Abstract: | An enzyme has been partially purified from Escherichia coli which catalyzes in vitro the transfer of the Δ2-isopentenyl group from Δ2-isopentenyl pyrophosphate to an adenosine residue in Mycoplasma sp. (Kid) tRNA. The product of the reaction is N6-(Δ2-isopentenyl) adenosine, which is known to be absent in this Mycoplasma tRNA. The enzyme has an approximate molecular weight of 55,000 daltons, requires reduced sulfhydryl groups and a divalent metal ion for full activity, and is specific for tRNA. |