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• W2082695635 endingPage "9639" @default.
• W2082695635 startingPage "9635" @default.
• W2082695635 abstract "It has been established that Tyr-42, Tyr-45, and Glu-46 take part in a structural motif that renders guanine specificity to ribonuclease T1. We report on the impact of Tyr-42, Tyr-45, and Glu-46 substitutions on the guanine specificity of RNase T1. The Y42A and E46A mutations profoundly affect substrate binding. No such effect is observed for Y45A RNase T1. From the kinetics of the Y42A/Y45A and Y42A/E46A double mutants, we conclude that these pairs of residues contribute to guanine specificity in a mutually independent way. From our results, it appears that the energetic contribution of aromatic face-to-face stacking interactions may be significant if polycyclic molecules, such as guanine, are involved. It has been established that Tyr-42, Tyr-45, and Glu-46 take part in a structural motif that renders guanine specificity to ribonuclease T1. We report on the impact of Tyr-42, Tyr-45, and Glu-46 substitutions on the guanine specificity of RNase T1. The Y42A and E46A mutations profoundly affect substrate binding. No such effect is observed for Y45A RNase T1. From the kinetics of the Y42A/Y45A and Y42A/E46A double mutants, we conclude that these pairs of residues contribute to guanine specificity in a mutually independent way. From our results, it appears that the energetic contribution of aromatic face-to-face stacking interactions may be significant if polycyclic molecules, such as guanine, are involved." @default.
• W2082695635 created "2016-06-24" @default.
• W2082695635 creator A5001394494 @default.
• W2082695635 creator A5009091494 @default.
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• W2082695635 date "1997-04-01" @default.
• W2082695635 modified "2023-09-30" @default.
• W2082695635 title "Additivity of Protein-Guanine Interactions in Ribonuclease T1" @default.
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• W2082695635 doi "https://doi.org/10.1074/jbc.272.15.9635" @default.
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• W2082695635 hasPublicationYear "1997" @default.
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