Identification of a vanadate-sensitive, membrane-bound ATPase in the archaebacterium Methanococcus voltae.
Membrane-bound ATPase activity was detected in the methanogen Methanococcus voltae. The ATPase was inhibited by vanadate, a characteristic inhibitor of E1E2 ATPases. The enzyme activity was also inhibited by diethylstilbestrol. However, it was insensitive to N,N'-dicyclohexylcarbodiimide, ouabain, and oligomycin. The enzyme displayed a high preference for ATP as substrate, was dependent on Mg2+, and had a pH optimum of approximately 7.5. The enzyme was completely solubilized with 2% Triton X-100. The enzyme was insensitive to oxygen and was stabilized by ATP. There was no homology with the Escherichia coli F0F1 ATPase at the level of DNA and protein. The membrane-bound M. voltae ATPase showed properties similar to those of E1E2 ATPases.
D000251:Adenosine Triphosphatases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D002499:Centrifugation, Density Gradient; D004269:DNA, Bacterial / Q000032:analysis; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004054:Diethylstilbestrol / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D019605:Euryarchaeota / Q000201:enzymology* / Q000648:ultrastructure; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D009840:Oligomycins / Q000494:pharmacology; D010042:Ouabain / Q000494:pharmacology; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology*
D004269:DNA, Bacterial; D009840:Oligomycins; D014639:Vanadium; D014638:Vanadates; D004024:Dicyclohexylcarbodiimide; D010042:Ouabain; D004054:Diethylstilbestrol; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D008274:Magnesium