Abstract
Treatment of adenosine with PSCl~3~ in trimethyl phosphate gave, after ion‐exchange chromatography, adenosine‐5′‐O‐monophosphate (AMP; 28%) and adenosine‐5′‐O‐monothiophosphate (AMPS; 48%). AMPS was studied as a thiophosphate residue donor in an enzymatic transphosphorylation with nucleoside phosphotransferase (NPase) of the whole cells of Erwinia herbicola. As exemplified by a number of natural and sugar‐ and base‐modified nucleosides, it was demonstrated that NPase of the whole cells of Erwinia herbicola catalyzes the transfer of both thiophosphate and phosphate residues with a similar efficiency. An incubation of AMPS in a phosphorylating extract of Saccharomyces cerevisiae (K‐phosphate buffer (0.3 M, pH 7.0); 3% glucose; 15 mM MgCl~2~; 28°, 8 h), followed by ion‐exchange column chromatography afforded AMP (8%), AMPS (recovered, 23%), ATP (11%), and (S~P~)‐adenosine‐5′‐O‐(1‐thiotriphosphate) ((S~P~)‐ATP__α__S); (total yield 37%; 48% based on the consumed AMPS). For comparison of physicochemical properties, adenosine was chemically transformed into ATP__α__S as a mixture of the (S~P~) (53%) and (R~P~) (44%) diastereoisomers.