Kinetic Mechanism for the Excision of Hypoxanthine by Escherichia coli AlkA and Evidence for Binding to DNA Ends
Author:
Affiliation:
1. Department of Biomedical Engineering and ‡Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi200232c
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5. Escherichia coil,Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA
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2. Biochemical characterization and mutational studies of a novel 3-methlyadenine DNA glycosylase II from the hyperthermophilic Thermococcus gammatolerans;DNA Repair;2021-01
3. Recognition of 1,N2-ethenoguanine by alkyladenine DNA glycosylase is restricted by a conserved active-site residue;Journal of Biological Chemistry;2020-02
4. Aag Hypoxanthine-DNA Glycosylase Is Synthesized in the Forespore Compartment and Involved in Counteracting the Genotoxic and Mutagenic Effects of Hypoxanthine and Alkylated Bases in DNA during Bacillus subtilis Sporulation;Journal of Bacteriology;2016-12-15
5. Base Excision Repair Enzymes Protect Abasic Sites in Duplex DNA from Interstrand Cross-Links;Biochemistry;2015-02-26
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