The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG-Reference-Cited by-同舟云学术

The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG

Published:2014 Issue:83 Volume:4 Page:44043-44051
ISSN:2046-2069
Container-title:RSC Adv.
language:en
Short-container-title:RSC Adv.

Author:

Šebera Jakub¹²,Trantírek Lukáš³⁴,Tanaka Yoshiyuki⁵⁶⁷,Nencka Radim¹²,Fukal Jiří¹²,Sychrovský Vladimír¹²

Affiliation:

1. Institute of Organic Chemistry and Biochemistry AS CR, v.v.i.

2. 16610 Praha, Czech Republic

3. Central European Institute of Technology – Masaryk University

4. 625 00 Brno, Czech Republic

5. Division of Pharmaceutical Chemistry

6. Tohoku University

7. Sendai, Japan

Abstract

NLMOs of lone-pair electrons at N9 nitrogen and Fukui indexesf²of N9.

Funder

Czech Science Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2014/RA/C4RA08278H

Reference62 articles.

1. Toward a Detailed Understanding of Base Excision Repair Enzymes: Transition State and Mechanistic Analyses of N-Glycoside Hydrolysis and N-Glycoside Transfer

2. Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair

3. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily

4. Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites

5. The critical active-site amine of the human 8-oxoguanine DNA glycosylase, hOgg1: direct identification, ablation and chemical reconstitution

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4. Benchmark Theoretical and Experimental Study on 15N NMR Shifts of Oxidatively Damaged Guanine;The Journal of Physical Chemistry B;2016-02-01

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