ADP-D-ribose synthesized by ADP-ribosyltransferase diphtheria toxin-like 1 in the presence of high NAD+ concentrations. MacroD2 does not remove ADP-D-ribose modifications generated by the arginine-specific enzyme CDTa or TccC3
-
-
?
additional information
?
-
-
neither 2''- nor 3''-N-acetyl-ADP-D-ribose is a substrate for the enzyme
-
-
?
additional information
?
-
-
no activity with ADP-ribosylated thymidine on single stranded DNA
-
-
?
additional information
?
-
no activity with ADP-ribosylated thymidine on single stranded DNA
-
-
?
additional information
?
-
-
no activity with ADP-ribosylated thymidine on single stranded DNA
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[SRPK2 protein]-ADP-D-ribose + H2O
[SRPK2 protein] + ADP-D-ribose
-
-
-
?
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
specific substrate
-
-
?
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
-
-
?
[protein]-ADP-D-ribose + H2O
[protein] + ADP-D-ribose
-
-
-
?
[protein]-ADP-D-ribose + H2O
[protein] + ADP-D-ribose
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by D-ribose 5-phosphate, AMP, ADP, or beta-NAD+
-
additional information
-
D-ribose 5-phosphate, AMP, ADP and beta-NAD have relatively little inhibitory effect on the enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
MACROD2 overexpression mediates estrogen independent growth and tamoxifen resistance in breast cancers.
Carcinogenesis
Copy Number Variation Pattern for Discriminating MACROD2 States of Colorectal Cancer Subtypes.
Carcinogenesis
MACROD2 Haploinsufficiency Impairs Catalytic Activity of PARP1 and Promotes Chromosome Instability and Growth of Intestinal Tumors.
Carcinogenesis
Mono-ADP-Ribosylhydrolase MACROD2 Is Dispensable for Murine Responses to Metabolic and Genotoxic Insults.
Carcinogenesis
The Controversial Roles of ADP-Ribosyl Hydrolases MACROD1, MACROD2 and TARG1 in Carcinogenesis.
Carcinoma, Hepatocellular
MACROD2 deficiency promotes hepatocellular carcinoma growth and metastasis by activating GSK-3?/?-catenin signaling.
Colonic Neoplasms
MACROD2 expression predicts response to 5-FU-based chemotherapy in stage III colon cancer.
Colorectal Neoplasms
Copy Number Variation Pattern for Discriminating MACROD2 States of Colorectal Cancer Subtypes.
Colorectal Neoplasms
MACROD2 deletions cause impaired PARP1 activity and chromosome instability in colorectal cancer.
Colorectal Neoplasms
MACROD2 Haploinsufficiency Impairs Catalytic Activity of PARP1 and Promotes Chromosome Instability and Growth of Intestinal Tumors.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Mono-ADP-Ribosylhydrolase MACROD2 Is Dispensable for Murine Responses to Metabolic and Genotoxic Insults.
Fatty Liver
Loss of the Mono-ADP-ribosyltransferase, Tiparp, Increases Sensitivity to Dioxin-induced Steatohepatitis and Lethality.
Graves Disease
Association of Polymorphisms in MACRO Domain Containing 2 With Thyroid-Associated Orbitopathy.
Insulin Resistance
High Genetic Risk Scores of ASIC2, MACROD2, CHRM3, and C2orf83 Genetic Variants Associated with Polycystic Ovary Syndrome Impair Insulin Sensitivity and Interact with Energy Intake in Korean Women.
Intellectual Disability
Intragenic Deletion in MACROD2: A Family with Complex Phenotypes Including Microcephaly, Intellectual Disability, Polydactyly, Renal and Pancreatic Malformations.
Intellectual Disability
Mono-ADP-Ribosylhydrolase MACROD2 Is Dispensable for Murine Responses to Metabolic and Genotoxic Insults.
Microcephaly
Intragenic Deletion in MACROD2: A Family with Complex Phenotypes Including Microcephaly, Intellectual Disability, Polydactyly, Renal and Pancreatic Malformations.
Neoplasm Metastasis
MACROD2 deficiency promotes hepatocellular carcinoma growth and metastasis by activating GSK-3?/?-catenin signaling.
Neoplasm Metastasis
MACROD2 overexpression mediates estrogen independent growth and tamoxifen resistance in breast cancers.
Neoplasms
Copy Number Variation Pattern for Discriminating MACROD2 States of Colorectal Cancer Subtypes.
Neoplasms
MACROD2 deficiency promotes hepatocellular carcinoma growth and metastasis by activating GSK-3?/?-catenin signaling.
Neoplasms
MACROD2 Haploinsufficiency Impairs Catalytic Activity of PARP1 and Promotes Chromosome Instability and Growth of Intestinal Tumors.
Neoplasms
MACROD2 overexpression mediates estrogen independent growth and tamoxifen resistance in breast cancers.
Neoplasms
Mono-ADP-Ribosylhydrolase MACROD2 Is Dispensable for Murine Responses to Metabolic and Genotoxic Insults.
Neoplasms
The Controversial Roles of ADP-Ribosyl Hydrolases MACROD1, MACROD2 and TARG1 in Carcinogenesis.
Neuroblastoma
Comparative analysis of MACROD1, MACROD2 and TARG1 expression, localisation and interactome.
o-acetyl-adp-ribose deacetylase deficiency
MACROD2 deficiency promotes hepatocellular carcinoma growth and metastasis by activating GSK-3?/?-catenin signaling.
Obesity
Association of MACROD2 gene variants with obesity and physical activity in a Korean population.
Obesity
Mono-ADP-Ribosylhydrolase MACROD2 Is Dispensable for Murine Responses to Metabolic and Genotoxic Insults.
Papilloma
Human papilloma virus (HPV) integration signature in Cervical Cancer: identification of MACROD2 gene as HPV hot spot integration site.
Polycystic Ovary Syndrome
High Genetic Risk Scores of ASIC2, MACROD2, CHRM3, and C2orf83 Genetic Variants Associated with Polycystic Ovary Syndrome Impair Insulin Sensitivity and Interact with Energy Intake in Korean Women.
Polydactyly
Intragenic Deletion in MACROD2: A Family with Complex Phenotypes Including Microcephaly, Intellectual Disability, Polydactyly, Renal and Pancreatic Malformations.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Next-generation-sequencing of recurrent childhood high hyperdiploid acute lymphoblastic leukemia reveals mutations typically associated with high risk patients.
Uterine Cervical Neoplasms
Human papilloma virus (HPV) integration signature in Cervical Cancer: identification of MACROD2 gene as HPV hot spot integration site.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4306
2''-O-acetyl-ADP-D-ribose
wild type enzyme, at pH 7.5 and 25°C
1.358
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
2.74
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.814
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
0.002
O-acetyl-ADP-D-ribose
mutant G270E of isoform MacroD1, at pH 7.3 and 23°C
0.014
O-acetyl-ADP-D-ribose
mutant N174A/D184A of isoform MacroD1, at pH 7.3 and 23°C
0.078
O-acetyl-ADP-D-ribose
mutant D184A of isoform MacroD1, at pH 7.3 and 23°C
0.082
O-acetyl-ADP-D-ribose
mutant N171A of isoform MacroD1, at pH 7.3 and 23°C
0.113
O-acetyl-ADP-D-ribose
mutant N174A of isoform MacroD1, at pH 7.3 and 23°C
0.114
O-acetyl-ADP-D-ribose
mutant D160A of isoform MacroD1, at pH 7.3 and 23°C
0.114
O-acetyl-ADP-D-ribose
mutant H188A of isoform MacroD1, at pH 7.3 and 23°C
0.136
O-acetyl-ADP-D-ribose
mutant D167A of isoform MacroD1, at pH 7.3 and 23°C
0.153
O-acetyl-ADP-D-ribose
mutant S268A of isoform MacroD1, at pH 7.3 and 23°C
0.179
O-acetyl-ADP-D-ribose
mutant C199A of isoform MacroD1, at pH 7.3 and 23°C
0.195
O-acetyl-ADP-D-ribose
mutant S176A of isoform MacroD1, at pH 7.3 and 23°C
0.204
O-acetyl-ADP-D-ribose
mutant T226A of isoform MacroD1, at pH 7.3 and 23°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.073
2''-O-acetyl-ADP-D-ribose
mutant enzyme D35A, at pH 7.5 and 25°C
0.599
2''-O-acetyl-ADP-D-ribose
mutant enzyme N25A, at pH 7.5 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoform MacroD2 regulates GSK3beta function
Show AA Sequence and Transmembrane Helices (1048 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
isoform MacroD1, sitting drop vapor diffusion method, using 0.2 M (NH4)2SO4, 0.1 M HEPES pH 7.5, 25% (w/v) PEG 3350 at 4°C
apoenzyme and in complex with ADP-D-ribose or ADP, sitting drop vapor diffusion method, using 20-25% (w/v) PEG 3350
apoenzyme, sitting drop vapor diffusion method, using 0.1 M Bis-Tris propane pH 8.0, 0.96 M trisodium citrate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D35A
the mutant shows strongly reduced activity compared to the wild type enzyme
N25A
the mutant shows strongly reduced activity compared to the wild type enzyme
E238Q/E239Q
-
the mutant shows wild type hydrolytic activity with O-acetyl-D-ADP-ribose
E261Q/E262Q
-
the mutant shows wild type hydrolytic activity with O-acetyl-D-ADP-ribose
G100E
the mutant isoform MacroD2 lacks hydrolase and ADP-ribose-binding activities
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 75 gel filtration
HisTrap column chromatography and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme isoform MacroD1 is expressed in Escherichia coli BL21(DE3)-R3-pRARE2 cells
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirsch, B.M.; Burgos, E.S.; Schramm, V.L.
Transition-state analysis of 2-O-acetyl-ADP-ribose hydrolysis by human macrodomain 1
ACS Chem. Biol.
9
2255-2262
2014
Homo sapiens (Q9BQ69), Homo sapiens
brenda
Agnew, T.; Munnur, D.; Crawford, K.; Palazzo, L.; Mikoc, A.; Ahel, I.
MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria
Front. Microbiol.
9
20
2018
Homo sapiens, Mus musculus (Q922B1), Mus musculus
brenda
Rafty, L.; Schmidt, M.; Perraud, A.; Scharenberg, A.; Denu, J.
Analysis of O-acetyl-ADP-ribose as a target for nudix ADP-ribose hydrolases
J. Biol. Chem.
277
47114-47122
2002
Saccharomyces cerevisiae, Homo sapiens
-
brenda
Chen, D.; Vollmar, M.; Rossi, M.N.; Phillips, C.; Kraehenbuehl, R.; Slade, D.; Mehrotra, P.V.; von Delft, F.; Crosthwaite, S.K.; Gileadi, O.; Denu, J.M.; Ahel, I.
Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases
J. Biol. Chem.
286
13261-13271
2011
Escherichia coli, Staphylococcus aureus, Homo sapiens (A1Z1Q3), Homo sapiens (Q9BQ69), Homo sapiens
brenda
Kasamatsu, A.; Nakao, M.; Smith, B.C.; Comstock, L.R.; Ono, T.; Kato, J.; Denu, J.M.; Moss, J.
Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3
J. Biol. Chem.
286
21110-21117
2011
Homo sapiens
brenda
Zhang, W.; Wang, C.; Song, Y.; Shao, C.; Zhang, X.; Zang, J.
Structural insights into the mechanism of Escherichia coli YmdB A 2-O-acetyl-ADP-ribose deacetylase
J. Struct. Biol.
192
478-486
2015
Escherichia coli (P0A8D6)
brenda
Rosenthal, F.; Feijs, K.L.; Frugier, E.; Bonalli, M.; Forst, A.H.; Imhof, R.; Winkler, H.C.; Fischer, D.; Caflisch, A.; Hassa, P.O.; Luescher, B.; Hottiger, M.O.
Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases
Nat. Struct. Mol. Biol.
20
502-507
2013
Homo sapiens, Homo sapiens (A1Z1Q3), Homo sapiens (Q9BQ69)
brenda
Ono, T.; Kasamatsu, A.; Oka, S.; Moss, J.
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
brenda
Haikarainen, T.; Lehtioe, L.
Proximal ADP-ribose hydrolysis in Trypanosomatids is catalyzed by a macrodomain
Sci. Rep.
6
24213
2016
Trypanosoma brucei gambiense (C9ZP98), Trypanosoma cruzi (Q4DQ03), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4DQ03)
brenda
Haikarainen, T.; Maksimainen, M.M.; Obaji, E.; Lehtioe, L.
Development of an inhibitor screening assay for mono-ADP-ribosyl hydrolyzing macrodomains using AlphaScreen technology
SLAS Discov.
23
255-263
2018
Homo sapiens (Q9BQ69), Homo sapiens
brenda
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