Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays

Authors:	Brinkmeyer Megan K Pope Mary Ann David Sheila S

Institution:	Department of Chemistry, University of California Davis, Davis, CA 95616, USA.

Abstract:	Download : Download high-res image (185KB) Download : Download full-size image Highlights? Asp 138 must be deprotonated to stabilize the transition state for maximal activity ? Consequences of altering catalytic amino acids in MutY on cellular mismatch repair ? Correlation of MutY enzymatic parameters with ability to mediate cellular repair ? Importance of high affinity binding of MutY to the OG:A mismatch for high levels of repair

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