Abstract
We used mutants of RNase T1 and the Rp isomer of a thiosubstituted substrate to determine stereospecific thioeffects on catalysis. The analysis reveals subtle structural and functional changes in the Lntermolecular transition state interactions. Tyr 38 contributes to catalysis through a hydrogen bond with the pro-Rp oxygen. Y38F RNase T1 prefers the Rp thiosubstituted analog over the natural phosphodiester substrate that is favored by the wild type enzyme.
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Loverix, S., Winquist, A., Strömberg, R. et al. An engineered ribonuclease preferring phosphorothioate RNA. Nat Struct Mol Biol 5, 365–368 (1998). https://doi.org/10.1038/nsb0598-365
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DOI: https://doi.org/10.1038/nsb0598-365
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