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Information on EC 3.2.2.31 - adenine glycosylase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P83847

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.31 adenine glycosylase
IUBMB Comments
The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA. The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity. After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break. In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases.
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This record set is specific for:
Geobacillus stearothermophilus
UNIPROT: P83847
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Word Map
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The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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hydrolyses free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Synonyms
adenine glycosylase, adenine dna glycosylase, adenine-dna glycosylase, adenine/guanine-specific dna glycosylase, a/g-specific adenine glycosylase, dna repair adenine glycosylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A/G-specific adenine glycosylase
-
-
-
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mutY
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
adenine-DNA deoxyribohydrolase (adenine-releasing)
The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA. The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity. After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break. In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DNA containing a 7,8-dihydro-8-oxo-2'-deoxyguanosine:adenine mismatch + H2O
?
show the reaction diagram
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-
-
?
DNA containing a guanine:adenine mismatch + H2O
?
show the reaction diagram
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-
-
?
DNA containing an adenine:8-oxoguanine mismatch + H2O
?
show the reaction diagram
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-
-
?
additional information
?
-
no activity with DNA containing a cytosine:8-oxoguanine mismatch
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-
?
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
DNA containing a 7,8-dihydro-8-oxo-2'-deoxyguanosine:adenine mismatch + H2O
?
show the reaction diagram
-
-
-
?
DNA containing a guanine:adenine mismatch + H2O
?
show the reaction diagram
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-
-
?
DNA containing an adenine:8-oxoguanine mismatch + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
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no activity with DNA containing a cytosine:8-oxoguanine mismatch
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MUTY_GEOSE
366
0
41835
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to an azaribose transition state analog
in complex with DNA, hanging drop vapor diffusion method, using 100 mM Tris, pH 8.0, 250 mM NaOAc, 29% (w/v) PEG 4000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D144N
active site mutant
P164C
active site mutant
Y126F
the mutant shows a 260fold slower rate of adenine removal compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MonoQ column chromatography
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Woods, R.D.; OShea, V.L.; Chu, A.; Cao, S.; Richards, J.L.; Horvath, M.P.; David, S.S.
Structure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidases
Nucleic Acids Res.
44
801-810
2016
Geobacillus stearothermophilus (P83847)
Manually annotated by BRENDA team
Wang, L.; Lee, S.J.; Verdine, G.L.
Structural basis for avoidance of promutagenic DNA repair by MutY adenine DNA glycosylase
J. Biol. Chem.
290
17096-17105
2015
Geobacillus stearothermophilus (P83847)
Manually annotated by BRENDA team