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Information on EC 3.1.1.106 - O-acetyl-ADP-ribose deacetylase and Organism(s) Homo sapiens and UniProt Accession A1Z1Q3
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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
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pargs
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macrodomain-containing
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adp-ribosylhydrolase
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poly-adp-ribosylation
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
macrod2, macrod1, c6orf130, adp-ribosyl hydrolase, macrodomain 1, o-acetyl-adp-ribose deacetylase, macrod-like protein, oaadpr hydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MACROD1
ymdB
-
-
-
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MACROD1
-
-
-
-
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.
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
[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
-
-
-
?
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
-
-
?
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
-
predominant substrate at pH 7.0
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
-
predominant substrate at pH 5.0 and 7.0
-
-
?
additional information
?
-
-
isoform MacroD2 is a mono-ADP-ribosylhydrolase specific for acidic residues of aspartates and glutamates
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-
?
additional information
?
-
isoform MacroD2 is a mono-ADP-ribosylhydrolase specific for acidic residues of aspartates and glutamates
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?
additional information
?
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isoform MacroD2 is a mono-ADP-ribosylhydrolase specific for acidic residues of aspartates and glutamates
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-
?
additional information
?
-
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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
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
-
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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
?
-
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neither 2''- nor 3''-N-acetyl-ADP-D-ribose is a substrate for the enzyme
-
-
?
additional information
?
-
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no activity with ADP-ribosylated thymidine on single stranded DNA
-
-
?
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
D-ribose 5-phosphate, AMP, ADP and beta-NAD have relatively little inhibitory effect on the enzyme activity
-
additional information
-
not inhibited by D-ribose 5-phosphate, AMP, ADP, or beta-NAD+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoform MacroD2 regulates GSK3beta function
physiological function
isoform MacroD2 regulates GSK3beta function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G100E
the mutant isoform MacroD2 lacks hydrolase and ADP-ribose-binding activities
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme isoform MacroD1 is expressed in Escherichia coli BL21(DE3)-R3-pRARE2 cells
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
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
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
-
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, Homo sapiens (A1Z1Q3), Homo sapiens (Q9BQ69), Homo sapiens, Staphylococcus aureus
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
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)
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
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