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Literature summary for 4.2.99.18 extracted from

  • van der Kemp, P.A.; Charbonnier, J.B.; Audebert, M.; Boiteux, S.
    Catalytic and DNA-binding properties of the human Ogg1 DNA N-glycosylase/AP lyase: biochemical exploration of H270, Q315 and F319, three amino acids of the 8-oxoguanine-binding pocket (2004), Nucleic Acids Res., 32, 570-578.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
F319A DNA glycosylase activity is reduced 52.6fold, activity towards abasic sites is reduced 1.5fold Homo sapiens
H270A DNA glycosylase activity is reduced 50fold, activity towards abasic sites is reduced 2.3fold Homo sapiens
H270L DNA glycosylase activity is reduced 71.4fold, activity towards abasic sites is reduced 3.7fold Homo sapiens
H270R DNA glycosylase activity is reduced 3.9fold, activity towards abasic sites is nearly identical to wild-type activity Homo sapiens
Q315A DNA glycosylase activity is reduced 1.6fold, activity towards abasic sites is increased 1.18fold Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O15527 recombinant
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Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes H270A, H270R, H270L, Q315A, F319A Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information hOgg1 protein catalyzes the excision of 8-oxo-7,8-dihydroguanine and the incision of apurinic and apyrimidinic sites in DNA Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
hOgg1 protein
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Homo sapiens