A comparison of enzymatic phosphorylation and phosphatidylation of beta-L- and beta-D-nucleosides.
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.
Birichevskaya
Larisa L
LL
Institute of Microbiology, National Academy of Sciences, Minsk, Belarus.
Kvach
Sergei V
SV
Sivets
Grigorii G
GG
Kalinichenko
Elena N
EN
Zinchenko
Anatoly I
AI
Mikhailopulo
Igor A
IA
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
D009705:Nucleosides; D010770:Phosphotransferases; C021892:nucleoside phosphotransferase