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The reconstituted alpha 3 beta 3 delta complex of the thermostable F1-ATPase.
Yokoyama K, Hisabori T, Yoshida M. Yokoyama K, et al. Among authors: yoshida m. J Biol Chem. 1989 Dec 25;264(36):21837-41. J Biol Chem. 1989. PMID: 2532213 Free article.
Unlike that of holoenzyme (TF1) and the alpha + beta + gamma mixture, ATPase activity of the alpha + beta + delta mixture was heat labile and insensitive to azide inhibition (Yoshida, M., Sone, N., Hirata, H., and Kagawa, Y. (1977) J. Biol. Chem. 252, 3480-3485). .. …
Unlike that of holoenzyme (TF1) and the alpha + beta + gamma mixture, ATPase activity of the alpha + beta + delta mixture was heat labile an …
Asymmetry of the three catalytic sites on beta subunits of TF1 from a thermophilic Bacillus strain PS3.
Hisabori T, Kobayashi H, Kaibara C, Yoshida M. Hisabori T, et al. Among authors: yoshida m. J Biochem. 1994 Mar;115(3):497-501. doi: 10.1093/oxfordjournals.jbchem.a124365. J Biochem. 1994. PMID: 8056763 Free article.
However, it can bind one ADP per mol of the enzyme on one of three beta subunits to form a stable TF1.ADP complex when incubated with a high concentration of ADP [Yoshida, M. & Allison, W.S. (1986) J. Biol. Chem. 261, 5714-5721]. The same TF1.ADP complex was rec …
However, it can bind one ADP per mol of the enzyme on one of three beta subunits to form a stable TF1.ADP complex when incubated with a high …
Structural asymmetry of F1-ATPase caused by the gamma subunit generates a high affinity nucleotide binding site.
Kaibara C, Matsui T, Hisabori T, Yoshida M. Kaibara C, et al. Among authors: yoshida m. J Biol Chem. 1996 Feb 2;271(5):2433-8. doi: 10.1074/jbc.271.5.2433. J Biol Chem. 1996. PMID: 8576203 Free article.
Surprisingly, in spite of very weak affinity of the isolated mutant beta subunits to nucleotides (Odaka, M., Kaibara, C., Amano, T., Matsui, T., Muneyuki, E., Ogasawara, K, Yutani, K., and Yoshida, M. (1994) J. ...
Surprisingly, in spite of very weak affinity of the isolated mutant beta subunits to nucleotides (Odaka, M., Kaibara, C., Amano, T., …
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