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1 monstrated that both variants have a reduced adenine glycosylase activity and affinity for substrate
2 alanine by site-directed mutagenesis reduces adenine glycosylase activity of MutY toward OG:A and G:A
3 cognition of substrate DNA necessary for the adenine glycosylase activity of MutY.
4 s in E.coli MutY revealed a reduction in the adenine glycosylase activity of the enzymes.
5      Previously, our laboratory analyzed the adenine glycosylase activity of the homologous variant E
6                                    Assays of adenine glycosylase activity of the Tyr82Cys and Gly253A
7                                          The adenine glycosylase activity on single-stranded DNA repo
8                           MutY also exhibits adenine glycosylase activity toward adenine in G:A and C
9                This implies that the reduced adenine glycosylase activity translates to a reduced cap
10 ecombinant MutY(Dr) expressed in E. coli has adenine glycosylase activity with A/G, A/C, and A/GO mis
11 tant could still bind DNA substrates and had adenine glycosylase activity.
12 tro studies show that the p26 domain retains adenine glycosylase and AP lyase activity on DNA contain
13 of SpMYH expressed in yeast cells had normal adenine glycosylase and DNA binding activities.
14 h lack the cluster are unable to perform the adenine glycosylase function and bind to DNA.
15                                   MutY is an adenine glycosylase in the base excision repair (BER) su
16                                     MutY, an adenine glycosylase, initiates the critical repair of an
17                         The Escherichia coli adenine glycosylase MutY and its human homolog (hMYH) pl
18                                  The E. coli adenine glycosylase MutY is a member of the base excisio
19                         The Escherichia coli adenine glycosylase MutY is involved in the repair of 7,
20                         The Escherichia coli adenine glycosylase MutY is involved in the repair of 7,
21                                          The adenine glycosylase MutY, which removes misincorporated
22 tures of the catalytic mechanism used by the adenine glycosylase MutY.
23                    The Escherichia coli MutY adenine glycosylase plays a critical role in repairing m
24                                         MutY adenine glycosylases prevent DNA mutations by excising a
25 G:A or G:A substrate, the time course of the adenine glycosylase reaction exhibits biphasic kinetic b

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