The intriguing chemical mechanism of the external transesterification by which large ribozymes
(group I, group II, and spliceosomal introns) splice RNA has been found to operate in the methanolysis of
ribonucleoside 2‘-/3‘-dimethyl phosphates in non-hydrogen-bonding organic solvents. Besides needing aprotic
organic media this mechanism requires a high concentration of the attacking alcohol accounting for the binding
of an external guanosine by group I introns and the use of a non-adjacent internal 2‘-OH by group II and
spliceosomal introns. This finding is the first example of an external non-ribozymic transesterification of
ribonucleotide esters and the means by which this crucial biochemical reaction can be accelerated.
The aminolysis of a mildly activated aminoacid ester, benzyloxycarbonyl-L-phenylalanine cyanomethyl ester, by glycine esters in the presence of catechol has been studied as a model of catalysis by RNA cis-vicinal-diol systems in protein biosynthesis. Catechol accelerated the aminolysis, especially in the presence of bases, probably by nucleophilic catalysis.
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