scholarly journals Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied.

1993 ◽  
Vol 268 (27) ◽  
pp. 20126-20133
Author(s):  
J Weber ◽  
S Wilke-Mounts ◽  
R.S. Lee ◽  
E Grell ◽  
A.E. Senior
Keyword(s):  
Escherichia Coli ◽  
Atp Hydrolysis ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Catalytic Sites

scholarly journals Observation of Asymmetry amongst Nucleotide Binding Sites of F1-ATPase of Escherichia coli by31P NMR Spectroscopy

2011 ◽  
Vol 32 (2) ◽  
pp. 531-535 ◽  
Author(s):  
Nam-Kung Jun ◽  
Joon-Hyung Sohn ◽  
Byung-Il Yeh ◽  
Jong-Whan Choi ◽  
Hyun-Won Kim
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Nucleotide Binding Sites

scholarly journals α3β3γ complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites

1999 ◽  
Vol 343 (1) ◽  
pp. 135 ◽  
Author(s):  
Toyoki AMANO ◽  
Tadashi MATSUI ◽  
Eiro MUNEYUKI ◽  
Hiroyuki NOJI ◽  
Kiyotaka HARA ◽  
...  
Keyword(s):  
Steady State ◽  
Atp Hydrolysis ◽  
Thermophilic Bacillus ◽  
F1 Atpase ◽  
Catalytic Sites ◽  
Hydrolysis Activity

.epsilon. Subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis

Biochemistry ◽  
1987 ◽  
Vol 26 (14) ◽  
pp. 4488-4493 ◽  
Author(s):  
Stanley D. Dunn ◽  
Varden D. Zadorozny ◽  
Richard G. Tozer ◽  
Linda E. Orr
Keyword(s):  
Escherichia Coli ◽  
Atp Hydrolysis ◽  
F1 Atpase ◽  
Product Release ◽  
Epsilon Subunit

scholarly journals α3β3γ complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites

1999 ◽  
Vol 343 (1) ◽  
pp. 135-138 ◽  
Author(s):  
Toyoki AMANO ◽  
Tadashi MATSUI ◽  
Eiro MUNEYUKI ◽  
Hiroyuki NOJI ◽  
Kiyotaka HARA ◽  
...  
Keyword(s):  
Steady State ◽  
Atp Hydrolysis ◽  
Catalytic Site ◽  
Wild Type ◽  
Thermophilic Bacillus ◽  
F1 Atpase ◽  
Type Complex ◽  
Catalytic Sites ◽  
Phase Activity ◽  
Hydrolysis Activity

Homogeneous preparations of α3β3γ complexes with one, two or three non-competent non-catalytic site(s) were performed as described [Amano, Hisabori, Muneyuki, and Yoshida (1996) J. Biol. Chem. 271, 18128-18133] and their properties were compared with those of the wild-type complex. The ATPase activity of the complex with three non-competent non-catalytic sites decayed rapidly to an inactivated state, as reported previously [Matsui, Muneyuki, Honda, Allison, Dou, and Yoshida (1997) J. Biol. Chem. 272, 8215-8221]. In contrast, the complex with one or two non-competent non-catalytic sites displayed a substantial steady-state phase activity depending on the number of non-competent non-catalytic sites in the complex. This result indicates that one competent non-catalytic site can maintain the continuous catalytic turnover of the enzyme and can potentially relieve all three catalytic sites from inhibition by MgADP-. Furthermore, the results suggest that the interaction between three non-catalytic sites might not be as strong as that between catalytic sites, which are all strictly required for a continuous catalytic turnover.

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