So far, in addition to halogen atoms, other non-metallic atoms can become part of the aromatic heterocycle, and the target ring system is still aromatic.Lukina, Maria V.; Popov, Alexander V.; Koval, Vladimir V.; Vorobjev, Yuri N.; Fedorova, Olga S.; Zharkov, Dmitry O. researched the compound: 8-Bromoguanine( cas:3066-84-0 ).Electric Literature of C5H4BrN5O.They published the article 《DNA damage processing by human 8-oxoguanine-DNA glycosylase mutants with the occluded active site》 about this compound( cas:3066-84-0 ) in Journal of Biological Chemistry. Keywords: oxoguanineDNA glycosylase mutant DNA damage processing active site plasticity; 8-Oxoguanine; Abasic Site; DNA Damage; DNA Repair; Enzyme Kinetics; Enzyme Mutation; Molecular Modeling; OGG1; Presteady-state Kinetics; Substrate Recognition. We’ll tell you more about this compound (cas:3066-84-0).
8-Oxoguanine-DNA glycosylase (OGG1) removes pre-mutagenic lesion 8-oxoguanine (8-oxo-G) from DNA and then nicks the nascent abasic (apurinic/apyrimidinic) site by β-elimination. Although the structure of OGG1 bound to damaged DNA is known, the dynamic aspects of 8-oxo-G recognition are not well understood. To comprehend the mechanisms of substrate recognition and processing, the authors constructed OGG1 mutants with the active site occluded by replacement of Cys-253, which forms a wall of the base-binding pocket, with bulky Leu or Ile residues. The conformational dynamics of OGG1 mutants were characterized by single-turnover kinetics and stopped-flow kinetics with fluorescent detection. Addnl., the conformational mobility of wild-type and the mutant OGG1 substrate complex was assessed using mol. dynamics simulations. Although pocket occlusion distorted the active site and greatly decreased the catalytic activity of OGG1, it did not fully prevent processing of 8-oxo-G and apurinic/apyrimidinic sites. Both mutants were notably stimulated in the presence of free 8-bromoguanine, indicating that this base could bind to the distorted OGG1 and facilitate β-elimination. The results agreed with the concept of enzyme plasticity, suggesting that the active site of OGG1 is flexible enough to compensate partially for distortions caused by mutation.
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Reference:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem