Inhibition of ATPase activity of the recA protein by ATP ribose-modified analogs.
The single-stranded, DNA-dependent ATPase activity of purified recA protein was found to be inhibited competitively by ribose-modified analogs of ATP, 3'-O-anthraniloyl-ATP (Ant-ATP), and 3'-O-(N-methylanthraniloyl)-ATP (Mant-ATP). The Ki values for Ant-ATP and Mant-ATP were around 7 and 3 microM at pH 7.5, respectively. The inhibitions by these analogs were much stronger than that by ADP, which is also a competitive inhibitor for the ATPase activity of the recA protein. The Ki value for ADP is 76 microM. Ant-ATP and Mant-ATP reduced the Hill coefficient for ATP hydrolysis and thus contributed to the cooperative effect of ATP.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000494:Allosteric Regulation; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors; D001665:Binding Sites / Q000187:drug effects; D001667:Binding, Competitive; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000378:metabolism; D005796:Genes; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011938:Rec A Recombinases / Q000037:antagonists & inhibitors* / Q000235:genetics
D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D011938:Rec A Recombinases; D000251:Adenosine Triphosphatases