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Mechanism of base excision with the hOGG1 DNA repair enzyme [Mechanism of base excision with the hOGG1 DNA repaeEnzyme]
Jakub Šebera, Lukáš Trantírek, Jiří Fukal, Yoshiyuki Tanaka, And Vladimír Sychrovský
Jazyk angličtina Země Česko
Typ dokumentu práce podpořená grantem
- Klíčová slova
- human 8-oxoguanine glycosylase1 protein,
- MeSH
- chemické jevy MeSH
- deoxyguanosin chemie MeSH
- DNA-glykosylasy * chemie MeSH
- enzymy opravy DNA * chemie MeSH
- lidé MeSH
- molekulární modely MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- práce podpořená grantem MeSH
This article suggests a new mechanistic scheme of the catalytic 8-oxoguanine excision with the hOGG1 base excision repair protein. The energy-efficient and substratespecific scheme employs enforced pyramidalization of the glycosidic nitrogen in the nucleobase within the hOGG1 catalytic pocket.
Central European Institute of Technology Masaryk University Brno
Division of Pharmaceutical Chemistry Tohoku University Aobayama Aoba ku Sendai Japan
Mechanism of base excision with the hOGG1 DNA repaeEnzyme
Literatura
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- $a This article suggests a new mechanistic scheme of the catalytic 8-oxoguanine excision with the hOGG1 base excision repair protein. The energy-efficient and substratespecific scheme employs enforced pyramidalization of the glycosidic nitrogen in the nucleobase within the hOGG1 catalytic pocket.
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