Kinetic analysis of the contribution of base flipping to the substrate specificity and catalytic activity of human alkyladenine dna glycosylase [electronic resource] /

by Vallur, Aarthy C.

Abstract (Summary)
ABSTRACT: KINETIC ANALYSIS OF THE CONTRIBUTION OF BASE FLIPPING TO THE SUBSTRATE SPECIFICITY AND CATALYTIC ACTIVITY OF HUMAN ALKYLADENINE DNA GLYCOSYLASE Human alkyladenine DNA glycosylase (AAG) removes a variety of alkylated and deaminated bases from double stranded DNA to initiate base excision repair of damaged adenines. The crystal structure of AAG shows that the enzyme uses a characteristic base flipping mechanism and does so by using Tyr- 162 to intercalate through the minor groove and occupy the space vacated by the flipped out substrate. The purpose of this dissertation is to further understand the contribution of base flipping to the specificity and efficiency of AAG. A Y162S mutant showed undetectable activity on hypoxanthine (Hx) and 1, N6- ethenoadenine (?A) substrates.
Bibliographical Information:


School:University of Florida

School Location:USA - Florida

Source Type:Master's Thesis

Keywords:research dna glycosylases repair toluene adenine hypoxanthine alkyladenine


Date of Publication:

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