Effect of ADP on ATPASE from a strain of Bacillus stearothermophilus.
Bacillus stearothermophilus ATCC 12016 was unable to grow at temperatures below 40 degrees C. On incubating the bacteria at the temperatures, ATP in cells disappeared, ADP was accumulated and ATPase (EC 3.6.1.3) was inactivated. When the purified ATPase was incubated at the temperatures for 1 h with 0.17 mM ADP in the presence of MgCl2, the enzyme was completely inactivated. The inactivated enzyme was reactivated on dilution or dialysis or on warming at 65 degrees C. During the incubation of the enzyme sample, the absorbance spectrum of the enzyme changed. On further incubating the sample over 1.5 h, the second step of spectral change occurred together with the change of the circular dichrosim and the dissociation into a lower molecular weight species of the protein. When the enzyme was treated with ADP-MgCl2 at 65 degrees C, the inactivation and conformational change of the enzyme was not observed.
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases; D008274:Magnesium