Incision of Pyrimidine Dimer Containing DNA by Small Molecular Weight Enzymes
In Micrococcus luteus the incision event during repair of DNA containing pyrimidine dimers has been shown in vitro to be a two-step enzymatic reaction. The first step results in the cleavage of the N-glycosylic bond between the 5′-thymine moiety of the pyrimidine dimer and the deoxyribose generating an apyrimidinic site (Apy) and a thymine-thymidylate dimer attached to the DNA. The second catalytic step involves phosphodiester bond hydrolysis 3′ to the Apy site generating a nicked DNA with an Apy site at its 3′ terminus and the mixed thymine-thymidylate dimer at the 5′ terminus.
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