Abstract
The chapter discusses the various classes of major deoxyribonucleic acid (DNA) glycosylases characterized so far in both eukaryotes and prokaryotes. The chapter discusses their general properties, such as: (1) most DNA glycosylases, with the notable exception of UDG, have strong preference for duplex DNA even though their initial substrate recognition may require subtle structural perturbation or base unpairing at the site of lesion. The base or nucleotide flipping appears to be the common mechanism of substrate recognition and catalysis, by all DNA glycosylases, and (2) DNA glycosylases require no cofactor, including exogenous divalent metal ions. The chapter discusses the specificity and the mechanism of DNA glycosylases is limited to DNA glycosylases responsible for the repair of 8-oxoguanine and thymine (U) in G.T (U) pairs. The mechanism and structural basis of enzymatic activity of several other DNA glycosylases have been extensively discussed in this chapter.
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