Dharmavaram R M, Konisky J
J Bacteriol. 1987 Sep;169(9):3921-5. doi: 10.1128/jb.169.9.3921-3925.1987.
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.
在产甲烷菌沃氏甲烷球菌中检测到膜结合ATP酶活性。该ATP酶被钒酸盐抑制，钒酸盐是E1E2 ATP酶的典型抑制剂。该酶活性也被己烯雌酚抑制。然而，它对N，N'-二环己基碳二亚胺、哇巴因和寡霉素不敏感。该酶对ATP作为底物表现出高度偏好，依赖于Mg2+，最适pH约为7.5。该酶用2% Triton X-100可完全溶解。该酶对氧气不敏感，且被ATP稳定。在DNA和蛋白质水平上与大肠杆菌F0F1 ATP酶没有同源性。膜结合的沃氏甲烷球菌ATP酶表现出与E1E2 ATP酶相似的特性。
