Purification and characterization of a DNA-dependent ATPase from Bacillus cereus.
A DNA-dependent ATPase (molecular weight 71 000) free of nuclease activity has been purified from Bacillus cereus. The enzyme shows similar characteristics as the enzyme isolated from Escherichia coli and Bacillus subtilis. Heat denatured DNA stimulates the rate of ATP hydrolysis to ADP and Pi to an extent about tenfold higher than the native DNA. Double stranded DNA without single stranded regions is not a suitable cofactor for the enzyme. The ATPase is inhibited by adenosine 5'-(beta, gamma-imino)-diphosphate, while another ATP analogue, adenosine 5'-(beta, gamma-methylene)-diphosphate has no effect on ATPase activity. KM for ATP is 0.38 mM, the apparent KM for nucleotide equivalent DNA is 1.2 microM. Evidence of the unwinding function of the enzyme is presented.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification* / Q000378:metabolism; D001409:Bacillus cereus / Q000201:enzymology*; D004247:DNA / Q000378:metabolism / Q000494:pharmacology*; D004269:DNA, Bacterial / Q000494:pharmacology; D004277:DNA, Single-Stranded / Q000494:pharmacology; D008970:Molecular Weight
D004269:DNA, Bacterial; D004277:DNA, Single-Stranded; D004247:DNA; D000251:Adenosine Triphosphatases