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- W2035960468 abstract "Apurinic/apyrimidinic endonuclease (AP endo, HAP1) recognizes abasic sites in ds DNA and makes a single nick in the backbone 5′ to the abasic site. In this report we examine the roles of three conserved tyrosine residues in close proximity to the active site. We show that Tyr128 and Tyr269, which interact upstream and downstream of the abasic site, respectively, are involved in recognition and binding of abasic site-containing double stranded DNA. However, the two residues are not equivalent, as their effects are differentiated by changes in salt concentration. In sharp contrast, Tyr171 is directly involved in catalysis as well as binding. Y171F, Y171H, and Y171A all show decreased catalytic efficiencies 25,000–50,000-fold from the WT enzyme. Both imidazole and basic pH markedly stimulate the WT enzyme. Imidazole stimulates Tyr171 mutant enzymes when tyrosine is also present but basic pH eliminates remaining mutant activity. These results underscore the importance of tyrosines in AP endo catalysis. They render the current hypotheses regarding enzyme action unlikely and allow us to consider the possibility that the phenolate of Tyr171 is the nucleophile that attacks the scissile phosphate." @default.
- W2035960468 created "2016-06-24" @default.
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- W2035960468 date "2004-11-01" @default.
- W2035960468 modified "2023-09-26" @default.
- W2035960468 title "Novel role of tyrosine in catalysis by human AP endonuclease 1" @default.
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- W2035960468 doi "https://doi.org/10.1016/j.dnarep.2004.06.009" @default.
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