Inhibition of the activities of DNA primase-polymerase alpha complex from KB cells by hexasodium sym-bis(m-aminobenzoyl-m-amino-p-methylbenzoyl-1-naphthylamino-4 ,6,8-trisulfonate)carbamide.
A trypanocidal drug suramin [hexasodium sym-bis(m-amino-benzoyl-m-amino-p-methylbenzoyl-1-naphthylamino-4, 6, 8-trisulfonate)carbamide] was found to be a potent inhibitor of the activities of DNA primase and polymerase alpha from human KB cells. The mechanism of the inhibition by suramin was, however, quite different by these two polymerases. In the case of DNA primase, suramin inhibited competitively the incorporation of a nucleotide substrate, GTP, on the template polydeoxycytidylate, while the polymerase alpha was inhibited competitively by the drug with respect to the template primer (activated DNA). The observed inhibitory effect of suramin on nucleic acid synthesis seems to explain yet unknown mechanism of trypanocidal action of the drug.
D001667:Binding, Competitive; D004257:DNA Polymerase II / Q000037:antagonists & inhibitors*; D019915:DNA Primase; D006801:Humans; D007624:KB Cells / Q000201:enzymology*; D007700:Kinetics; D019384:Nucleic Acid Synthesis Inhibitors; D012316:RNA Nucleotidyltransferases / Q000037:antagonists & inhibitors*; D013498:Suramin / Q000494:pharmacology*
D019384:Nucleic Acid Synthesis Inhibitors; D013498:Suramin; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases; D004257:DNA Polymerase II