[Interaction of oligophosphates of pyridoxal with certain enzymes of polynucleotide synthesis].
The interaction of pyridoxal, pyridoxal-5'-mono-, di- and triphosphate with certain enzymes of polynucleotide synthesis (DNA-dependent RNA polymerase, DNA-dependent DNA polymerase I and polynucleotide phosphorylase from Escherichia coli and terminal deoxyribonucleotide transferase from calf thymus) was studied. All compounds tested was found to be reversible and competitive inhibitors of these enzymes. The reduction of the enzyme-inhibitor complex with NaBH4 gives rise to the complete irreversible inhibition of the enzymes under study. The comparison of the inhibition constants for pyridoxal and its phosphorylated derivatives with those for mono-, di- and triphosphates of nucleosides was carried out for the enzymes. The results obtained suggest that the modified epsilon-amino-group of lysine residue should be localized at the catalytic site in the vicinity of the pyrophosphate binding area of an enzyme.
D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004256:DNA Polymerase I / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D011117:Polyribonucleotide Nucleotidyltransferase / Q000378:metabolism*; D011730:Pyridoxal / Q000494:pharmacology*; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013950:Thymus Gland / Q000201:enzymology
D011730:Pyridoxal; D011732:Pyridoxal Phosphate; D004254:DNA Nucleotidyltransferases; D012321:DNA-Directed RNA Polymerases; D004256:DNA Polymerase I; D004259:DNA-Directed DNA Polymerase; D011117:Polyribonucleotide Nucleotidyltransferase
Vzaimodeĭstvie oligofosfatov piridoksalia s polinukleotidsinteziruiushchimi fermentami.