N 6 -( 2 -isopentenyl) adenosine: biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli |
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| Authors: | John K. Bartz,Dieter Sö ll |
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| Affiliation: | Department of Molecular Biophysics and Biochemistry Yale University New Haven, Connecticut 06520, USA |
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| 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. |
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| Keywords: | iA, N6-(Δ2-isopentenyl-adenosine msiA, 2-methylthio-N6-(Δ2-isopentenyl)adenosine A, adenosine Ap, adenosine 3′-phosphate pA, adenosine 5′-phosphate ψp, pseudouridine 3′-phosphate Cp, cytidine 3'-phosphate BD-cellulose, benzoylated DEAE-cellulose |
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