ß‐Subunit of Escherichia coli F1‐ATPase

FEBS Letters

Futai, Masamitsu²  Maeda, Masatomo²  Ishibashi, Sadahiko¹  Noumi, Takato²  Hsu, Shih-Yuan²  Takeyama, Michiyasu² 

[1] Department of Physiological Chemistry, Hiroshima University School of Medicine, Kasumi, Hiroshima 734 Japan;Department of Organic Chemistry and Biochemistry, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567, Japan

关键词: F1-ATPase;    Nucleotide-binding protein;    Uni-site catalysis;    Oncogene;   

DOI  :  10.1016/0014-5793(87)81050-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A mutant strain KF87 of E. coli with a defective ß-subunit (Ala-151 → Val) of F₁-ATPase was isolated. The mutation is within the conserved sequence (G-X-X-X-X-G-K-T/S) of nucleotide-binding proteins. The mutant F₁-ATPase had a much higher rate of uni-site hydrolysis of ATP than the wild type, and about 6% of the wild-type multi-site activity. The mutant enzyme showed defective transmission of conformational change(s) between the ligand- and aurovertin-binding sites.

【 授权许可】

Unknown