title: A comparison of enzymatic phosphorylation and phosphatidylation of beta-L- and beta-D-nucleosides.
abstract: Enzymatic 5'-monophosphorylation and 5'-phosphatidylation of a number of beta-L- and beta-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-alpha-lecithin with a series of beta-L- and beta-D-nucleosides as the phosphatidyl acceptor resulted in the formation of the respective phospholipid-nucleoside conjugates. Some beta-L-nucleosides displayed similar or even higher substrate activity compared to the beta-D-enantiomers.
authors.affiliation: Institute of Microbiology, National Academy of Sciences, Minsk, Belarus.
authors.forename: Larisa L
authors.initials: LL
authors.lastname: Birichevskaya
authors.forename: Sergei V
authors.initials: SV
authors.lastname: Kvach
authors.forename: Grigorii G
authors.initials: GG
authors.lastname: Sivets
authors.forename: Elena N
authors.initials: EN
authors.lastname: Kalinichenko
authors.forename: Anatoly I
authors.initials: AI
authors.lastname: Zinchenko
authors.forename: Igor A
authors.initials: IA
authors.lastname: Mikhailopulo
mesh_terms: D004789:Enzyme Activation; D004885:Erwinia / Q000201:enzymology*; D007536:Isomerism; D009705:Nucleosides / Q000737:chemistry*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000737:chemistry*; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D009705:Nucleosides; D010770:Phosphotransferases; C021892:nucleoside phosphotransferase