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Volume 271, Number 46, Issue of November 15, 1996 pp. 28818-28824
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

The alpha 3beta 3gamma Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the beta T165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover

(Received for publication, June 24, 1996, and in revised form, August 5, 1996)

Jean-Michel Jault Dagger , Chao Dou Dagger , Neil B. Grodsky Dagger , Tadashi Matsui , Masasuke Yoshida and William S. Allison Dagger

From the Dagger  Department of Chemistry and Biochemistry, School of Medicine, University of California at San Diego, La Jolla, California 92093-0601 and  Tokyo Institute of Technology, Research Laboratory of Resources Utilization, R-1, 4259 Nagastuta, Yokohama 227, Japan

The hydrolytic properties of the mutant alpha 3(beta T165S)3gamma and wild-type alpha 3beta 3gamma subcomplexes of TF1 have been compared. Whereas the wild-type complex hydrolyzes 50 µM ATP in three kinetic phases, the mutant complex hydrolyzes 50 µM ATP with a linear rate. After incubation with a slight excess of ADP in the presence of Mg2+, the wild-type complex hydrolyzes 2 mM ATP with a long lag. In contrast, prior incubation of the mutant complex under these conditions does not affect the kinetics of ATP hydrolysis. The ATPase activity of the wild-type complex is stimulated 4-fold by 0.1% lauryl dimethylamine oxide, whereas this concentration of lauryl dimethylamine oxide inhibits the mutant complex by 25%. Compared with the wild-type complex, the activity of the mutant complex is much less sensitive to turnover-dependent inhibition by azide. This comparison suggests that the mutant complex does not entrap substantial inhibitory MgADP in a catalytic site during turnover, which is supported by the following observations. ATP hydrolysis catalyzed by the wild-type complex is progressively inhibited by increasing concentrations of Mg2+ in the assay medium, whereas the mutant complex is insensitive to increasing concentrations of Mg2+. A Lineweaver-Burk plot constructed from rates of hydrolysis of 20-2000 µM ATP by the wild-type complex is biphasic, exhibiting apparent Km values of 30 µM and 470 µM with corresponding kcat values of 26 and 77 s-1. In contrast, a Lineweaver-Burk plot for the mutant complex is linear in this range of ATP concentration, displaying a Km of 133 µM and a kcat of 360 s-1.


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