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• W2041421251 startingPage "6498" @default.
• W2041421251 abstract "A mechanism is proposed for the RNA-catalyzed reactions involved in RNA splicing and RNase P hydrolysis of precursor tRNA. The mechanism postulates that chemical catalysis is facilitated by two divalent metal ions 3.9 A apart, as in phosphoryl transfer reactions catalyzed by protein enzymes, such as the 3',5'-exonuclease of Escherichia coli DNA polymerase I. One metal ion activates the attacking water or sugar hydroxyl, while the other coordinates and stabilizes the oxyanion leaving group. Both ions act as Lewis acids and stabilize the expected pentacovalent transition state. The symmetry of a two-metal-ion catalytic site fits well with the known reaction pathway of group I self-splicing introns and can also be reconciled with emerging data on group II self-splicing introns, the spliceosome, and RNase P. The role of the RNA is to position the two catalytic metal ions and properly orient the substrates via three specific binding sites." @default.
• W2041421251 created "2016-06-24" @default.
• W2041421251 creator A5005980770 @default.
• W2041421251 creator A5035064101 @default.
• W2041421251 date "1993-07-15" @default.
• W2041421251 modified "2023-10-09" @default.
• W2041421251 title "A general two-metal-ion mechanism for catalytic RNA." @default.
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• W2041421251 doi "https://doi.org/10.1073/pnas.90.14.6498" @default.
• W2041421251 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/46959" @default.
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