The Tetrahymena ribozyme cleaves a 5'-methylene phosphonate monoester about 10 (super)2 -fold faster than a normal phosphate diester: implications for enzyme catalysis of phosphoryl transfer reactions

Research has been conducted on the transition state interactions in the Tetrahymena ribozyme reaction. The oxygen atoms near the reaction center have been examined in investigating the effect of these interactions on the catalysis, and the use of the new type DNA substrate where 5'-oxygen is replaced with a methylene has been described.