Membrane-bound ATPase of a Psychrophilic Marine Bacterium, Vibrio sp. Strain ABE-1

概要

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Several properties of ATPase bound to the inner membrane of a psychrophilic marine bacterium Vibrio sp. strain ABE-1 were examined. The membrane-bound ATPase had two optimal peaks of the activity at pH 5.8 and 7.3. The ATPase activity was strongly inhibited by N,N'-dicyclohexylcarbodiimide (DCCD) and NaN_3 at pH 5.8 and 8.0, and stimulated by MgCl_2 and CaCl_2 at pH 8.0. At pH 8.0, the enzyme hydrolyzed GTP and ITP as well as ATP but not AMP or p-nitrophenylphosphate. CTP, UTP, and ADP were poor substrates. These characteristics indicate that there is a F_0F_1-type ATPase in the inner membrane of this bacterium. In addition, the ATPase activity was also significantly inhibited by Na_3VO_4, suggesting the coexistence of a P-type ATPase as a minor constituent. The membrane-bound ATPase activity was maximum at 50℃, but the strong DCCD-sensitivity observed at 20℃ was greatly reduced at this temperature.
社団法人日本農芸化学会の論文
1993-06-23