About: The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG     Goto   Sponge   NotDistinct   Permalink

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  • The activation of N-glycosidic bond cleavage performed by the lysine 249 (Lys 249) residue of base-excision repair enzyme hOGG1 was calculated for 2'-deoxyguanosine (G), 8-oxo-2'-deoxyguanosine (OxoG) and N6-(2'-beta-D-deoxyribofuranosyl)-2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG). The interaction sites of Lys 249 included the C1', N3, and N9 atoms of the nucleosides. The N9-pathway, specifically the attack of lone-pair electrons of glycosidic nitrogen N9 of a nucleoside on the proton of the N epsilon-ammonium group of Lys 249, resulted in effective activation of the C1'-N9 bond that was highly specific with respect to normal (G) and damaged (OxoG, FapyG) nucleosides.
  • The activation of N-glycosidic bond cleavage performed by the lysine 249 (Lys 249) residue of base-excision repair enzyme hOGG1 was calculated for 2'-deoxyguanosine (G), 8-oxo-2'-deoxyguanosine (OxoG) and N6-(2'-beta-D-deoxyribofuranosyl)-2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG). The interaction sites of Lys 249 included the C1', N3, and N9 atoms of the nucleosides. The N9-pathway, specifically the attack of lone-pair electrons of glycosidic nitrogen N9 of a nucleoside on the proton of the N epsilon-ammonium group of Lys 249, resulted in effective activation of the C1'-N9 bond that was highly specific with respect to normal (G) and damaged (OxoG, FapyG) nucleosides. (en)
Title
  • The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG
  • The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG (en)
skos:prefLabel
  • The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG
  • The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG (en)
skos:notation
  • RIV/00216224:14740/14:00079762!RIV15-MSM-14740___
http://linked.open...avai/riv/aktivita
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  • I, P(ED1.1.00/02.0068), P(EE2.3.20.0042), P(GA13-27676S)
http://linked.open...iv/cisloPeriodika
  • 83
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  • 1513
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  • RIV/00216224:14740/14:00079762
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  • 8-OXOGUANINE DNA GLYCOSYLASE; INDEPENDENT CHEMICAL-SHIFTS; OXIDATIVELY DAMAGED DNA; TRANSITION-STATE; PROTEIN HOGG1; GAS-PHASE; OGG1 GENE; RECOGNITION; DENSITY; MECHANISM (en)
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  • GB - Spojené království Velké Británie a Severního Irska
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  • [79F298B864FE]
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  • 4
http://linked.open...iv/tvurceVysledku
  • Šebera, Jakub
  • Tanaka, Y.
  • Trantírek, Lukáš
  • Fukal, J.
  • Nencka, R.
  • Sychrovský, V.
http://linked.open...ain/vavai/riv/wos
  • 000344527300030
issn
  • 2046-2069
number of pages
http://bibframe.org/vocab/doi
  • 10.1039/c4ra08278h
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  • 14740
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