Abstract
The removal of damaged bases by DNA glycosylases is thought to be effectively irreversible, because of an overall equilibrium that favors hydrolysis over synthesis of the N-glycosyl bond. Surprisingly, human alkyladenine DNA glycosylase (AAG) can make damaged DNA by catalyzing formation of an N-glycosyl bond between 1,N(6)-ethenoadenine (εA) and abasic DNA. We attribute the ready reversibility of this glycosylase reaction to the exceptionally tight binding and slow subsequent hydrolysis of DNA containing an εA lesion. In principle, reversibility could provide a mechanism for direct reversal of base damage by a DNA glycosylase, allowing the glycosylase to bypass the rest of the base excision repair pathway.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
