A stereochemical study of the mechanism of activation of donor oligonucleotides by RNA ligase from bacteriophage T4 infected Escherichia coli

Abstract
RNA ligase from bacteriophage T4 infected Escherichia coli catalyzes the activation of adenosine 3'',5''-bisphosphate (representing the donor oligonucleotide) by adenosine 5''-[(S)-.alpha.-17O,.alpha.,.alpha.-18O2]triphosphate with retention of configuration at P.alpha.. Since single-step enzyme-catalyzed nucleotidyl transfer reactions proceed with inversion, this stereochemical result provides support for a double displacement mechanism involving an adenylyl-enzyme intermediate as proposed previously from isotope exchange experiments.

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