A comparison of enzymatic phosphorylation and phosphatidylation of b-l- and b-d-nucleosides

Enzymatic 5'-monophosphorylation and 5'-phosphatidylation of a number of b-l- and b-d-nucleosides was investigated. The first reaction, catalyzed by nucleoside phosphotransferase (NPT) from Erwinia herbicola, consisted of the transfer of the phosphate residue from p-nitrophenylphosphate (p-NPP) to the 5'-hydroxyl group of nucleoside; the second was the phospholipase d (PLD)-catalyzed transphosphatidylation of l-a-lecithin with a series of b-l- and b-d-nucleosides as the phosphatidyl acceptor resulted in the formation of the respective phospholipid-nucleoside conjugates. Some b-l-nucleosides displayed similar or even higher substrate activity compared to the b-d-enantiomers.