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Information on EC 3.2.2.B5 - 8-oxoguanine DNA glycosylase
for references in articles please use BRENDA:EC3.2.2.B5preliminary BRENDA-supplied EC number
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EC Tree
3.2.2.B5 8-oxoguanine DNA glycosylaseSpecify your search results
Word Map
- 3.2.2.B5
- endonuclease
-
ser326cys
- mtdna
- glycosylases
-
8-ohdg
- 7,8-dihydro-8-oxoguanine
- comet
- ape1
- 8-oxo-7,8-dihydroguanine
- xrcc1
-
8-hydroxy-2'-deoxyguanosine
- formamidopyrimidine
-
base-excision
-
cross-complementing
-
excises
-
abasic
- 8-hydroxyguanine
-
8-oxoguanine-dna
-
8-oxo-dg
-
mutyh
-
8-hydroxydeoxyguanosine
-
arg399gln
-
asp148glu
The enzyme appears in viruses and cellular organisms
Reaction Schemes
DNA containing 8-oxoguanine
+
=
DNA with an abasic site
+
Synonyms
8-oxoguanine dna glycosylase, tvg_rs00315, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8-oxoG DNA glycosylase
8-oxoguanine DNA glycosylase
Afogg enzyme
bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities
archaeal GO glycosylase
GO-glycosylase
MJ0724
MjaOgg2
mjOgg
Ogg2
oxoG DNA glycosylase
Pa-AGOG
Pa-AGOG DNA glycosylase
PAE2237
SSO0904
8-oxoguanine DNA glycosylase
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
8-oxoguanine DNA glycosylase
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
MjaOgg2
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
MjaOgg2
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
Pa-AGOG
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
Pa-AGOG
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
Pa-AGOG DNA glycosylase
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity)
Pa-AGOG DNA glycosylase
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
Pa-AGOG DNA glycosylase
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity)
-
Pa-AGOG DNA glycosylase
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA containing 8-oxoguanine + H2O = DNA with an abasic site + 8-oxoguanine
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
DNA glycohydrolase [8-oxoguanine releasing]
-
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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
additional information
?
-
-
enzyme displays DNA glycosylase, and apurinic/apyrimidinic lyase activities on 7,8-dihydro-8-oxoguanine/N (where N is A, T, G, or C) mismatch. The enzyme cannot eliminate U from U/G or T from T/G
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme excises an oxidatively-damaged form of guanine. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities. The specificity of DNA glycosylase activity of is compared using 39-mer DNA duplexes containing an 8-oxoG residue opposite each of the four natural DNA bases (A, T, G and C). The enzyme efficiently cleaves oligomers containing 8-oxoG:C and 8-oxoG:G base pairs, less effective on oligomers containing 8-oxoG:T and 8-oxoG:A mispairs. The enzyme catalyzes a beta-elimination reaction at the apurinic site produced by excision of the 8-oxoguanine and thus generates a 5'-phosphate terminus and a 3'-alpha,beta-unsaturated aldehyde sugar terminus at the incision site
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
base excision repair pathway
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
DNA substrate used for glycosylase assay: 5'-TGTCAATAGCAAG-X-GGAGAAGTCAATCGTAGTCT-3' for the damage-containing strand, where X is either 8-oxoguanine or uracil, and 5'-AGACTCACGATTGACTTCTCC-Y-CTTGCTATTGACA-3' for the complementary strand, where Y is either one of the four bases. The enzyme displays little preference for the base opposite 8-oxoguanine
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
base excision repair pathway
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
DNA substrate used for glycosylase assay: 5'-TGTCAATAGCAAG-X-GGAGAAGTCAATCGTAGTCT-3' for the damage-containing strand, where X is either 8-oxoguanine or uracil, and 5'-AGACTCACGATTGACTTCTCC-Y-CTTGCTATTGACA-3' for the complementary strand, where Y is either one of the four bases. The enzyme displays little preference for the base opposite 8-oxoguanine
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme that is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
at 37°C and 47°C, the enzyme shows a slightly higher rate for the removal of 8-oxoguanine fom the double-stranded DNA substrate as compared to the single stranded substrate. At 5°C, the activity on 8-oxoguanine containing duplex DNA is much more strongly reduced than on the single-stranded substrate. For the double-stranded DNA substrates, the observed rate constants for both base excision and base excision/beta-lyase activity show a small but significant preference for 8-oxoguanine/G as against 8-oxoguanine/C and 8-oxoguanine/A
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
at 60°C, the enzyme is able to process more than 90% of the 8-oxoguanine/guanine and 8-oxoguanine/cytosine substrates in 15 min, at a substrate to enzyme ratio of 10:1
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
at 37°C and 47°C, the enzyme shows a slightly higher rate for the removal of 8-oxoguanine fom the double-stranded DNA substrate as compared to the single stranded substrate. At 5°C, the activity on 8-oxoguanine containing duplex DNA is much more strongly reduced than on the single-stranded substrate. For the double-stranded DNA substrates, the observed rate constants for both base excision and base excision/beta-lyase activity show a small but significant preference for 8-oxoguanine/G as against 8-oxoguanine/C and 8-oxoguanine/A
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme that is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
at 60°C, the enzyme is able to process more than 90% of the 8-oxoguanine/guanine and 8-oxoguanine/cytosine substrates in 15 min, at a substrate to enzyme ratio of 10:1
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
-
-
-
-
?
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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
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme excises an oxidatively-damaged form of guanine. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
base excision repair pathway
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
base excision repair pathway
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme that is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
the enzyme that is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates
-
-
?
DNA containing 8-oxoguanine + H2O
DNA with an abasic site + 8-oxoguanine
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
catalytic activity is inhibited in buffer more than 100 mM NaCl
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3 - 9.5
pH 7.3: about 50% of maximal activity, pH 9.5: about 45% of maximal ativity, glycosylase/lyase activity is very similar to that of the glycosylase activity alone
7.5 - 10
pH 7.5: about 50% of maximal activity, pH 10.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
60
since the Tm-value of the DNA substrates (39-mer) of is 74°C, the activity above 60°C is not convincible. The actual optimum temperature of the enzyme might be higher than 60°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 50
the enzyme is 6fold more active at 50°C than at 37°C, glycosylase/lyase activity is very similarto that of the glycosylase activity alone
40 - 80
40°C: about 60% of maximal activity, 80°C: about 70% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme that is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates. Bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
physiological function
-
the enzyme that is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates. Bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity, EC 4.2.99.18)
-
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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). OGG1_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
198
0
22639
Swiss-Prot
-
OGG1_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
207
0
24827
Swiss-Prot
-
AGOG_PYRAE
Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)
256
0
29467
Swiss-Prot
-
OGG1_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
207
0
24253
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 25000, SDS-PAGE, x * 26400, calculated from sequence, His-tagged protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion at 12°C. A structural comparison with 8-oxoguanine DNA glycosylase 1 and archaeal GO glycosylase suggests that the C-terminal lysine of 8-oxoguanine DNA glycosylase 2 may play a key role in discriminating between guanine and 8-oxoguanine
hanging-drop, vapor-diffusion method at 12°C. A single crystal of the mutant enzyme K129Q in complex with a 15-mer duplex DNA oligonucleotide containing 8-oxoG paired with C is used to collect a 2.7 A data
crystal structure of the enzyme and that of its complex with 8-oxo-guanosine at 1.0 and 1.7 A resolution, respectively, are grown by sitting drops method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K129S
D172N
D172Q
K140Q
W222F
mutant is similarly active as wild type on 8-oxoguanine/C substrates
W69F
mutant is similarly active as wild type on 8-oxoguanine/C substrates
K128Q
D172N
binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair
D172Q
binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair
K140Q
binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
87
93
additional information
80
pH 7.5 (20 mM TrisCl buffer), denatured irreversibly above 80°C
additional information
thermostability of the enzyme is the highest near 0.5 M NaCl
additional information
-
thermostability of the enzyme is the highest near 0.5 M NaCl
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
overproduced in Escherichia coli as a maltose binding protein(MBP)-Afogg fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lingaraju, G.M.; Prota, A.E.; Winkler, F.K.
Mutational studies of Pa-AGOG DNA glycosylase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum
DNA Repair
8
857-864
2009
Pyrobaculum aerophilum (Q8ZVK6), Pyrobaculum aerophilum DSM 7523 (Q8ZVK6)
brenda
Gogos, A.; Clarke, N.D.
Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus jannaschii
J. Biol. Chem.
274
30447-30450
1999
Methanocaldococcus jannaschii (Q58134), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58134)
brenda
Faucher, F.; Wallace, S.S.; Doubli, S.
The C-terminal lysine of Ogg2 DNA glycosylases is a major molecular determinant for guanine/8-oxoguanine distinction
J. Mol. Biol.
397
46-56
2010
Methanocaldococcus jannaschii (Q58134), Methanocaldococcus jannaschii DSM 2661 (Q58134)
brenda
Chung, J.H.; Suh, M.J.; Park, Y.I.; Tainer, J.A.; Han, Y.S.
Repair activities of 8-oxoguanine DNA glycosylase from Archaeoglobus fulgidus, a hyperthermophilic archaeon
Mutat. Res.
486
99-111
2001
Archaeoglobus fulgidus (O29876), Archaeoglobus fulgidus
brenda
Sartori, A.A.; Lingaraju, G.M.; Hunziker, P.; Winkler, F.K.; Jiricny, J.
Pa-AGOG, the founding member of a new family of archaeal 8-oxoguanine DNA-glycosylases
Nucleic Acids Res.
32
6531-6539
2004
Pyrobaculum aerophilum (Q8ZVK6), Pyrobaculum aerophilum DSM 7523 (Q8ZVK6)
brenda
Lingaraju, G.M.; Sartori, A.A.; Kostrewa, D.; Prota, A.E.; Jiricny, J.; Winkler, F.K.
A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure
Structure
13
87-98
2005
Pyrobaculum aerophilum (Q8ZVK6), Pyrobaculum aerophilum DSM 7523 (Q8ZVK6)
brenda
Faucher, F.; Duclos, S.; Bandaru, V.; Wallace, S.S.; Doublie, S.
Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction
Structure
17
703-712
2009
Methanocaldococcus jannaschii (Q58134), Saccharolobus solfataricus (Q97ZK2), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97ZK2), Methanocaldococcus jannaschii DSM 2661 (Q58134)
brenda
Minoshima, H.; Ikeda, Y.; Fujii, M.; Satoh, M.; Ishikawa, T.; Itoh, Y.; Kawashima-Ohya, Y.; Tomobe, K.; Omata, Y.; Kawashima, T.
Specificity of Fur binding to the oxidative stress response gene promoter in the facultative anaerobic archaeon Thermoplasma volcanium
Biol. Pharm. Bull.
37
481-485
2014
Thermoplasma volcanium
brenda
Fujii, M.; Hata, C.; Ukita, M.; Fukushima, C.; Matsuura, C.; Kawashima-Ohya, Y.; Tomobe, K.; Kawashima, T.
Characterization of a thermostable 8-oxoguanine DNA glycosylase specific for GO/N mismatches from the thermoacidophilic archaeon Thermoplasma volcanium
Archaea
2016
8734894
2016
Thermoplasma volcanium
brenda
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