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Information on EC 3.1.1.106 - O-acetyl-ADP-ribose deacetylase and Organism(s) Mus musculus and UniProt Accession Q922B1

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.106 O-acetyl-ADP-ribose deacetylase
IUBMB 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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This record set is specific for:
Mus musculus
UNIPROT: Q922B1
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
macrod2, macrod1, c6orf130, adp-ribosyl hydrolase, macrodomain 1, macrod-like protein, oaadpr hydrolase, o-acetyl-adp-ribose deacetylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-ribosyl hydrolase
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MACROD1
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-
-
-
ymdB
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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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
show the reaction diagram
-
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
show the reaction diagram
-
-
-
?
mono-ADP-ribosylated phosphorylated double stranded DNA ends + H2O
?
show the reaction diagram
the enzyme can efficiently remove ADP-D-ribose from 5' and 3'-phosphorylated double stranded DNA adducts in vitro
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-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
show the reaction diagram
-
-
-
?
3''-O-acetyl-ADP-D-ribose + H2O
ADP-D-ribose + acetate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MACD1_MOUSE
323
0
35295
Swiss-Prot
Mitochondrion (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28000, SDS-PAGE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team