Membrane-bound ATPase of a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius.
Membrane-bound ATPase of a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius.
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嗜热嗜酸古细菌，酸热硫化叶菌的膜结合 ATP 酶。
DOI：
10.1016/0005-2736(85)90065-3
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
T. Oshima
中科院分区：
文献类型：
--
作者：
T. Wakagi;T. Oshima
嗜热嗜酸古细菌硫化叶菌的细胞膜具有两种ATP水解活性。一种是中性ATP酶，最适pH为6.5左右。该酶被10 mM硫酸盐激活，最适pH值变为5。在这些方面，该酶类似于Searcy和Whatley（（1982）Zbl.巴克特Hyg.，I. ABT. Orig.C3，245-257）。该酶水解ATP和其他NTPs，但不水解ADP或AMP。它是高度热稳定的，但在0.1 M HCl中不可逆地失活。另一种活性是酸性腺苷三磷酸双磷酸酶在最适pH 2.5左右的活性。该酶对高温和酸性非常稳定，且受硫酸盐抑制。这两种ATP水解酶对N，N′-二环己基碳二亚胺（DCCD）、叠氮化合物、寡霉素、N′-乙基马来酰亚胺、对氯汞苯甲酸盐、原钒酸盐和哇巴因均具有抗性。硫化叶菌ATP酶不同于F1和迄今为止描述的其它转运ATP酶.
The membranes of Sulfolobus, a thermoacidophilic archaebacterium showed two types of ATP hydrolyzing activity. One was that of a neutral ATPase at an optimum pH around 6.5. This enzyme was activated by 10 mM sulfate with a shift of optimum pH to 5. In these respects, the enzyme was similar to membrane-bound ATPase of Thermoplasma, another thermoacidophilic archaebacterium, reported by Searcy and Whatley ((1982) Zbl. Bakt. Hyg., I. Abt. Orig. C3, 245–257). The enzyme hydrolyzed ATP and other NTPs, but not ADP or AMP. It was highly thermostable, but irreversibly inactivated in 0.1 M HCl. The other activity was that of an acidic apyrase at an optimum pH around 2.5. This enzyme was extremely stable toward high temperature and acid and inhibited by sulfate. Both of these ATP hydrolyzing enzymes were resistant to N, N′-dicyclohexylcarbodiimide (DCCD), azide, oligomycin, N′-ethylmaleimide, p-chloromercuribenzoate, orthovanadate, or ouabain. Sulfolobus ATPases differ from F 1 and other transport ATPases so far described.