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Transition-State Analysis of the DNA Repair Enzyme...
Journal article

Transition-State Analysis of the DNA Repair Enzyme MutY

Abstract

The transition state (TS) structure of MutY-catalyzed DNA hydrolysis was solved using multiple kinetic isotope effect (KIE) measurements. MutY is a base excision repair enzyme which cleaves adenine from 8-oxo-G:A mismatches in vivo, and also from G:A mismatches in vitro. TS analysis of G:A-DNA hydrolysis revealed a stepwise S(N)1 (D(N)*A(N)(double dagger)) mechanism proceeding through a highly reactive oxacarbenium ion intermediate which would …

Authors

McCann JAB; Berti PJ

Journal

Journal of the American Chemical Society, Vol. 130, No. 17, pp. 5789–5797

Publisher

American Chemical Society (ACS)

Publication Date

April 1, 2008

DOI

10.1021/ja711363s

ISSN

0002-7863