DNA-dependent ATPase II from Bacillus cereus.
A new DNA-dependent ATPase been purified close to homogeneity from soluble extracts of Bacillus cereus. This enzyme, called ATPase II catalyses the hydrolysis of ATP in the presence of Mg2+ or Ca2+ and DNA. Single-stranded linear DNA is a cofactor about 3-fold more effective than double-stranded DNA. The enzyme catalyses the strand separation of duplex DNA in the presence of ATP. However, at concentrations higher than 0.5 mM, phosphohydrolysis can occur without concomitant DNA unwinding. The enzyme has a molecular weight of 84 000 according to SDS-polyacrylamide gel electrophoresis. ATPase II is inhibited by adenosine 5'-(beta, gamma-imido)-diphosphate, actinomycin D and ethidium bromide, but not by nalidixic acid.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology; D001409:Bacillus cereus / Q000201:enzymology*; D004265:DNA Helicases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism; D008970:Molecular Weight
D004277:DNA, Single-Stranded; D000266:Adenylyl Imidodiphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D004265:DNA Helicases