(Q45028083)

8 December 2017

title

Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase (English)

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8 December 2017

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Raymond C Manuel

1

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8 December 2017

Kenichi Hitomi

2

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8 December 2017

Andrew S Arvai

3

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8 December 2017

Paul G House

4

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8 December 2017

Andrew J Kurtz

5

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8 December 2017

M L Dodson

6

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8 December 2017

Amanda K McCullough

7

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8 December 2017

John A Tainer

8

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8 December 2017

R Stephen Lloyd

9

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8 December 2017

language of work or name

English

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publication date

23 August 2004

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Journal of Biological Chemistry

8 December 2017

published in

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8 December 2017

volume

279

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8 December 2017

issue

45

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8 December 2017

page(s)

46930-46939

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A mechanistic perspective on the chemistry of DNA repair glycosylases

8 December 2017

cites work

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Mechanistic comparisons among base excision repair glycosylases

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Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition

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A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA

21 January 2018

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MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily

21 January 2018

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Structural basis for the excision repair of alkylation-damaged DNA

21 January 2018

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Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA

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DNA bending and a flip-out mechanism for base excision by the helix–hairpin–helix DNA glycosylase, Escherichia coli AlkA

21 January 2018

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Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase

21 January 2018

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T4 endonuclease V: use of NMR and borohydride trapping to provide evidence for covalent enzyme-substrate imine intermediate

21 January 2018

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Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA.

21 January 2018

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The active site of the Escherichia coli MutY DNA adenine glycosylase

21 January 2018

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Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain

21 January 2018

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Flipping duplex DNA inside out: a double base-flipping reaction mechanism by Escherichia coli MutY adenine glycosylase

21 January 2018

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DNA-mediated charge transport as a probe of MutY/DNA interaction

21 January 2018

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DNA-mediated charge transport for DNA repair

21 January 2018

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Probing the requirements for recognition and catalysis in Fpg and MutY with nonpolar adenine isosteres

21 January 2018

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Catalytic mechanism and DNA substrate recognition of Escherichia coli MutY protein.

21 January 2018

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Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme

21 January 2018

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21 January 2018

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XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

21 January 2018

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Potential double-flipping mechanism by E. coli MutY.

21 January 2018

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Evidence for multiple imino intermediates and identification of reactive nucleophiles in peptide-catalyzed beta-elimination at abasic sites

21 January 2018

1 reference

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AP endonuclease-independent DNA base excision repair in human cells

21 January 2018

1 reference

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Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M403944200

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8 December 2017

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