A plasma-membrane associated ATPase from the acidophilic bacterium Acidiphilium cryptum.
A membrane-bound ATPase of Acidiphilium cryptum, an acidophilic bacterium of mine origin, has been studied. The enzyme has a pH optimum of 8.4 Mg2+ is required for its activity and could be replaced by Mn2+, but not by Ca2+. The enzyme shows a strong preference for ATP as substrate, with the apparent Km of about 0.2 mM. Sulphite ion significantly stimulated the enzyme activity. N,N'-Dicyclohexylcarbodiimide, oligomycin, and azide strongly inhibited the enzyme, whereas vanadate was without effect, suggesting that the A. cryptum ATPase might be of F0F1 type.
Bhattacharyya
S
S
Indian Institute of Chemical Biology, Calcutta.
Banerjee
P C
PC
Das
P K
PK
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004734:Energy Metabolism / Q000502:physiology; D006091:Gram-Negative Chemolithotrophic Bacteria / Q000201:enzymology*; D007700:Kinetics; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D000251:Adenosine Triphosphatases