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Literature summary for 3.2.2.23 extracted from

  • Sidorenko, V.S.; Grollman, A.P.; Jaruga, P.; Dizdaroglu, M.; Zharkov, D.O.
    Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase (2009), FEBS J., 276, 5149-5162.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information the human AP endonuclease APEX1 can stimulate wild-type OGG1 activity by increasing its turnover rate, but very little stimulation of 8-oxoGua removal in the presence of APEX1 occurs with phosphomimetic mutants, overview Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
genotyping, overview. Expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
A288V naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1, activity, substrate specificity and kinetics compared to the wild-type enzyme, overview Homo sapiens
D322N naturally occuring polymorphism, the mutant is 2.3fold more specific for the correct opposite base than the wild-type enzyme, activity, substrate specificity and kinetics compared to the wild-type enzyme Homo sapiens
additional information the gene shows several polymorphisms in vivo Homo sapiens
S231E naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview Homo sapiens
S231E/S232E naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview Homo sapiens
S232E naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview Homo sapiens
S280E naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview Homo sapiens
S326C naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1. The mutant efficiently excises 8-oxoGua from oligodeoxynucleotides and 2,6-diamino-4-hydroxy-5-formamidopyrimidine from gamma-irradiated DNA, but excises 8-oxoG rather inefficiently from gamma-irradiated DNA Homo sapiens
S326E naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000034
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S326C Homo sapiens
0.0000034
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, wild-type enzyme Homo sapiens
0.0000057
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S231E Homo sapiens
0.0000061
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant D322N Homo sapiens
0.0000074
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S280E Homo sapiens
0.0000075
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S326E Homo sapiens
0.0000086
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant A288V Homo sapiens
0.0000092
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S232E Homo sapiens
0.00001
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S231E/S232E Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt-DNA + H2O Homo sapiens
-
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt-DNA
-
?
8-oxo-7,8-dihydroguanine:Cyt-DNA + H2O Homo sapiens
-
8-oxo-7,8-dihydroguanine + Cyt-DNA
-
?
additional information Homo sapiens 8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1 ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens O15527
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of OGG1 can affect its biological functions at several levels, including the intrinsic activity and intracellular localization Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
substrate specificity of wild-type and mutant enzymes, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O
-
Homo sapiens 2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt oligodeoxynucleotide
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt-DNA + H2O
-
Homo sapiens 2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt-DNA
-
?
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O
-
Homo sapiens 8-oxo-7,8-dihydroguanine + Cyt oligodeoxynucleotide
-
?
8-oxo-7,8-dihydroguanine:Cyt-DNA + H2O
-
Homo sapiens 8-oxo-7,8-dihydroguanine + Cyt-DNA
-
?
additional information 8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1 Homo sapiens ?
-
?
additional information 8-oxoguanine-DNA glycosylase, OGG1, efficiently removes mutagenic 8-oxo-7,8-dihydroguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine when paired with cytosine in oxidatively damaged DNA. Excision of 8-oxoGua mispaired with adenine may lead to G to T transversions. Substrate specificity of wild-type and mutant enzymes, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure of OGG1, PDB ID 1EBM, overview Homo sapiens

Synonyms

Synonyms Comment Organism
8-oxoguanine-DNA glycosylase
-
Homo sapiens
OGG1
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00037
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S326C Homo sapiens
0.00047
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant D322N Homo sapiens
0.00048
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S280E Homo sapiens
0.0005
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, wild-type enzyme Homo sapiens
0.00053
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S326E Homo sapiens
0.00065
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S232E Homo sapiens
0.00068
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S231E/S232E Homo sapiens
0.0007
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant S231E Homo sapiens
0.00092
-
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide pH 7.4-7.5, mutant A288V Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4 7.5 assay at Homo sapiens

General Information

General Information Comment Organism
malfunction OGG1 polymorphisms might be associated with succeptibility of humans to cancer and other diseases Homo sapiens
physiological function OGG1 is part of an enzymatic system responsible for prevention of mutations generated by 8-oxo-7,8-dihydroguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine Homo sapiens