首页> 外文期刊>Nucleic Acids Research >Role of lysine-57 in the catalytic activities of Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg protein).
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Role of lysine-57 in the catalytic activities of Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg protein).

机译:赖氨酸57在大肠杆菌甲酰胺嘧啶-DNA糖基化酶(Fpg蛋白)的催化活性中的作用。

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摘要

The Escherichia coli Fpg protein is involved in the repair of oxidized residues. We examined, by targeted mutagenesis, the effect of the conserved lysine residue at position 57 upon the various catalytic activities of the Fpg protein. Mutant Fpg protein with Lys-57-->Gly (K57G) had dramatically reduced DNA glycosylase activity for the excision of 7,8-dihydro-8-oxo-guanine (8-oxoG). While wild type Fpg protein cleaved 8-oxoG/C DNA with a specificity constant ( k cat/ K M) of 0.11/(nM
机译:大肠杆菌Fpg蛋白参与氧化残基的修复。通过有针对性的诱变,我们检查了第57位保守赖氨酸残基对Fpg蛋白各种催化活性的影响。具有Lys-57-> Gly(K57G)的突变Fpg蛋白具有显着降低的DNA糖基化酶活性,可用于切除7,8-二氢-8-氧代鸟嘌呤(8-oxoG)。而野生型Fpg蛋白以0.11 /(nM)的特异性常数(k cat / K M)切割8-oxoG / C DNA。

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