Guarraia L J, Peck H D
J Bacteriol. 1971 Jun;106(3):890-5. doi: 10.1128/jb.106.3.890-895.1971.
A dinitrophenol (DNP)-stimulated adenosine triphosphatase (ATPase) has been found in both the soluble and particulate fractions of the anaerobic sulfate-reducing bacterium, Desulfovibrio gigas. As the soluble ATPase was labile to storage, only the particulate enzyme was studied in detail. It was optimally stimulated by DNP at 4 mm, and activity was insensitive to inhibition by ouabain. The ATPase was stimulated by both Ca(2+) and Mg(2+), but the magnitude of the stimulation was dependent upon pH. In the presence of Ca(2+) the optimum pH was 6.5, whereas, in the presence of Mg(2+) the pH optimum was 8.0. However, under optimal conditions the activity was the same with either Mg(2+) or Ca(2+). Both adenosine triphosphate and guanosine triphosphate were hydrolyzed, but activity toward guanosine triphosphate was only one-tenth that observed with adenosine triphosphate.
在厌氧硫酸盐还原菌巨大脱硫弧菌的可溶性组分和颗粒组分中均发现了一种二硝基苯酚（DNP）刺激的三磷酸腺苷酶（ATPase）。由于可溶性ATPase对储存不稳定，因此仅对颗粒酶进行了详细研究。它在4 mM的DNP作用下受到最佳刺激，并且活性对哇巴因的抑制不敏感。该ATPase受到Ca(2+)和Mg(2+)的刺激，但刺激程度取决于pH值。在Ca(2+)存在下，最佳pH值为6.5，而在Mg(2+)存在下，最佳pH值为8.0。然而，在最佳条件下，Mg(2+)或Ca(2+)的活性相同。三磷酸腺苷和三磷酸鸟苷均被水解，但对三磷酸鸟苷的活性仅为三磷酸腺苷的十分之一。
