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

Author: Birichevskaya Larisa   Kvach Sergei   Sivets Grigorii   Kalinichenko Elena   Zinchenko Anatoly   Mikhailopulo Igor  

Publisher: Springer Publishing Company

ISSN: 0141-5492

Source: Biotechnology Letters, Vol.29, Iss.4, 2007-04, pp. : 585-591

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Abstract

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