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ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
mechanism of proton conduction through F0, and the catalytic mechanism of F1
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
X-ray structure is compatible with a catalytic mechanism in which all three F1-ATPase catalytic sites must fill with MgATP to initiate steady-state hydrolysis
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
catalytic mechanism of the enzyme complex
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
catalytic mechanism of the enzyme complex
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
structure-function relationship from F1 crystal structure in the stable conformational state, catalytic mechanism, F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state, betaDP is the catalytically active form, overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
ATP synthase uses a unique rotary mechanism to couple ATP synthesis and hydrolysis to transmembrane proton translocation. As part of the synthesis mechanism, the torque of the rotor has to be converted into conformational rearrangements of the catalytic binding sites on the stator to allow synthesis and release of ATP. The gamma subunit of the rotor plays a central role in the energy conversion. The N-terminal helix alone is able to fulfill the function of full-length gamma in ATP synthesis as long as it connects to the rest of the rotor. This connection can occur via the epsilon subunit. No direct contact between epsilon and the gamma ring seems to be required. The epsilon subunit of the rotor exists in two different conformations during ATP synthesis and ATP hydrolysis. Reaction mechanism, overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
model of mechanochemical coupling, overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism and structure-fucntion analysis, overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
Halalkalibacterium halodurans
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
Desulforamulus reducens
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
Alkalihalophilus pseudofirmus
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
substrate modulation of multi-site activity of F1 is due to the substrate binding to the second catalytic site, bi-site catalytic mechanism, effects of Mg2+, overview
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
structure-function relationship from F1 crystal structure in the stable conformational state, catalytic mechanism, F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state, betaDP is the catalytically active form, overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
Alkalihalophilus pseudofirmus OF4
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
Desulforamulus reducens MI-1
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
Halalkalibacterium halodurans C-125
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
reaction mechanism, cytoplasmic pH homeostasis and the problem it creates for protonmotive force-driven ATP synthesis, adaptive mechanisms, comparison of alkaliphiles and neutralophiles, detailed overview
-
-
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
-
-
-
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2'-deoxy-ATP + H2O
2'-deoxy-ADP + phosphate + H+/out
-
-
-
?
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
ADP + phosphate + H+
ATP + H2O
ADP + phosphate + H+/out
ATP + H2O + H+/in
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + Fe2+/in
ADP + phosphate + Fe2+/out
-
the enzyme transports Fe2+ and contributes to the iron uptake into rat heart. The activity of ATPase and ATP synthase may be associated with iron uptake in a different manner, probably via antiport of H+
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
?
ATP + phosphate + H+/in
ADP + phosphate + H+/out
-
the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen
-
r
ATPgammaS + H2O + H+/in
ADP + thiophosphate + H+/out
CTP + H2O + H+/in
CDP + phosphate + H+/out
dATP + H2O + H+/in
dADP + phosphate + H+/out
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
ITP + H2O + H+/in
IDP + phosphate + H+/out
UTP + H2O + H+/in
UDP + phosphate + H+/out
additional information
?
-
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
-
-
r
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis
-
-
r
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ADP + phosphate + H+
ATP + H2O
-
couples the H+-translocation driven by an electrochemical potential of H+ to the synthesis of ATP from ADP and phosphate. ATPase in photosynthetic bacteria and strict aerobes seems to function strictly as the ATP-synthetase of photophosphorylation or oxidative phosphorylation
-
r
ADP + phosphate + H+
ATP + H2O
-
terminal enzyme in oxidative phosphorylation
-
r
ADP + phosphate + H+
ATP + H2O
-
-
-
-
r
ADP + phosphate + H+
ATP + H2O
low rates of ATP synthesis
-
-
?
ADP + phosphate + H+
ATP + H2O
low rates of ATP synthesis
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
nucleotide-induced conformational changes in beta subunits are considered to be the essential driving force for rotational catalysis in F1
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
the ATP synthase beta subunit hinge domain dramatically changes in conformation upon nucleotide binding, overview. The rotation speed of the gamma subunit and the structure of the beta subunit hinge domain are responsible for ATP synthesis activity
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
the enzyme synthesizes ATP at the expense of a proton gradient
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
the enzyme synthesizes ATP at the expense of a proton gradient
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
Thermosynechococcus vestitus
-
the enzyme cannot synthesize ATP in the dark, but may catalyze futile ATP hydrolysis reactions
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
ATP in form of MgATP2-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
ATP in form of MgATP2-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
ADP-analogue ADP-ATTO-647N bind slightly weaker to subunit A than the ATP-analogue ATP-ATTO-647N, binding of different nucleotides cause different secondary structural alterations in this subunit
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Alkalihalophilus pseudofirmus
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Alkalihalophilus pseudofirmus
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Alkalihalophilus pseudofirmus OF4
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Alkalihalophilus pseudofirmus OF4
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
a distinct glutamate side chain, conserved across all c-subunits of F-ATP synthases, plays a prominent role in ion coordination
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
subunit epsilon plays a role in intra-enzymatic energy transfer and is required for coupling of ATP synthesis and hydrolysis to proton pumping, the isolated F1 domain shows reduced ATPase activity compared to the complete enzyme complex F1Fo-ATP synthase involving intramolecular inhibition by the C-terminal subunit epsilon, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the gamma-subunit against the alpha3beta3 ring, betaDP is the catalytically active form
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
ATP hydrolysis is essentially reversible, implying that phosphate is released after the gamma rotation and ADP release, although extremely slow, phosphate release is found at the ATP hydrolysis angle as an uncoupling side reaction, affinity for phosphate is strongly angle dependent, selective ADP binding, overview. Models of phosphate release in chemomechanical coupling of F1
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase synthesizes ATP in the F1 portion when protons flow through Fo to rotate the shaft common to F1 and Fo, Kinetic analysis of ATP synthesis using active proteoliposomes
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the rate enhancement induced by ATP binding upon rotation is greater than that brought about by hydrolysis, suggesting that the ATP binding step contributes more to torque generation than does the hydrolysis step
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase synthesizes ATP in the F1 portion when protons flow through Fo to rotate the shaft common to F1 and Fo, Kinetic analysis of ATP synthesis using active proteoliposomes
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
ATP hydrolysis is essentially reversible, implying that phosphate is released after the gamma rotation and ADP release, although extremely slow, phosphate release is found at the ATP hydrolysis angle as an uncoupling side reaction, affinity for phosphate is strongly angle dependent, selective ADP binding, overview. Models of phosphate release in chemomechanical coupling of F1
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the rate enhancement induced by ATP binding upon rotation is greater than that brought about by hydrolysis, suggesting that the ATP binding step contributes more to torque generation than does the hydrolysis step
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
subunit epsilon plays a role in intra-enzymatic energy transfer and is required for coupling of ATP synthesis and hydrolysis to proton pumping, the isolated F1 domain shows reduced ATPase activity compared to the complete enzyme complex F1Fo-ATP synthase involving intramolecular inhibition by the C-terminal subunit epsilon, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the gamma-subunit against the alpha3beta3 ring, betaDP is the catalytically active form
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
ATP binding is rate limiting at a concentration below 0.002 mM
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1-ATPase is a reversible ATP-driven rotary motor protein. When its rotary shaft is reversely rotated, F1 produces ATP against the chemical potential of ATP hydrolysis, suggesting that F1 modulates the rate constants and equilibriums of catalytic reaction steps depending on the rotary angle of the shaft
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1 is resting in the subunit epsilon-inhibited state, Fo motor must transmit to gamma subunit a torque larger than expected from thermodynamic equilibrium to initiate ATP synthesis, reaction mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the temperature-sensitive reaction is a structural rearrangement of beta subunit before or after ATP binding, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
210232, 210233, 210234, 210237, 210244, 210248, 210250, 210257, 210262, 673318, 684136, 685315, 696051, 698676, 733403, 733516 -
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1Fo-ATPase is a large membrane-bound multisubunit complex that catalyses the synthesis of ATP from ADP and phosphate using a transmembrane proton motive force generated by respiration or photosynthesis as a source of energy, ATP hydrolytic catalysis takes place in its hydrophilic F1 domain
-
-
ir
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the F1 domain of the F1Fo-ATP synthase complex catalyzes hydrolysis of ATP to ADP, when isolated from the Fo domain or in conditions where the proton gradient is absent or inverted, e.g. hypoxia, promoting a spontaneous reverse rotation of the gamma-subunit which may drive a reverse proton flux
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the H+ FoF1-ATP synthase complex of coupling membranes converts the proton-motive force into rotatory mechanical energy to drive ATP synthesis, the IF1 component of the mitochondrial complex is a basic 10 kDa protein, which inhibits the FoF1-ATP hydrolase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
nucleotide binding structure, nucleotide occupancy of the catalytic sites, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
catalytic mechanism of F1-ATPase by structure-function relationship analysis, overview. During hydrolysis of ATP, the rotor turns counterclockwise as viewed from the membrane domain of the intact enzyme in 120 degree steps. Because the rotor is asymmetric, at any moment the three catalytic sites are at different points in the catalytic cycle. One site is devoid of nucleotide and represents a state that has released the products of ATP hydrolysis. A second site has bound the substrate, magnesium. ATP, in a precatalytic state, and in the third site, the substrate is about to undergo hydrolysis
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1-ATPase is a motor protein that converts the free energy of binding of ATP and its hydrolysis products ADP and phosphate into a mechanical force for gamma-subunit rotation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
Desulforamulus reducens
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Desulforamulus reducens
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Desulforamulus reducens MI-1
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Desulforamulus reducens MI-1
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
210228, 210230, 210231, 210234, 210236, 210238, 210242, 210246, 210247, 210248, 210258, 210260, 210262, 210263, 674416, 685326, 734256, 734299 -
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the primary function of the enzyme is H+ pumping for cytoplasmic pH regulation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the side chain at position 28 is part of the ion binding pocket
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the transmembrane domain of subunit b of F1F0 ATP synthase is sufficient for H+-translocating activity together with subunits a and c
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the enzyme complex can pump protons in the reverse direction driven by ATP hydrolysis generating a ion-motive force, the F1 domain, comprising subunits alpha3beta3gammadeltaepsilon and possessing the nucleotide binding site, is responsible for the ATP hydrolysis upon detachment from the Fo domain
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
subunit epsilon plays a role in intra-enzymatic energy transfer and is required for coupling of ATP synthesis and hydrolysis to proton pumping, the isolated F1 domain shows reduced ATPase activity compared to the complete enzyme complex F1Fo-ATP synthase involving intramolecular inhibition by the C-terminal subunit epsilon, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the peripheral EF1, subunits a3b3gde, processes ADP/phosphate or ATP, and the membrane integral EFO, subunits ab2c10, translocates ions
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the FOF1-ATPase is a rotary molecular motor. Driven by ATP-hydrolysis, its central shaft rotates in 80° and 40° steps, interrupted by catalytic and ATP-waiting dwells, structure-function relationship, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
nucleotide binding structure, nucleotide occupancy of the catalytic sites, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the epsilon subunit of FoF1-ATP synthase inhibits the FoF1 ATP hydrolysis activity. The rate-limiting step in ATP synthesis is unaltered by the C-terminal domain of epsilon
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Halalkalibacterium halodurans
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Halalkalibacterium halodurans
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Halalkalibacterium halodurans C-125
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Halalkalibacterium halodurans C-125
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the F1 domain of the F1Fo-ATP synthase complex catalyzes hydrolysis of ATP to ADP, when isolated from the Fo domain or in conditions where the proton gradient isabsent or inverted, e.g. hypoxia, promoting a spontaneous reverse rotation of the gamma-subunit which may drive a reverse proton flux
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
enzyme regulation, especially under salt stress, involving plant hormones, overview. Under salt stress, the accelerated extrusion and vacuolar compartmentalization of Na+ from the cytoplasm by the Na+/H+ antiporter cause lower pH in the cytoplasm, and V-PPase, EC 3.6.1.1, activity might complement the V-ATPase activity increased by the pH change, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the function of the ATP synthase is analyzed in an inverted membrane vesicle system of Escherichia coli DK8
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the function of the ATP synthase is analyzed in an inverted membrane vesicle system of Escherichia coli DK8
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the mitochondrial F1F0 ATP synthase mitochondrial F1F0 ATP synthase is also an ATP hydrolase under ischemic conditions, and is a critical enzyme that works by coupling the proton motive force generated by the electron transport chain via proton transfer through the F0 or proton-pore forming domain of this enzyme to release ATP from the catalyticF1 domain. The enzyme is regulated by calcium, ADP, and inorganic phosphate as well as increased transcription through several pathways. Role of the F1F0 ATPase during myocardial ischemia and reperfusion, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the mitochondrial F1F0 ATP synthase is also an ATP hydrolase under ischemic conditions. A a conformational change in the F1F0 ATPase enzyme occurs when switching from synthase to hydrolase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the binding of ATP and ADP/phosphate on an open site is competitive while that of ADP and phosphate is random. The chemical reaction of ATP hydrolysis takes place in the tight to loose, and vice versa, conformational changing, and is tightly coupled with transmembrane proton transport in Fo by the rotation of rotor. ATP can be reversibly synthesized and hydrolyzed in FoF1-ATPase, reversible reaction pathways of the enzyme F1, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
210233, 210234, 210237, 210248, 210262, 696430, 699252, 710844, 712599, 713383, 718970, 719502 -
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the binding of ATP and ADP/phosphate on an open site is competitive while that of ADP and phosphate is random. The chemical reaction of ATP hydrolysis takes place in the tight to loose, and vice versa, conformational changing, and is tightly coupled with transmembrane proton transport in Fo by the rotation of rotor. ATP can be reversibly synthesized and hydrolyzed in FoF1-ATPase, reversible reaction pathways of the enzyme F1, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
Thermosynechococcus vestitus
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
Thermosynechococcus vestitus
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the enzyme transports protons, not Na+ ions
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATPgammaS + H2O + H+/in
ADP + thiophosphate + H+/out
-
-
-
-
r
ATPgammaS + H2O + H+/in
ADP + thiophosphate + H+/out
-
-
-
-
r
CTP + H2O + H+/in
CDP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
?
CTP + H2O + H+/in
CDP + phosphate + H+/out
-
poorly hydrolyzed
-
?
CTP + H2O + H+/in
CDP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
3.3fold slower reaction compared to ATP hydrolysis
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
3.3fold slower reaction compared to ATP hydrolysis
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
17% of the activity with ATP
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
enzyme shows maximal activity with ITP
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
17% of the activity with ATP
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
-
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
-
poorly hydrolyzed
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
-
3% of the activity with ATP
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
no hydrolysis of UTP nor ADP
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
structure-function relationship of the R84C/E190D/E391C mutant enzyme, overview
-
-
?
additional information
?
-
-
angle dependence of ATP or GTP binding and of hydrolysis, overview. Modulation of the high reversibility of mechanochemical coupling, the kinetics and chemical equilibrium of the individual reaction steps comprising ATP hydrolysis on F1 inevitably in response to the gamma rotation
-
-
?
additional information
?
-
-
angle dependence of ATP or GTP binding and of hydrolysis, overview. Modulation of the high reversibility of mechanochemical coupling, the kinetics and chemical equilibrium of the individual reaction steps comprising ATP hydrolysis on F1 inevitably in response to the gamma rotation
-
-
?
additional information
?
-
-
structure-function relationship of the R84C/E190D/E391C mutant enzyme, overview
-
-
?
additional information
?
-
-
F0 of ATP synthase is a rotary proton channel. Proton efflux and influx through F0 are blocked by cross.link between b and c subunit
-
-
?
additional information
?
-
-
modelling of regulation of FoF1-ATPase activity, overview
-
-
?
additional information
?
-
-
an essential arginine residue R169 of the Fo-alpha subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel, overview
-
-
?
additional information
?
-
-
transduction of the conformation signal between catalytic and noncatalytic sites, linking segments involving e.g. residues are S344, G348 from one segment and S370, S372 from the other segment of the mitochondrial F1 alpha-subunit, interactions, overview
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
other reactions catalyzed by ATPase and its components
-
-
?
additional information
?
-
-
the F1Fo-ATP synthase acts as cell surface receptor for unrelated ligands, it binds angiostatin on endothelial cell surface, regulates ATP surface levels, and modulates endothelial cell proliferation and differentiation, in addition the enzyme complexes enterostatin on brain cells, or apolipoprotein A-I on hepatocytes mediating HDL internalization and playing a regulatory role in lipoprotein metabolism, mechanism, physiological functions, F1-ATPase acts as a natural target for innate cytotoxicity by killer cell and lymphokine-activated killer cells toards certain tumor cells, the bovine F1-ATPase specifically activates Vgamma9Vdelta2 T-cell clones, overview
-
-
?
additional information
?
-
-
cyclophilin D associates to the F0F1-ATP synthase complex in bovine heart mitochondria. The ATP synthase-CyPD interactions have functional consequences on enzyme catalysis and are modulated by phosphate, leading to increased CyPD binding and decreased enzyme activity, and by cyclosporin A, leading to decreased CyPD binding and increased enzyme activity
-
-
?
additional information
?
-
-
F1-ATP synthase beta-subunit binds to the pigment epithelium-derived factor and acts as a cell-surface receptor in retinal cells. PEDF is a ligand for endothelial cell-surface F1Fo-ATP synthase
-
-
?
additional information
?
-
-
structure-function analysis, overview
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
structure-function relationship of the proton conductor F0
-
-
?
additional information
?
-
-
other reactions catalyzed by ATPase and its components
-
-
?
additional information
?
-
-
occupancy of the noncatalytic sites is not required for formation of the high-affinity catalytic site of F1 and has no significant effect on unisite catalysis
-
-
?
additional information
?
-
-
sites around residues 70 and/or between 202 and 212 of the gamma subunit are involved in epsilon subunit binding
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
the F1Fo-ATP synthase acts as cell surface receptor for unrelated ligands, it binds angiostatin on endothelial cell surface, regulates ATP surface levels, and modulates endothelial cell proliferation and differentiation, in addition the enzyme complexes enterostatin on brain cells, or apolipoprotein A-I on hepatocytes mediating HDL internalization and playing a regulatory role in lipoprotein metabolism, mechanism, physiological functions, F1-ATPase acts as a natural target for innate cytotoxicity by killer cell and lymphokine-activated killer cells toards certain tumor cells, overview
-
-
?
additional information
?
-
-
the cell surface F1-ATPase pathway may contribute to the antiapoptotic and proliferative effects mediated by apoA-I and HDLs on endothelial cells. The antiapoptotic and proliferative effects of apoA-I on HUVECs are totally blocked by the F1-ATPase ligands IF1-H49K, angiostatin and anti-F1-ATPase antibody, independently of the scavenger receptor SR-BI and ABCA1, overview
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of tolerance to salt stress, it energizes the the Na+/H+ antiporter NHX by ATP hydrolysis, mechanism modelling, overview
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
H+-ATPase is induced at low pH. This regulation seems to occur at the level of transcription. This agrees with the role of this enzyme in the regulation of the cytoplasmic pH and in the acid tolerance of Oenococcus oeni
-
-
?
additional information
?
-
-
H+-ATPase is induced at low pH. This regulation seems to occur at the level of transcription. This agrees with the role of this enzyme in the regulation of the cytoplasmic pH and in the acid tolerance of Oenococcus oeni
-
-
?
additional information
?
-
H+-ATPase is induced at low pH. This regulation seems to occur at the level of transcription. This agrees with the role of this enzyme in the regulation of the cytoplasmic pH and in the acid tolerance of Oenococcus oeni
-
-
?
additional information
?
-
-
transgenic expression of the Na+/H+ antiporter SsNHX1 from in rice leads to increased V-ATPase activitx and increased salt tolerance in the trangenic plants, SsNHX1 activity is mainly energized by the rice V-ATPase activity, regulation and coordination of gained salt tolerance involves the V-ATPase, , overview
-
-
?
additional information
?
-
-
at steady-state conditions, the F0F1-ATPase hydrolyzes ATP with significant participation of two sites
-
-
?
additional information
?
-
-
the enzyme also performs slight transport of common divalent and trivalent metal ions such as Mg2+, Ca2+, Mn2+, Zn2+, Cu2+, Fe3+, and Al3+
-
-
?
additional information
?
-
-
transduction of the conformation signal between catalytic and noncatalytic sites, linking of catalytic and noncatalytic sites of F1, overview. Linking segments invovle residues Tyr345 with Arg356, Asp352 with Arg171, and Gln172 with Arg356, structures and interactions, overview
-
-
?
additional information
?
-
Gly133 of beta subunit is important for structural stability, Glu222 and Arg293 are important for catalytic cooperativity
-
-
?
additional information
?
-
-
Gly133 of beta subunit is important for structural stability, Glu222 and Arg293 are important for catalytic cooperativity
-
-
?
additional information
?
-
-
other reactions catalyzed by ATPase and its components
-
-
?
additional information
?
-
-
bacterially expressed B subunit from the yeast Saccharomyces cerevisiae binds actin filaments. Actin-binding activity confers on the B subunit of yeast a function that is distinct from its role in the enzymatic activity of the proton pump
-
-
?
additional information
?
-
-
the enzyme B subunit binds purified polymerized actin from rabbit muscle
-
-
?
additional information
?
-
-
F1-ATP synthase beta-subunit binds specifically to the human pigment epithelium-derived factor and acts as a cell-surface receptor in retinal cells. PEDF is a ligand for endothelial cell-surface F1Fo-ATP synthase
-
-
?
additional information
?
-
electron density at the catalytic sites of F1 ATPase in the absence of nucleotides, overview
-
-
?
additional information
?
-
-
electron density at the catalytic sites of F1 ATPase in the absence of nucleotides, overview
-
-
?
additional information
?
-
-
subunit D plays an important role in coupling of proton transport and ATP hydrolysis
-
-
?
additional information
?
-
-
subunit D plays an important role in coupling of proton transport and ATP hydrolysis
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
-
in chlorpoplast ATP synthase, both the N-terminus and C-terminus of the epsilon subunit show importance in regulation of the ATPase activity. The N-terminus of the epsilon subunit is more important for its interaction with gamma and some CF0 subunits, and crucial for the blocking of the proton leakage
-
-
?
additional information
?
-
-
membrane potential changes in dark-adapted leaves after short illumination impulses in dark times, electrochemical proton gradient is induced by a short light-pulse, life-time of the light-induced electrochemical proton gradient, detailed overview
-
-
?
additional information
?
-
upon deprotonation, the conformation of Glu61 is changed to another rotamer and becomes fully exposed to the periphery of the ring. Reprotonation of Glu61 by a conserved arginine in the adjacent alpha subunit returns the carboxylate to its initial conformation, structure of putative proton-binding site at the conserved carboxylate Glu61, structure comparison, modelling, overview
-
-
?
additional information
?
-
-
upon deprotonation, the conformation of Glu61 is changed to another rotamer and becomes fully exposed to the periphery of the ring. Reprotonation of Glu61 by a conserved arginine in the adjacent alpha subunit returns the carboxylate to its initial conformation, structure of putative proton-binding site at the conserved carboxylate Glu61, structure comparison, modelling, overview
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
structure-function relationship of the intrinsic inhibitor subunit epsilon subunit in F1 from photosynthetic organism, overview
-
-
?
additional information
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
ADP + phosphate + H+
ATP + H2O
ADP + phosphate + H+/out
ATP + H2O + H+/in
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
ATP + H2O + cellular protein[side 1]
ADP + phosphate + cellular protein[side 2]
-
-
-
?
ATP + H2O + Fe2+/in
ADP + phosphate + Fe2+/out
-
the enzyme transports Fe2+ and contributes to the iron uptake into rat heart. The activity of ATPase and ATP synthase may be associated with iron uptake in a different manner, probably via antiport of H+
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
ATP + phosphate + H+/in
ADP + phosphate + H+/out
-
the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen
-
r
additional information
?
-
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
-
-
r
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis
-
-
r
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ADP + phosphate + 4 H+[side 2]
ATP + H2O + 4 H+[side 1]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ADP + phosphate + H+
ATP + H2O
-
couples the H+-translocation driven by an electrochemical potential of H+ to the synthesis of ATP from ADP and phosphate. ATPase in photosynthetic bacteria and strict aerobes seems to function strictly as the ATP-synthetase of photophosphorylation or oxidative phosphorylation
-
-
r
ADP + phosphate + H+
ATP + H2O
-
terminal enzyme in oxidative phosphorylation
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
the enzyme synthesizes ATP at the expense of a proton gradient
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
the enzyme synthesizes ATP at the expense of a proton gradient
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
-
-
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
Thermosynechococcus vestitus
-
the enzyme cannot synthesize ATP in the dark, but may catalyze futile ATP hydrolysis reactions
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
the enzyme is a membrane-bound molecular motor that uses proton-motive force to drive the synthesis of ATP from ADP and phosphate. Reverse operation generates proton-motive force via ATP hydrolysis
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
decreasing pH from 8.0 to 7.0 results in reversible inhibition of hydrolytic activity, whereas ATP synthesis activity is not changed
-
-
r
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Alkalihalophilus pseudofirmus
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Alkalihalophilus pseudofirmus OF4
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1Fo-ATPase is a large membrane-bound multisubunit complex that catalyses the synthesis of ATP from ADP and phosphate using a transmembrane proton motive force generated by respiration or photosynthesis as a source of energy, ATP hydrolytic catalysis takes place in its hydrophilic F1 domain
-
-
ir
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the F1 domain of the F1Fo-ATP synthase complex catalyzes hydrolysis of ATP to ADP, when isolated from the Fo domain or in conditions where the proton gradient is absent or inverted, e.g. hypoxia, promoting a spontaneous reverse rotation of the gamma-subunit which may drive a reverse proton flux
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the H+ FoF1-ATP synthase complex of coupling membranes converts the proton-motive force into rotatory mechanical energy to drive ATP synthesis, the IF1 component of the mitochondrial complex is a basic 10 kDa protein, which inhibits the FoF1-ATP hydrolase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1-ATPase is a motor protein that converts the free energy of binding of ATP and its hydrolysis products ADP and phosphate into a mechanical force for gamma-subunit rotation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Desulforamulus reducens
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Desulforamulus reducens MI-1
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the primary function of the enzyme is H+ pumping for cytoplasmic pH regulation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the enzyme complex can pump protons in the reverse direction driven by ATP hydrolysis generating a ion-motive force, the F1 domain, comprising subunits alpha3beta3gammadeltaepsilon and possessing the nucleotide binding site, is responsible for the ATP hydrolysis upon detachment from the Fo domain
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the peripheral EF1, subunits a3b3gde, processes ADP/phosphate or ATP, and the membrane integral EFO, subunits ab2c10, translocates ions
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
FOF1-ATPase uses transmembrane ion flow to drive the synthesis of ATP from ADP and phosphate. Molecular mechanism of proton-based driving force of ATP synthesis, the cooperativity between the chemical reaction sites on the F1 motor, and the stepping of rotation, overview. The electrical rotary nanomotor FO drives the chemical nanomotor F1 by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. F1 can hydrolyse ATP in at least two equivalent reaction sites with alternating activity
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Halalkalibacterium halodurans
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Halalkalibacterium halodurans C-125
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the F1 domain of the F1Fo-ATP synthase complex catalyzes hydrolysis of ATP to ADP, when isolated from the Fo domain or in conditions where the proton gradient isabsent or inverted, e.g. hypoxia, promoting a spontaneous reverse rotation of the gamma-subunit which may drive a reverse proton flux
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
enzyme regulation, especially under salt stress, involving plant hormones, overview. Under salt stress, the accelerated extrusion and vacuolar compartmentalization of Na+ from the cytoplasm by the Na+/H+ antiporter cause lower pH in the cytoplasm, and V-PPase, EC 3.6.1.1, activity might complement the V-ATPase activity increased by the pH change, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the mitochondrial F1F0 ATP synthase mitochondrial F1F0 ATP synthase is also an ATP hydrolase under ischemic conditions, and is a critical enzyme that works by coupling the proton motive force generated by the electron transport chain via proton transfer through the F0 or proton-pore forming domain of this enzyme to release ATP from the catalyticF1 domain. The enzyme is regulated by calcium, ADP, and inorganic phosphate as well as increased transcription through several pathways. Role of the F1F0 ATPase during myocardial ischemia and reperfusion, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
Thermosynechococcus vestitus
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
Thermosynechococcus vestitus
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
additional information
?
-
-
F0 of ATP synthase is a rotary proton channel. Proton efflux and influx through F0 are blocked by cross.link between b and c subunit
-
-
?
additional information
?
-
-
modelling of regulation of FoF1-ATPase activity, overview
-
-
?
additional information
?
-
-
the F1Fo-ATP synthase acts as cell surface receptor for unrelated ligands, it binds angiostatin on endothelial cell surface, regulates ATP surface levels, and modulates endothelial cell proliferation and differentiation, in addition the enzyme complexes enterostatin on brain cells, or apolipoprotein A-I on hepatocytes mediating HDL internalization and playing a regulatory role in lipoprotein metabolism, mechanism, physiological functions, F1-ATPase acts as a natural target for innate cytotoxicity by killer cell and lymphokine-activated killer cells toards certain tumor cells, the bovine F1-ATPase specifically activates Vgamma9Vdelta2 T-cell clones, overview
-
-
?
additional information
?
-
-
cyclophilin D associates to the F0F1-ATP synthase complex in bovine heart mitochondria. The ATP synthase-CyPD interactions have functional consequences on enzyme catalysis and are modulated by phosphate, leading to increased CyPD binding and decreased enzyme activity, and by cyclosporin A, leading to decreased CyPD binding and increased enzyme activity
-
-
?
additional information
?
-
-
F1-ATP synthase beta-subunit binds to the pigment epithelium-derived factor and acts as a cell-surface receptor in retinal cells. PEDF is a ligand for endothelial cell-surface F1Fo-ATP synthase
-
-
?
additional information
?
-
-
the F1Fo-ATP synthase acts as cell surface receptor for unrelated ligands, it binds angiostatin on endothelial cell surface, regulates ATP surface levels, and modulates endothelial cell proliferation and differentiation, in addition the enzyme complexes enterostatin on brain cells, or apolipoprotein A-I on hepatocytes mediating HDL internalization and playing a regulatory role in lipoprotein metabolism, mechanism, physiological functions, F1-ATPase acts as a natural target for innate cytotoxicity by killer cell and lymphokine-activated killer cells toards certain tumor cells, overview
-
-
?
additional information
?
-
-
the cell surface F1-ATPase pathway may contribute to the antiapoptotic and proliferative effects mediated by apoA-I and HDLs on endothelial cells. The antiapoptotic and proliferative effects of apoA-I on HUVECs are totally blocked by the F1-ATPase ligands IF1-H49K, angiostatin and anti-F1-ATPase antibody, independently of the scavenger receptor SR-BI and ABCA1, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of tolerance to salt stress, it energizes the the Na+/H+ antiporter NHX by ATP hydrolysis, mechanism modelling, overview
-
-
?
additional information
?
-
H+-ATPase is induced at low pH. This regulation seems to occur at the level of transcription. This agrees with the role of this enzyme in the regulation of the cytoplasmic pH and in the acid tolerance of Oenococcus oeni
-
-
?
additional information
?
-
-
H+-ATPase is induced at low pH. This regulation seems to occur at the level of transcription. This agrees with the role of this enzyme in the regulation of the cytoplasmic pH and in the acid tolerance of Oenococcus oeni
-
-
?
additional information
?
-
H+-ATPase is induced at low pH. This regulation seems to occur at the level of transcription. This agrees with the role of this enzyme in the regulation of the cytoplasmic pH and in the acid tolerance of Oenococcus oeni
-
-
?
additional information
?
-
-
transgenic expression of the Na+/H+ antiporter SsNHX1 from in rice leads to increased V-ATPase activitx and increased salt tolerance in the trangenic plants, SsNHX1 activity is mainly energized by the rice V-ATPase activity, regulation and coordination of gained salt tolerance involves the V-ATPase, , overview
-
-
?
additional information
?
-
-
bacterially expressed B subunit from the yeast Saccharomyces cerevisiae binds actin filaments. Actin-binding activity confers on the B subunit of yeast a function that is distinct from its role in the enzymatic activity of the proton pump
-
-
?
additional information
?
-
-
F1-ATP synthase beta-subunit binds specifically to the human pigment epithelium-derived factor and acts as a cell-surface receptor in retinal cells. PEDF is a ligand for endothelial cell-surface F1Fo-ATP synthase
-
-
?
additional information
?
-
-
membrane potential changes in dark-adapted leaves after short illumination impulses in dark times, electrochemical proton gradient is induced by a short light-pulse, life-time of the light-induced electrochemical proton gradient, detailed overview
-
-
?
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1,3-dicyclohexyl carbodiimide
-
2-[[4-(trifluoromethoxy)phenyl]hydrazinylidene]propanedinitrile
-
acts as an uncoupler and abolishes ATP synthesis
42-58 IF1 synthetic peptide
-
inhibits both H+ uptake and H+ release of the enzyme complex
-
7-chloro-4-nitrobenz-2-oxa-1,3-diazole
-
i.e. NBD-Cl, MgADP at low concentrations promotes the inhibition, whereas at higher concentrations EcF1 is protected from inhibition, that need to be higher for the mutant betaY331W, than for the wild-type enzyme. In absence of added MgATP, selenite slows down inhibition of EcF1 by 0.2 mM NBD-Cl
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
adenosine-5'-(beta,gamma-imino)-triphosphate
-
inhibits F1 rotation
AlCl3
-
irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP-
ATP
-
free ATP, MgATP2- is the true substrate
ATPase inhibitor factor 1
-
ATPase inhibitory factor 1
-
physiological inhibitor
-
aurovertin B
-
non-selective ATPase inhibitor
BMS-199264
-
a benzopyran analogue, selectively inhibits F1F0 ATP hydrolase activity with no effect on ATP synthase activity, BMS-199264 has no effect on ATP before ischemia, but reduces the decline in ATP during ischemia
cyclophilin D
-
cyclophilin D associates to the FOF1-ATP synthase complex in bovine heart mitochondria. The ATP synthase-cyclophilin D interactions have functional consequences on enzyme catalysis and are modulated by phosphate, leading to increased CyPD binding and decreased enzyme activity, and by cyclosporin A, leading to decreased CyPD binding and increased enzyme activity
-
diphosphate
-
location and properties of diphosphate-binding sites
F1-ATPase inhibitor
-
-
-
Fluorescein 5'-isothiocyanate
iejimalide A
-
a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
iejimalide B
-
a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
IF1-H49K protein
-
the F1-ATpase specific inhibitor inhibits the ATPase activity, the IF1 mutant shows inhibitory activity at neutral pH
-
inhibitor protein IF1
-
F1 in mitochondria is associated with a small regulatory protein, IF1, which inhibits its ATPase activity and the ecto-FOF1 activity, overview
-
intrinsic inhibitory peptide IF1
-
from Saccharomyces cerevisiae, the N-terminal part of the inhibitory peptide IF1 interacts with the central gamma subunit of mitochondrial isolated extrinsic part of ATP synthase in the inhibited complex. Kinetics of inhibition of the isolated and membrane-bound enzymes with IF1 modified in N-terminal extremity, i.e. IF1-Nter, overview. IF1-Nter plays no role in the recognition step but contributes to stabilize the inhibited complex. Its binding to the enzyme is not affected by truncations or fusion with PsaE, a 8 kDa globular-like protein
-
m-chlorophenylhydrazone
-
-
Mn2+
-
1 mM reduces ATPase activity 50% in the presence of 5 mM MgSO4
monensin
70% inhibition at 0.1 mM; 70% inhibition at 0.1 mM; 70% inhibition at 0.1 mM
N,N'-dicyclohexylcarbodiimide
N,N-dicyclohexylcarbodiimide
-
NaCl
-
inhibits ATPase activity
NaF
-
irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP-
NEM
-
modification of the Cys at position 10 with NEM or fluorescein maleimide further reduces the binding affinity of, and the maximal inhibition by the epsilon subunit
Ni2+
-
1 mM reduces ATPase activity 47% in the presence of 5 mM MgSO4
p-Trifluoromethoxyphenylhydrazone
-
diminishes ATP synthesis very effectively at 200 mM
piceatanol
-
an F1 inhibitor, also inhibits Fe2+ uptake
pigment epithelium-derived factor
-
quercetin
-
an F1 inhibitor, also inhibits Fe2+ uptake
regulatory protein IF1
-
the only significant modulator of enzyme activity, 1300-1400 mM of IF1 is predicted to fully inactivate 1000 mM of synthase, both in vivo and in vitro, thus excluding significant binding numbers of non-inhibitory binding sites for IF1 in the F0 sector
-
resveratrol
-
an F1 inhibitor, also inhibits Fe2+ uptake
SidK
-
a protein of Legionella pneumophila, an intracellular pathogen, specifically targets host v-ATPase. SidK interacts via an N-terminal portion with VatA, a key component of the proton pump leading to the inhibition of ATP hydrolysis and proton translocation. SidK inhibits vacuole acidification and impairs the ability of the cells to digest non-pathogenic Escherichia coli
-
Sodium dodecyl sulfate
-
-
sulfate
-
slightly inhibits
Trialkyltin derivatives
-
Tributyltin chloride
80% inhibition at 0.1 mM; 80% inhibition at 0.1 mM; 80% inhibition at 0.1 mM
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
ADP
-
-
ADP
-
F1 strongly binds ADP lapsing into ADP inhibition, which pauses the rotation
ADP
-
inhibition mechanism, overview
ADP
-
negative allosteric effector
ADP
-
incubation prior to assay abolishes Mg2+-ATPase activity of reduced thylakoids, has no effect on Mg2+-ATPase activity of trypsinized thylakoids
ADP
Thermosynechococcus vestitus
-
inhibition of the enzyme causing pauses in the ATP synthesis or hydrolysis, reversible by lauryl dimethylamine-N-oxide
ADP
Thermosynechococcus vestitus
-
-
angiostatin
-
-
-
angiostatin
-
competes with pigment epithelium-derived factor
-
ATPase inhibitor factor 1
-
i.e. IF1, intrinsic peptide inhibitor, up-regulated in human breast, colon and lung carcinomas. The binding of IF1 to beta-F1-ATPase is regulated by the energetic state of mitochondria. siRNA-mediated silencing of IF1 in cells expressing high levels of IF1 triggers the down-regulation of aerobic glycolysis and an increase in the activity of the H+-ATP synthase
-
ATPase inhibitor factor 1
-
i.e. IF1
-
ATPase inhibitor factor 1
-
i.e. IF1
-
Aurovertin
-
-
azide
-
2 mM inhibits 91% ATPase activity
azide
-
inhibits F1 rotation
azide
-
interacts with the beta-phosphate of ADP and with residues in the ADP-binding catalytic subunit, occupying a position between the catalytically essential amino acids beta-Lys-162 in the P loop and the arginine finger residue alpha-Arg-373, tightens the binding of the side chains to the nucleotide, enhancing its affinity and thereby stabilizing the state with bound ADP
bafilomycin A1
-
completely inhibited by less than 50 nM bafilomycin A1
Ca2+
-
-
Ca2+
-
extracellular, inhibits the enzym ein osteoclast membranes, Ca2+ behaves as a negative feedback signal for osteoclast function
Cu2+
-
1 mM reduces ATPase activity 99% in the presence of 5 mM MgSO4
Cu2+
-
Cu2+ affects the FoF1 ATPase directly, inhibits the enzyme, causes conformational changes in the FoF1 ATPase complex, and thereby affects growth of wild-type strain ATCC9790 and of atpD mutant strain MS116, overview
Dicyclohexylcarbodiimide
-
DCCD
Dicyclohexylcarbodiimide
Thermosynechococcus vestitus
-
-
Efrapeptin
-
-
-
Ethidium bromide
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Hg2+
-
-
I2
-
-
IF1 protein
-
the IF1 component of the mitochondrial complex is a basic 10 kDa protein, which inhibits the FoF1-ATP hydrolase activity, and both H+ uptake and H+ release. IF1, and in particular its central 42-58 segment, displays different inhibitory affinity for proton conduction from the F1 to the Fo side and in the opposite direction. Cross-linking of IF1 toF1-a/b subunits inhibits the ATP-driven H+ translocation but enhances H+ conduction in the reverse direction
-
IF1 protein
-
the ability of IF1 to inhibit F1-ATPase activity depends on pH with a better efficiency at pH below 6.5
-
IF1 protein
-
the hydrolytic activity of the mitochondrial F1F0 ATP hydrolase, but not the synthase, is naturally inhibited by an 84 residue, heat-stable protein IF-1, which binds to F1F0 ATP hyrolase at the F1 domain with a 1:1 stoichiometry. In the absence of a proton motive force, IF-1 is a reversible, non-competitive inhibitor of ATPase hydrolase activity and is optimally functional at a pH below 7.0. The mechanism of IF-1 inhibition is via trapping of adenine nucleotides within the catalytic sites of F1
-
Mg2+
-
Ca2+-activated enzyme
Mg2+
-
free Mg+ inhibits, MgATP is the true substrate
Mg2+
-
0.3 mM, 50% inhibition of Ca2+-dependent activity
MgADP-
-
the enzyme is inhibited by tightly binding MgADP- and the inhibited fraction accumulates gradually until a steady state is reached that represents a dynamic equilibrium between active and MgADP-inhibited forms
MgADP-
-
irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after addition of AlCl3 and NaF
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
binds to F0
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
70% inhibition of the purified enzyme, 75% inhibition of the enzyme from mebrane vesicles
N,N'-dicyclohexylcarbodiimide
-
a nonspecific FOF1-ATPase inhibitor, inhibits ATPase activity and also other membrane mechanisms involved in H+ translocation, in a pH-dependent manner in hya mutants, overview
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
incubation of the membranes overnight at 4°C in the presence of 1 mM N,N'-dicyclohexylcarbodiimide results in a residual activity of 18% of the ATP synthesis rate measured with vesicles that are stored under the same conditions without N,N'-dicyclohexylcarbodiimide. Lower concentrations of N,N'-dicyclohexylcarbodiimide and short incubation times have only negligible effects
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%
N-ethylmaleimide
-
-
N-ethylmaleimide
-
a potent V-ATPase inhibitor, causes only a 510% loss of activity if the vesicles are preincubated for 2 h and a concentration of 10 mM is employed
N3-
-
-
N3-
-
inhibits cooperativity but not unisite catalysis in F1-ATPase
nigericin
-
acts as an uncoupler in the presence of valinomycin, and abolishes ATP synthesis
nigericin
-
50% inhibition at 4 mM
nitrate
-
more than 81% inhibition at 1 mM
NO3-
-
-
NO3-
-
50 mM NO3- inhibits 90% of the hydrolytic activity, while H+ transport activity is decreased by 50%
oligomycin
-
binds to F0
oligomycin
-
inhibits ATP hydrolysis
oligomycin
-
non-selective ATPase inhibitor
oligomycin
-
a specific inhibitor of F1Fo ATP synthase, severely blocks transport of iron
peptide IF1
-
the inhibitory effect might be mediated through interaction of IF1 with the betaDELSEED sequence of the F1 domain of the mitochondrial enzyme, the alpha-helical IF1 N-terminus can penetrate into the alpha3beta3-hexamer between alpha and beta subunits, overview
-
peptide IF1
-
a natural inhibitor of the F1-ATPase, which binds at acidic pH, at cell surfaces
-
peptide IF1
-
a natural inhibitor of the F1-ATPase, which binds at acidic pH, at cell surfaces
-
phosphate
-
-
phosphate
-
phosphate in the medium exerted an opposite effect on iron uptake depending on the type of adenosine nucleotide, which is suppressed with ATP, but enhanced with ADP
pigment epithelium-derived factor
-
-
-
pigment epithelium-derived factor
-
competes with angiostatin. Human PEDF significantly reduces the amount of extracellular ATP produced by endothelial cells, in agreement with direct interactions between cell-surface ATP synthase and PEDF, 53% inhibition at 10 nM
-
subunit epsilon
-
subunit epsilon is required for inhibitory activity on F1 ATPase activity, mechanism, subunit epsilon can extend its C-terminus further inside the alpha3beta3-hexamer up to the N-terminus of subunit gamma, which has an anisotropic effect and enhances ATP hydrolysis inhibition to about 80% without affecting ATP synthesis, the C-terminal alpha-helix residues DELSDED are involved in inhibition, overview
-
subunit epsilon
-
subunit epsilon is required for inhibitory activity on F1 ATPase activity, the C-terminal alpha-helix residues DELSEED are involved in inhibition, mechanism, overview
-
Trialkyltin derivatives
-
-
-
Trialkyltin derivatives
-
-
-
Trialkyltin derivatives
-
-
-
Venturicidin
-
-
Venturicidin
-
noncompetitively inhibits ATP synthesis and coupled ATP hydrolysis
Zn2+
-
1 mM reduces ATPase activity 80% in the presence of 5 mM MgSO4
additional information
-
relatively resistant to vanadate, N,N'-dicyclohexylcarbodiimide and nitrate, 1 mM Fe3+, Ca2+ and Na+ do not affect ATPase activity in the presence of 5 mM MgSO4
-
additional information
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
-
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
-
not inhibited by azide or vanadate
-
additional information
-
strong inhibitory effect of the TF1 epsilon subunit on nucleotide binding
-
additional information
-
in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety. Subunit Asa7 plays a role in the sensitivity to oligomycin
-
additional information
-
in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety
-
additional information
-
the epsilon subunit of FoF1-ATP synthase inhibits the FoF1 ATP hydrolysis activity. The inhibitory effect is modulated by the conformation of the C-terminal alpha-helices of epsilon, and the extended but not hairpin-folded state is responsible for inhibition
-
additional information
-
the enzyme is autoinhibited by the subunit epsilon C-terminal domain. Nucleotide hydrolysis is required to form the epsilon-inhibited state
-
additional information
-
the ATP synthase activity is inhibited neither by the F-ATPase inhibitors 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (up to 1 mM) and phlorizin (up to 2 mM) nor by the V-ATPase inhibitor bafilomycin (0.1 mM)
-
additional information
-
both inhibitors, iejimalides A and B, sequentially neutralize the pH of lysosomes, induce S-phase cell-cycle arrest, and trigger apoptosis in MCF-7 cells, overview
-
additional information
tyrosine nitration is a covalent post-translational protein modification associated with various diseases related to oxidative/nitrative stress, that leads to inactivation of the ATPase activity of the enzyme
-
additional information
-
no inhibition of Fe2+ uptake and ATPase activity by ouabain at 0.1 mM, and by ATP at 1 mM
-
additional information
-
inhibitor screening, overview
-
additional information
-
the addition of 0.05 mM acetazolamide has practically no effect on the rate of ATP hydrolysis
-
additional information
-
the FoF1 ATPase epsilon subunit strongly inhibits ATP hydrolysis activity
-
additional information
-
in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety
-
additional information
Thermosynechococcus vestitus
-
ATP synthase contains an intrinsic inhibitor subunit epsilon, that acts as an endogenous inhibitor of chloroplast F1-ATPase, structure-function analysis, overview. Inhibition of ATPase activity by the cyanobacterial epsilon subunit and the chimaeric subunits composed of the N-terminal domain from the cyanobacterium and the C-terminal domain from spinach, overview
-
additional information
Thermosynechococcus vestitus
-
the epsilon subunit of the enzyme inhibits ATP hydrolysis activity, while the global conformational change of the gamma subunit indirectly regulates complex activity by changing both ADP inhibition and epsilon inhibition
-
additional information
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
regulatory protein IF1
additional information
-
modulates changes in activity
-
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evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
Halalkalibacterium halodurans
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
Desulforamulus reducens
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
Alkalihalophilus pseudofirmus
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
evolution
-
among eukaryotes, complex V from Chlamydomonadales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is accompanied by the recruitment of novel polypeptides. Such a massive modification of complex V stator features might have conferred novel properties, including the stabilization of the enzyme dimeric form and the shielding of the proton channel
evolution
-
among eukaryotes, complex V from Chlorococcales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is accompanied by the recruitment of novel polypeptides. Such a massive modification of complex V stator features might have conferred novel properties, including the stabilization of the enzyme dimeric form and the shielding of the proton channel
evolution
-
among eukaryotes, complex V from Sphaeropleales algae (order of chlorophycean class) has an atypical subunit composition of its peripheral stator and dimerization module, with nine subunits of unknown evolutionary origin, i.e. Asa subunits. The loss of canonical components of the complex V stator happened at the root of chlorophycean lineage and is accompanied by the recruitment of novel polypeptides. Such a massive modification of complex V stator features might have conferred novel properties, including the stabilization of the enzyme dimeric form and the shielding of the proton channel
evolution
the general structure and core subunits of the F1FO ATP synthase are highly conserved from bacteria to fungi, plants and animals
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
Alkalihalophilus pseudofirmus OF4
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
Desulforamulus reducens MI-1
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
Halalkalibacterium halodurans C-125
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
evolution
-
ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values of over 10. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient, overview
-
malfunction
-
deletion of the 3'-UTR in the ATP2 gene leads to deficient protein import and reduced ATP synthesis, mtDNA depletion and respiratory dysfunction
malfunction
-
down-regulation of beta-F1-ATPase expression in chronic myeloid leukemia leads to adriamycin resistance. Deletion of IEX-1, a stress-inducible gene that apparently targets IF1 for degradation, results in the inhibition of the ATP synthase activity in vivo. Relevance of mitochondrial dysfunction as a central player of tumorigenesis, mechanisms participating in controlling the content and activity of the H+-ATP synthase, which is a bottleneck component of oxidative phosphorylation, overview
malfunction
-
Escherichia coli FoF1-ATP synthase atp mutant strain DK8 lacks hydrogenase activity during fermentative growth on glucose at pH 7.0, while at pH 5.5 hydrogenase activity is only 20% that of the wild-type
malfunction
-
expression of Atp6p in HeLa cells depleted of the F1 beta subunit. Instead of being translationally downregulated, HeLa cells lacking F1 degrade Atp6p, thereby preventing proton leakage across the inner membrane. Yeast mutants lacking beta subunit have stable aggregated F1 alpha subunit in the mitochondrial matrix
malfunction
-
HeLa cells lacking F1 degrade Saccharomyces cerevisiae Atp6p, thereby preventing proton leakage across the inner membrane. The human alpha subunit is completely degraded in cells deficient in F1 beta subunit. Depletion of the F1 beta subunit in the mutant shbeta-3 HeLa cell line elicits a remarkable decrease of alpha subunit. In MR6DATP1 lacking the F1 alpha subunit, the F1 beta subunit fails to assemble into the F1 oligomer and forms aggregates that resist solubilization by non-denaturing detergents such as lauryl maltoside
malfunction
-
lethal phenotype of the epsilon knock-out mutant
malfunction
-
loss of Asa7 atypical subunit in Chlamydomonas reinhardtii leads to an unstable complex V and increased sensitivity to oligomycin impared to the wild-type
malfunction
-
lysine substitution of the alpha subunit catalytically critical Arg364 residue causes frequent pauses because of severe ADP inhibition, and a slight decrease in ATP binding rate
malfunction
-
the siRNA-mediated downregulation of the beta subunit of the F1Fo-ATPase reduces influenza virion formation and virus growth in cell culture
malfunction
-
virion formation/Budding of Influenza virus particles is reduced in F1beta-depleted cells
malfunction
-
silencing of subunit ATPase Tb2 inhibits cell growth by decreasing the mitochondrial membrane potential in bloodstream form of Trypanosoma brucei. Depletion of subunit ATPase Tb2 does not significantly alter ATP hydrolysis capabilities but affects cell growth, the mitochondrial membrane potential and FoF1-ATPase integrity in dyskinetoplastic Trypanosoma brucei evansi
malfunction
-
lysine substitution of the alpha subunit catalytically critical Arg364 residue causes frequent pauses because of severe ADP inhibition, and a slight decrease in ATP binding rate
-
metabolism
-
F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis. Chloroplast F1-ATPase is subject to redox regulation, whereby ATP hydrolysis activity is regulated by formation and reduction of the disulfide bond located on the gamma-subunit, molecular mechanism, overview
metabolism
-
internal inhibition of ATP hydrolysis activity of F0F1-ATP synthase is very important for cyanobacteria that are exposed to prolonged dark adaptation and, in general, for the survival of photosynthetic organisms in an ever-changing environment
metabolism
-
repression of the bioenergetic function of mitochondria is one of the strategies of the cancer cell in order to ensure its proliferation by diminishing the potential to execute ROS-mediated cell death
metabolism
-
the coupling of conformational cycle to electrochemical gradient is an efficient means of energy transduction and regulation, for ion binding to the membrane domain, known as Fo, is appropriately selective. H+ selectivity is most likely a robust property of all Fo rotors. In H+-coupled rotors, the incorporation of hydrophobic side chains to the binding sites enhances this inherent H+ selectivity. Size restriction may also favor H+ over Na+, but increasing size alone does not confer Na+ selectivity
metabolism
-
in order to synthesize ATP, the enzyme is capable of rotating its central rotor in a reversible manner. In the clockwise direction, it functions as ATP synthase, while in counter clockwise sense it functions as a proton pumping ATPase
metabolism
-
the enzyme energizes the inner mitochondrial membrane by coupling ATP hydrolysis with the exchange of ADP3- for ATP4- by the ATP/ADP carrier
metabolism
-
the enzyme modulates signaling pathways that activate the mitohormetic response, namely ATP, reactive oxygen species, and target of rapamycin
metabolism
the enzyme uses the proton motive force across the bacterial plasma membrane to drive rotation of the central rotor subunits within a stator subunit complex. Through this mechanical rotation, the rotor coordinates three nucleotide binding sites that sequentially catalyze the synthesis of ATP. Moreover, the enzyme can hydrolyze ATP to turn the rotor in the opposite direction and generate proton motive force
physiological function
-
F1-ATPase is a rotary molecular motor in which the gamma-subunit rotates against the alpha3beta3 cylinder. The unitary gamma-rotation is a 120° step comprising 80° and 40° substeps, each of these initiated by ATP binding and ADP release and by ATP hydrolysis and inorganic phosphate release, respectively
physiological function
-
F1Fo-ATP synthase is a key enzyme of oxidative phosphorylation that is localized in the inner membrane of mitochondria. It uses the energy stored in the proton gradient across the inner mitochondrial membrane to catalyze the synthesis of ATP from ADP and phosphate
physiological function
-
FoF1-ATP synthase is an enzyme that is responsible for ATP synthesis during oxidative phosphorylation and photosynthesis. FoF1 is a complex of two rotary motors F1 and Fo, and the ATP synthesis/hydrolysis reaction that is reversibly catalyzed by F1 is coupled with proton transport across membrane-embedded Fo
physiological function
-
FOF1-ATP synthase synthesizes cellular ATP from ADP and inorganic phosphate. The FOF1-ATP synthase is localized in the mitochondria of eukaryotic cells, where it utilizes the electrochemical gradient, established across the inner mitochondrial membrane by oxidative phosphorylation, for the synthesis of ATP from ADP and inorganic phosphate. Recombinant ATP synthase alpha suppresses huntingtin aggregation when transiently overexpressed in SH-SY5Y cells, overview
physiological function
-
FoF1-ATPase/synthase consists of two rotary molecular motors: a water-soluble, ATP-driven F1 motor and a membrane embedded, H+-driven Fo motor. These molecular motors are connected together to couple ATP synthesis/hydrolysis and ion flow.The F1-ATPase hydrolyzes ATP into ADP and inorganic phosphate, and the hydrolysis of one ATP drives discrete 120° rotation of the gammaepsilon subunits relative to the other subunits
physiological function
-
role of the F1Fo ATP synthase in iron transport, and involvement of proton-coupled transport associated with the cgamma subunit
physiological function
-
the aurovertin B-sensitive ATPase activity of ecto-FOF1 is markedly inhibited in cholestatic rats, to about 45% of that from control rats
physiological function
-
the enzyme is an essential machine of the power stations of the cell. In principle, it can operate in either direction, to synthesize ATP at the expense of ion flow, or to drive ion flow while hydrolysing ATP, although this sometimes occurs only in the forward direction
physiological function
-
the enzyme is an essential machine of the power stations of the cell. In principle, it can operate in either direction, to synthesize ATP at the expense of ion flow, or to drive ion flow while hydrolysing ATP, although this sometimes occurs only in the forward direction
physiological function
-
the protons secreted by the enzyme in osteoclast membrane into the closed extracellular compartment are essential for demineralization of calcified bone
physiological function
-
v-ATPase is a multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells
physiological function
-
efficient influenza virion formation requires the ATPase activity of F1Fo-ATPase. Plasma membrane-associated, but not mitochondrial, F1Fo-ATPase, is important for influenza virion formation and budding, and release from cells
physiological function
-
F1-ATPase is an ATP-driven rotary motor protein in which the gamma-subunit rotates against the catalytic stator ring
physiological function
-
FoF1-ATP synthase is the main membrane protein complex of bioenergetic relevance catalyzing ATP synthesis as terminal step in oxidative phosphorylation. Requirement for the FoF1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases Hyd-1 and Hyd-2
physiological function
Na+-dependent F1F0-ATP synthase in the cytoplasmic membrane plays a potential role in salt-stress tolerance
physiological function
-
the functional mechanism of the F1Fo ATP synthase entails a conformational cycle that is coupled to the movement of H+ or Na+ ions across its transmembrane domain, down an electrochemical gradient
physiological function
the hydrophilic F1 component catalyzes ATP formation and protrudes into the matrix, while the hydrophobic FO component channels protons through the membrane and anchors the entire complex to the mitochondrial inner membrane
physiological function
ATP synthase subunit a deletion results in an increased motility phenotype. The amount of membrane-bound ATPase is reduced in the mutants. Deletion or mutation confers faster motility in low concentrations of sodium than in the parental strain and this phenotype is suppressed in the presence of KCN
physiological function
-
F1-ATPase serves as a receptor for a gastrointestinal peptide mediating cell growth
physiological function
-
at the plant vacuole enzyme, the is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
at the plant vacuole, the enzyme is responsible for energization of transport of ions and metabolites, and thus the enzyme is important as a house-keeping and stress response enzyme
physiological function
-
overexpression of subunit VHA-A confers transgenic tobacco seedlings with enhanced vacuole H+-ATPase activity and improved drought tolerance
physiological function
-
the enzyme can support general mitochondrial and cellular functions, working in extremely efficient energy saving reverse mode and flexibly recruiting free radical detoxication and ATP producing / transporting pathways
physiological function
-
the membrane-bound ATPaseTb2 subunit is essential for maintaining normal growth and the mitochondrial membrane potential of dyskinetoplastic cells
physiological function
-
the robust ATP-hydrolyzing activity occurs in ischemia for maintaining the transmembrane proton motive force of mitochondria inner membrane
physiological function
-
F1-ATPase is an ATP-driven rotary motor protein in which the gamma-subunit rotates against the catalytic stator ring
-
additional information
-
Ca2+ facilitates a dynamin- and V-ATPase-dependent endocytosis in association with with an inhibition of the plasma membrane V-ATPase, overview
additional information
-
FOF1-ATP synthase plays a role in neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease
additional information
-
pigment epithelium-derived factor-mediated inhibition of ATP synthase may form part of the biochemical mechanisms by which PEDF exerts its antiangiogenic activity
additional information
-
pigment epithelium-derived factor-mediated inhibition of ATP synthase may form part of the biochemical mechanisms by which PEDF exerts its antiangiogenic activity
additional information
-
the atpD mutant strain MS116 expresses the FoF1 ATPase to the level as wild-type one, but it has significantly lowered H+ efflux and ATPase activity, overview
additional information
-
Asn90 is located in the middle of putative second transmembrane helix and likely to play an important role in H+-translocation
additional information
-
ATP2 mRNA is no Puf3p target and belongs to the class of Puf3-independent mitochondria-localized mRNAs
additional information
-
expression of the catalytic subunit beta-F1-ATPase is tightly regulated at post-transcriptional levels during mammalian development and in the cell cycle. Downregulation of beta-F1-ATPase is a hallmark of most human carcinomas. Role of the ATPase inhibitor factor 1 and of Ras-GAP SH3 binding protein 1, G3BP1, controlling the activity of the H+-ATP synthase and the translation of beta-F1-ATPase mRNA respectively in cancer cells
additional information
-
expression of the catalytic subunit beta-F1-ATPase is tightly regulated at post-transcriptional levels during mammalian development and in the cell cycle. Downregulation of beta-F1-ATPase is a hallmark of most human carcinomas. Role of the ATPase inhibitor factor 1 and of Ras-GAP SH3 binding protein 1, G3BP1, controlling the activity of the H+-ATP synthase and the translation of beta-F1-ATPase mRNA respectively in cancer cells. A trans-acting factor that regulate beta-F1-ATPasemRNA translation, is G3BP1, Ras-GAP SH3 binding protein 1, that interacts with the 3'UTR of beta-mRNA, the interaction specifically represses mRNA translation by preventing its recruitment into active polysomes
additional information
-
F1-ATPase is a water-soluble portion of the FoF1-ATP synthase and an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine at position 364, termed the arginine finger, with stereogeometric similarities with the arginine finger of G-protein-activating proteins. The principal role of the arginine finger is not to mediate cooperativity among the catalytic sites, but to enhance the rate of the ATP cleavage by stabilizing the transition state of ATP hydrolysis
additional information
-
F1-ATPase is the isolated extrinsic part of ATP synthase, the extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
additional information
modular assembly of the F1Fo ATP synthase. F1 precursor proteins are imported and rapidly assembled into both apparently free F1 and F1FO ATP synthase in organello
additional information
-
molecular dynamics simulations and free-energy calculations of ion coordination and transfer in wild-type enzyme and mutant A63S, overview
additional information
NP_393483
the peripheral stalk of the A1A0-ATP synthase is formed by the heterodimeric EH complex and is part of the stator domain, which counteracts the torque of rotational catalysis. The BNT peptide specifically interacts with 26 residues of the ECT1HCT domain
additional information
-
the peripheral stalk of the A1A0-ATP synthase is formed by the heterodimeric EH complex and is part of the stator domain, which counteracts the torque of rotational catalysis. The BNT peptide specifically interacts with 26 residues of the ECT1HCT domain
additional information
-
F1-ATPase is a water-soluble portion of the FoF1-ATP synthase and an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine at position 364, termed the arginine finger, with stereogeometric similarities with the arginine finger of G-protein-activating proteins. The principal role of the arginine finger is not to mediate cooperativity among the catalytic sites, but to enhance the rate of the ATP cleavage by stabilizing the transition state of ATP hydrolysis
-
additional information
-
Asn90 is located in the middle of putative second transmembrane helix and likely to play an important role in H+-translocation
-
additional information
-
the atpD mutant strain MS116 expresses the FoF1 ATPase to the level as wild-type one, but it has significantly lowered H+ efflux and ATPase activity, overview
-
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13000
-
x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
14722
-
x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
14741
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
15000
-
alpha3,beta3,tau1,delta1,epsilon1, 3 * 66000 + 3 * 60200 + 1 * 36300 + 1 * 15000 + 1 * 12000, F1 subunit, SDS-PAGE
15457
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
17000
-
subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
17500
-
x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
19617
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
20621
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
21000
-
alpha3,beta3,gamma1,delta1,epsilon1, 1 * 60000 + 3 * 53000 + 1 * 31000 + 1 * 25000 + 1 * 21000, SDS-PAGE
22880
calculated from sequence
25000
-
alpha3,beta3,gamma1,delta1,epsilon1, 1 * 60000 + 3 * 53000 + 1 * 31000 + 1 * 25000 + 1 * 21000, SDS-PAGE
280000
-
equilibrium sedimentation
31000
-
alpha3,beta3,gamma1,delta1,epsilon1, 1 * 60000 + 3 * 53000 + 1 * 31000 + 1 * 25000 + 1 * 21000, SDS-PAGE
325000
-
equilibrium ultracentrifugation
33000
-
subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
347000
-
F1, sedimentation equilibrium ultracentrifugation
35013
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
360000
-
purified F1-ATP synthase, gel filtration
360000 - 384000
-
equilibrium sedimentation
36300
-
alpha3,beta3,tau1,delta1,epsilon1, 3 * 66000 + 3 * 60200 + 1 * 36300 + 1 * 15000 + 1 * 12000, F1 subunit, SDS-PAGE
379000
-
strain KM, sedimentation equilibrium centrifugation
385000
-
sedimentation equilibrium analysis
47000
-
alpha6,beta6, 6 * 47000 + 6 * 51000, SDS-PAGE
50000
-
subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
51000
-
alpha6,beta6, 6 * 47000 + 6 * 51000, SDS-PAGE
51305
-
x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
51526
-
x * 51526, calculated for beta subunit
51795
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
53000
-
alpha3,beta3,gamma1,delta1,epsilon1, 1 * 60000 + 3 * 53000 + 1 * 31000 + 1 * 25000 + 1 * 21000, SDS-PAGE
54000
-
subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
54271
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
55000
-
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
56000
-
x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
5700
-
subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
59000
-
x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
60200
-
alpha3,beta3,tau1,delta1,epsilon1, 3 * 66000 + 3 * 60200 + 1 * 36300 + 1 * 15000 + 1 * 12000, F1 subunit, SDS-PAGE
62800
-
x * 62800, recombinant His3-tagged subunit A of V1VO ATPase, SDS-PAGE
66009
x * 66009, calculated for alpha subunit
70000
-
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
9700
-
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
12000
-
alpha3,beta3,tau1,delta1,epsilon1, 3 * 66000 + 3 * 60200 + 1 * 36300 + 1 * 15000 + 1 * 12000, F1 subunit, SDS-PAGE
12000
-
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
300000
-
gel filtration
37000
-
x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
37000
-
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
60000
-
alpha3,beta3,gamma1,delta1,epsilon1, 1 * 60000 + 3 * 53000 + 1 * 31000 + 1 * 25000 + 1 * 21000, SDS-PAGE
60000
-
x * 60000, F1-ATP synthase beta-subunit, SDS-PAGE
60000
-
x * 60000, F1-ATP synthase beta-subunit, SDS-PAGE
66000
subunit A, gel filtration
66000
-
alpha3,beta3,tau1,delta1,epsilon1, 3 * 66000 + 3 * 60200 + 1 * 36300 + 1 * 15000 + 1 * 12000, F1 subunit, SDS-PAGE
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dodecamer
-
alpha6,beta6, 6 * 47000 + 6 * 51000, SDS-PAGE
heterodecamer
-
x * 70000 + x * 60000 + x * 44000 + x * 42000 + x * 36000 + x * 32000 + x * 29000 + x * 16000 + x * 13000 + x * 12000, SDS-PAGE
oligomer
-
oligomerization of ATP synthase is critical for the morphology of the inner mitochondrial membrane because it supports the generation of tubular cristae membrane domains, overview. Association of individual F1Fo-ATP synthase complexes is mediated by the membrane-embedded Fo-part. Subunits e, g, k, and i are involved in the stepwise assembly of F1Fo-ATP synthase dimers and oligomers. Subunit i facilitates the incorporation of newly synthesized subunits into ATP synthase complexes, while subunit k stabilizes the dimer. Formation of one dimeric form of ATP synthase is inhibited in the absence of subunit. Detailed overview i
?
x * 16000, proteolipid subunit c of V-ATPase, SDS-PAGE
?
-
x * 16000, proteolipid subunit c of V-ATPase, SDS-PAGE
-
?
-
x * alpha, 52000-53000 + x * beta, 51000 + x * gamma, 40000, SDS-PAGE
?
-
x * 62800, recombinant His3-tagged subunit A of V1VO ATPase, SDS-PAGE
?
-
subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
?
-
x * 60000, F1-ATP synthase beta-subunit, SDS-PAGE
?
-
the calculated molecular masses of the deduced gene products are 22.0 kDa (subunit D), 38.7 kDa (subunit C), 11.6 kDa (subunit E), 52.0 kDa (subunit B), and 64.5 kDa (subunit A). The described operon contains genes in the order D, C, E, B, and A. It contains no gene for the hydrophobic, so-called proteolipid (subunit c, the proton-conducting subunit of the A0 part). This subunit is isolated and purified its molecular mass as deduced by SDS-polyacrylamide gel electrophoresis is 9.7 kDa
?
-
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
?
-
the calculated molecular masses of the deduced gene products are 22.0 kDa (subunit D), 38.7 kDa (subunit C), 11.6 kDa (subunit E), 52.0 kDa (subunit B), and 64.5 kDa (subunit A). The described operon contains genes in the order D, C, E, B, and A. It contains no gene for the hydrophobic, so-called proteolipid (subunit c, the proton-conducting subunit of the A0 part). This subunit is isolated and purified its molecular mass as deduced by SDS-polyacrylamide gel electrophoresis is 9.7 kDa
-
?
-
x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
-
?
-
x * 68500, catalytic subunit A, calculated from amino acid sequence
?
-
x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
?
-
x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
-
?
-
x * 60000, F1-ATP synthase beta-subunit, SDS-PAGE
?
-
x * 100000, subunit a, SDS-PAGE
?
-
x * 100000, subunit a, SDS-PAGE
-
?
-
x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
?
-
x * 51526, calculated for beta subunit
?
x * 66009, calculated for alpha subunit
?
Thermosynechococcus vestitus
-
x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b'-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
?
-
x * 40000, subunit ATPaseTb2, SDS-PAGE
dimer
-
complex V exhibits an increased stability of its dimeric form
dimer
-
complex V exhibits an increased stability of its dimeric form
dimer
-
complex V exhibits an increased stability of its dimeric form
multimer
-
subunit composition of bacterial F1 and Fo is alpha3beta3gammadeltaepsilon and ab2c10-15, respectively, and the gammaepsilonc10-15 complex rotates against the alpha3beta3deltaab2 complex in FoF1. The epsilon subunit has a molecular mass of 14 kDa and a two-domain structure consisting of an N-terminal 10-stranded beta-sandwich and two C-terminal alpha-helices
multimer
-
FOF1-ATP synthase is a multi-subunit protein
multimer
-
the ATP synthase enzymes of chloroplasts is composed of two protein segments, FO and F1, the chloroplast FO1 contains four different polypeptide subunits with a stoichiometry of I1II1III14IV1. The F1 segment contains the catalytic sites for ATP synthesis and hydrolysis. The chloroplast F1 is comprised of five different polypeptide subunits, alpha to epsilon, with a stoichiometry of alpha3beta3gamma1delta1epsilon1
nonamer
-
alpha3,beta3,tau1,delta1,epsilon1, 3 * 66000 + 3 * 60200 + 1 * 36300 + 1 * 15000 + 1 * 12000, F1 subunit, SDS-PAGE
nonamer
-
alpha3,beta3,gamma1,delta1,epsilon1, 1 * 60000 + 3 * 53000 + 1 * 31000 + 1 * 25000 + 1 * 21000, SDS-PAGE
additional information
-
x * F1alpha, 55000 + x * F1beta, 50000, + x * F1gamma, 33000, + x * F1delta, 20000, + x * F1epsilon, 18000, SDS-PAGE of strain NASF-1, x * F1alpha, 55000 + x * F1beta, 50000, + x * F1gamma, 30000, + x * F1delta, 23000, + x * F1epsilon, 14000, SDS-PAGE of strain ATCC33020, x * F1alpha, 55500 + x * F1beta, 50500, + x * F1gamma, 33100, + x * F1delta, 19200, + x * F1epsilon, 15100, sequence analysis of strain NASF-1
additional information
-
secondary structure analysis by circular dichroism spectroscopy shows that subunit A of V1VO ATPase comprises 43% alpha-helix, 25% beta-sheet and 40% random coil content
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
Alkalihalophilus pseudofirmus
subunit organisation model, overview
additional information
Alkalihalophilus pseudofirmus OF4
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
modular assembly of the F1Fo ATP synthase. F1 is an intermediate of assembly of plant F1FO ATP synthase. The catalytic F1 subunit complex alpha3beta3 and FO components subunits (a, c, e, f, g, and A6L (or ATP8)) are connected by a central stalk (including F1 subunits gamma, delta and epsilon) and a peripheral stalk (including OSCP, subunit b, subunit d and F6)
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
four bands alpha, beta, gamma and epsilon in F1 deltasigma with identical molecular mass values as those in the native enzyme, SDS-PAGE
additional information
-
structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
additional information
-
structure analysis F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state
additional information
-
subunit organisation model, overview
additional information
-
F1-ATPase is an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine, termed the arginine finger
additional information
-
F1-ATPase is an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine, termed the arginine finger
-
additional information
-
structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
-
additional information
-
structure analysis F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state
-
additional information
-
four bands alpha, beta, gamma and epsilon in F1 deltasigma with identical molecular mass values as those in the native enzyme, SDS-PAGE
-
additional information
-
subunit organisation model, overview
-
additional information
-
FoF1-ATPase/synthase consists of two rotary molecular motors: a water-soluble, ATP-driven F1 motor and a membrane embedded, H+-driven Fo motor, F1-ATPase is formed by 5 subunits types: alpha3beta3gammadeltaepsilon. F1-ATPase hydrolysis of one ATP drives discrete 120° rotation of the gammaepsilon subunits relative to the other subunits, structure analysis, overview. Strong inhibitory effect of the TF1 epsilon subunit on nucleotide binding, the presence of the extended epsilon subunit will change the rotational potential profile of gamma and epsilon subunits by changing the free energy difference between the nucleotide binding to high and low affinity binding sites. This may directly relate to the role of the epsilon subunit in efficient ATP synthesis under certain conditions
additional information
-
transduction of the conformation signal between catalytic and noncatalytic sites, overview
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
the enzyme is composed of two structurally and functionally distinct sectors, F1 and F0. F1 shows ATPase activity, Fo mediates H+ translocation across the membrane
additional information
-
-
additional information
-
-
additional information
-
the whole ATPase, 468000 Da, contains one F1 sector, one oligomycin-sensitivity confering protein, and one chain each of four membrane sector subunits, F1 contains 5 tightly bound subunits
additional information
-
subunit composition
additional information
-
molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
-
the gamma-subunit of the enzyme complex rotates and turns into the F1 domain, when protons cross the membrane, generating conformation changes in the alpha- and beta-chains, which are responsible for catalysis of ATP synthesis from ADP and phosphate, a reserve gamma-subunit rotation reverses the proton flux and promotes ATP hydrolysis, subunit structure of the F1Fo-ATP synthase complex, overview
additional information
-
F1 is a rotary chemical motor and generator, structure modelling, overview
additional information
structure analysis of conformations of the betaE-, betaTP- and betaDP-subunits in ground-state structure of F1-ATPase, catalytic sites and conformational changes, overview
additional information
-
structure analysis of conformations of the betaE-, betaTP- and betaDP-subunits in ground-state structure of F1-ATPase, catalytic sites and conformational changes, overview
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
Desulforamulus reducens
-
subunit organisation model, overview
additional information
Desulforamulus reducens MI-1
-
subunit organisation model, overview
-
additional information
-
size of major subunits
additional information
-
x * F1alpha, 55259 + x * F1beta, 50117, + x * F1gamma, 19303, + x * F1epsilon, 14914, + x * F0a, 30275, + x * F0b, 17244, + x * F0c, 8246
additional information
-
size of major subunits
additional information
-
structure-function relationship of the proton conductor F0
additional information
-
F1 is composed of five types of subunits, F0 is composed of three types of subunits, ratio of F1 subunits: alpha3beta3gamma1delta1epsilon1, ratio of F0 subunits: chi2psi2omega10
additional information
-
the stoichiometry of subunits in F1 is alpha3beta3gamma1delta1epsilon1, the stoichiometry of F0 subunits is not yet settled
additional information
-
subunit composition
additional information
-
structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the N-terminal beta-sandwich of the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
additional information
-
homology modeling of the immobilized enzyme, structure, overview
additional information
-
F1 is a rotary chemical motor and generator, structure modelling, overview
additional information
-
the ATP synthase beta subunit hinge domain dramatically changes in conformation upon nucleotide binding, structure and modelling, overview
additional information
-
the epsilon subunit has a molecular mass of 14 kDa and a two-domain structure consisting of an N-terminal 10-stranded beta-sandwich and two C-terminal alpha-helices
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
Halalkalibacterium halodurans
-
subunit organisation model, overview
additional information
Halalkalibacterium halodurans C-125
-
subunit organisation model, overview
-
additional information
-
the gamma-subunit of the enzyme complex rotates and turns into the F1 domain, when protons cross the membrane, generating conformation changes in the alpha- and beta-chains, which are responsible for catalysis of ATP synthesis from ADP and phosphate, a reserve gamma-subunit rotation reverses the proton flux and promotes ATP hydrolysis, subunit structure of the F1Fo-ATP synthase complex, overview
additional information
-
beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
additional information
-
size of major subunits
additional information
-
molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
additional information
-
subunit organisation model, overview
-
additional information
-
size of major subunits
additional information
-
size of major subunits
-
additional information
-
-
additional information
-
the whole ATPase, 468000 Da, contains one F1 sector, one oligomycin-sensitivity confering protein, and one chain each of four membrane sector subunits, F1 contains 5 tightly bound subunits
additional information
-
molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
three-dimensional structures of wild-type and mutant beta-subunits, overview
additional information
-
beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
additional information
-
transduction of the conformation signal between catalytic and noncatalytic sites, linking of catalytic and noncatalytic sites of F1, overview
additional information
-
-
additional information
-
-
additional information
-
subunit composition
additional information
-
molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
structure analysis, overview
additional information
-
structure analysis, overview
additional information
-
subunits alpha, beta, gamma, delta and sigma of the purified chimeric enzyme, with the stoichiometry of 3:3:1:1:1, SDS-PAGE
additional information
-
V-ATPase consists of a cytoplasmic domain V1 and a transmembrane domain V0. Both domains contain several subunits. The V0 transmembrane domain consists of subunits a, c, c', c'' and d. Proton translocation takes place at the interface of subunit a and the rotating c, c', and c'' subunits. NMR structure determination, 3D structure of a peptide derived from the putative transmembrane segment 7 of subunit a from H+-V-ATPase determined by solution state NMR in SDS solution. A stable helix is formed from L736 up to and including Q745, the lumenal half of the putative TM7. The helical region extends well beyond A738. The secondary structure of the peptide depends on the pH and the type of detergent used, overview
additional information
-
the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Dimerization of ATP synthase complexes is a prerequisite for the generation of larger oligomers that promote membrane bending and formation of tubular cristae membranes. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers. Subunits e and g sequentially assemble with monomeric ATP synthase to form a dimerization-competent primed monomer, overview
additional information
-
beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
additional information
-
subunits alpha, beta, gamma, delta and sigma of the purified chimeric enzyme, with the stoichiometry of 3:3:1:1:1, SDS-PAGE
-
additional information
-
subunit composition
additional information
-
molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
-
in chlorpoplast ATP synthase, both the N-terminus and C-terminus of the epsilon subunit show importance in regulation of the ATPase activity. The N-terminus of the epsilon subunit is more important for its interaction with gamma and some CF0 subunits, and crucial for the blocking of the proton leakage
additional information
structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase, overview
additional information
-
structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase, overview
additional information
-
comparison of amino acid sequence with alpha subunit and with alpha and beta subunits of Escherichia coli F1-ATPase
additional information
comparison of amino acid sequence with alpha and beta subunits of Escherichia coli Fl-ATPase. Protein shows cross-reactivity with yeast vacuolar H+-ATPase
additional information
-
interaction between delta and epsilon subunits
additional information
-
the tryptophan residue, located within the N-terminal region of the epsilon subunit is involved in deltaepsilon interaction
additional information
Thermosynechococcus vestitus
-
structure-function relationship of the intrinsic inhibitor subunit epsilon subunit in F1 from photosynthetic organism, NMR structure of the epsilon subunits, wild-type and mrecombinant/chimeric, overview. Analysis of the flexibility of the C-terminal domains using molecular dynamics simulations, overview
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
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9 subunits as calculated from DNA sequence
additional information
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9 subunits as calculated from DNA sequence
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A63S
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site-directed mutagenesis, mutation in the c15 rotor reduces its H+ selectivity against Na+, ion coordination and transfer in wild-type enzyme compared to the wild-type enzyme
S66A
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site-directed mutagenesis, the mutation in the c11 rotor ring increases its proton-binding propensity, consistent with the impaired Na+ binding capacity
S66A/T67L
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site-directed mutagenesis, the double mutant is in its sequence composition identical to the wild-type c15 rotor, and accordingly it is very highly H+ selective
C193S
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alpha(His6 at N terminus/C193S)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
C193S/R364K
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alpha(His6 at N terminus/C193S/R364K)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
D112A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
E190A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
E190Q
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
K164A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
N173A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant retains full activity compared to the wild-type enzyme
N90A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
Q217A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
R169A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
R364A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
R364K
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alpha-subunit catalytic arginine finger mutant, the mutant shows a 350fold longer catalytic pause than the wild-type enzyme, but highly unidirectional rotation with a coupling ratio of 3 ATPs/turn, the same as wild-type, suggesting that cooperative torque generation by the 3 beta-subunits is not impaired. The alphaR364K mutation causes severe ADP inhibition of TF1
R84C/E190D/E391C
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incorporating of a single copy of the mutant beta-subunit to construct the chimera F1, alpha3beta2beta(E190D/E391C)gamma(R84C) which shows slowed ATP hydrolysis
C193S
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alpha(His6 at N terminus/C193S)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
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C193S/R364K
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alpha(His6 at N terminus/C193S/R364K)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
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D112A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
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E190A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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E190Q
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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K164A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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N173A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant retains full activity compared to the wild-type enzyme
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N90A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
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R169A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
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R364A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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R364K
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alpha-subunit catalytic arginine finger mutant, the mutant shows a 350fold longer catalytic pause than the wild-type enzyme, but highly unidirectional rotation with a coupling ratio of 3 ATPs/turn, the same as wild-type, suggesting that cooperative torque generation by the 3 beta-subunits is not impaired. The alphaR364K mutation causes severe ADP inhibition of TF1
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R84C/E190D/E391C
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incorporating of a single copy of the mutant beta-subunit to construct the chimera F1, alpha3beta2beta(E190D/E391C)gamma(R84C) which shows slowed ATP hydrolysis
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alphaC193S
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site-directed mutagenesis, the betaN-terminal His10-tagged mutant is constructed for bulk ATPase assays
alphaC193S/gammaS108C/I211C
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site-directed mutagenesis
alphaF244C
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the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme
alphaG351D
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaR169A
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thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1
alphaR169E
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thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1
alphaR169G/Q217R
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substitutions in the gamma subunit of Fo, the mutation blocks the passive proton translocation
alphaR169X
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thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation
alphaR304C
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the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme
alphaS347F
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaS373F
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaS375F
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaW463F/betaY341W
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site-directed mutagenesis,
alphaY300C
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the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme
betaE190D
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site-directed mutagenesis, mutation of the beta subunit of F1 mutant alphaC193S/gammaS108C/I211C, the mutant shows a clear pause of the temperature-sensitive reaction below 18°C, the catalytic state of the temperature-sensitive reaction in rotation of the hybrid F1, carrying a single copy of betaE190D is observed at 18°C
gammaE56Q
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substitution of Glu56 in the gamma subunit of Fo, the mutation blocks the passive proton translocation
gammaS107C/E165C
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site-directed mutagenesis, the alphaN-terminal His6-tagged mutant is constructed for single molecule manipulation
D262C
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modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
D262H
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modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
D262T
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modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
E197C
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modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3
E197D
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modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3
E197S
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modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3
aR210A/aN214R
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site-directed mutagenesis, the subunit a mutant supports proton conduction onyl through EF1-depleted EFo, but not in EfoEF1, nor ATP-driven proton pumping
betaM159A
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homology modeling shows a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaS174F, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network suppressing the ATPase activity as well as subunit rotation of betaS174F
betaM159I
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homology modeling shows a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaS174F, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network suppressing the ATPase activity as well as subunit rotation of betaS174F
betaS174F
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the F1 beta subunit mutation in the hinge domain lowers the gamma subunit rotation speed, and thus decreases the ATPase activity. Homology modeling shows that the amino acid replacement induces a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaPhe174, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network
betaY331W
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the F1 beta subunit mutant shows higher sensitivity to Mg2+ increasing the inhibitory potency of 7-chloro-4-nitrobenz-2-oxa-1,3-diazole
cD61N/cM65D
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site-directed mutagenesis, the subunit c mutant grows on succinate, retains the ability to synthesize ATP, and supports passive proton conduction, but not ATP hydrolysis-driven proton pumping, overview
D61G
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growth on succinate is abolished, reduced ATPase activity
E196L
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the mutation decreases ATP synthase activity 15fold
E196Q
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the mutation decreases ATP synthase activity 4.7fold
I28D
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growth on succinate is reduced to 25% of the wild-type value,reduced ATPase activity
I28D/D61G
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growth on succinate is abolished, reduced ATPase activity
I28E
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reduced ATPase activity
I28E/D61G
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growth on succinate is abolished, reduced ATPase activity
M138C
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modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit
R50L
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the mutation decreases ATP synthase activity 11fold
S10C
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modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit
S65C
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modification of epsilon-subunit, increases inhibition of ECF1 by the epsilon subunit
K212Q
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site-directed mutagenesis for generation of mutation F1betaK212Q
F446I
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the mutation in the alpha subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
G419D
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the mutation in the beta subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
F446I
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the mutation in the alpha subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
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G419D
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the mutation in the beta subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
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R563A
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mutation in the a subunit leads to total loss of ATP synthesis activity
R563A/R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
R563K
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mutation in the a subunit leads to total loss of ATP synthesis activity
R563K/R625K
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mutation in the a subunit leads to total loss of ATP synthesis activity
R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
R625K
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mutation in the a subunit, almost 50% of the ATP synthesis activity is retained compared to the wild type enzyme
R563A
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R563A/R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R563K
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R563K/R625K
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
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betaY345F
site-directed mutagenesis, the mutant shows 72% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
betaY345F/Y368F
site-directed mutagenesis, the mutant shows 99% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
betaY368F
site-directed mutagenesis, the mutant shows 46% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
K30C/A276C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
K30C/R278C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
V31C/A276C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
V31C/R278C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
A49G/L87S/R246K/N268Y/V312F
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the mutant is resistant towards zinc
A49T/R60S/W83R/Q132H/V163I/H236N/L296M/T338A
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the mutant is resistant towards zinc
A49V/K362N/Q379R/I393V
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the mutant is resistant towards zinc
D205V/D401Y/N415D
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the mutant is resistant towards zinc
D218V
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the mutant shows 85% of wild type ATPase activity
D249G
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the mutant shows 64% of wild type ATPase activity
D46E/F50L/S198R/D217V/Y238F/K298E/T345A/T405M/L418P
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the mutant is resistant towards zinc
E127V/A168T/L314Q/H344Y/H351Q
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the mutant is resistant towards zinc
E220V
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the mutant shows 73% of wild type ATPase activity
E222K
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
E76V/A79P/N164D/E340D/Q341K/H344Y/I403V
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the mutant is resistant towards zinc
F50L/Q152L/F203L/L259S/E409D
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the mutant is resistant towards zinc
G133D
modification of beta-subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
G227D
modification of beta-subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
G80D
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the mutant shows 90% of wild type ATPase activity
G80D/E220V
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the mutant shows 50% of wild type ATPase activity
G80D/E220V/M221V
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the mutant shows 10% of wild type ATPase activity
G80D/K209E
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the double mutant shows increased coupling efficiency of proton transport and ATPase activity
H88L/I193S/Q209H/V303A/D337Y/I417N
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the mutant is resistant towards zinc
H88L/Q150L/W257L/I304L/T324A
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the mutant is resistant towards zinc
I188N
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the mutant shows 62% of wild type ATPase activity
I188N/I173N/A232T
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the mutant shows 20% of wild type ATPase activity
I188N/R198G
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the mutant shows 15% of wild type ATPase activity
I86F
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the mutant is resistant towards zinc
I86N/G212D
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the mutant is resistant towards zinc
K209E
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the mutant shows 110% of wild type ATPase activity
K210E
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the mutant shows 95% of wild type ATPase activity
K210E/D218V
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the mutant shows 42% of wild type ATPase activity
L149V
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the mutant shows wild type ATPase activity
L149V/D249G
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the mutant shows 55% of wild type ATPase activity
L149V/E182D/D249G
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the mutant shows 35% of wild type ATPase activity
L43P/K121R
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the mutant is resistant towards zinc
L47S/D146Y/Q379R
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the mutant is resistant towards zinc
N100I
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the mutant shows 60% of wild type ATPase activity
N117S/Q152L/L276M/F414S
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the mutant is resistant towards zinc
N56T/P110H/I176V/L307I/N372D/N415D
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the mutant is resistant towards zinc
N72I/N117S/I329M/N415D
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the mutant is resistant towards zinc
P179L
modification of beta subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
P179S
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the mutant shows 60% of wild type ATPase activity
Q98H/K299R/K310N/H351R/K362N/Q379K
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the mutant is resistant towards zinc
R198G
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the mutant shows 96% of wild type ATPase activity
R293K
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
R59G/L218I/N415D
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the mutant is resistant towards zinc
R735A
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735C
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735E
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735K
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the mutant, although completely inactive for proton transport, retains 24% of wild type ATPase activity
R735L
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735N
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735Q
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R762A
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the mutant retains full wild type ATPase activity and about 90% of wild type proton transport activity
R762K
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the mutant retains about 80% of wild type ATPase activity and about 80% of wild type proton transport activity
R762L
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the mutant retains about 75% of wild type ATPase activity and about 85% of wild type proton transport activity
R799A
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the mutant is almost totally devoid of proton transport and ATPase activity
R799K
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the mutant, which is almost completely inactive for proton transport, retains about 10% of wild type ATPase activity
R799L
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the mutant is totally devoid of proton transport and ATPase activity
T124S/T219A/I417N
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the mutant is resistant towards zinc
V104E
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the mutant shows wild type ATPase activity
V71D
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the mutant shows 30% of wild type ATPase activity
V71D/E220V/M221V
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the mutant shows 7% of wild type ATPase activity
D218V
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the mutant shows 85% of wild type ATPase activity
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D249G
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the mutant shows 64% of wild type ATPase activity
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G80D
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the mutant shows 90% of wild type ATPase activity
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K210E
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the mutant shows 95% of wild type ATPase activity
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P179S
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the mutant shows 60% of wild type ATPase activity
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R735E
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
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R735K
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the mutant, although completely inactive for proton transport, retains 24% of wild type ATPase activity
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R735N
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
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R735Q
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
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R762A
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the mutant retains full wild type ATPase activity and about 90% of wild type proton transport activity
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A49G/L87S/R246K/N268Y/V312F
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the mutant is resistant towards zinc
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E127V/A168T/L314Q/H344Y/H351Q
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the mutant is resistant towards zinc
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I86F
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the mutant is resistant towards zinc
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L43P/K121R
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the mutant is resistant towards zinc
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Q98H/K299R/K310N/H351R/K362N/Q379K
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the mutant is resistant towards zinc
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C163V
the Walker A motif mutant exhibits a similar rate of ATP hydrolysis to the wild type enzyme
D249E
the mutation leads to abrogation of the ATPase activity
D308A
the mutant shows reduced activity compared to the wild type enzyme
D310A
the mutant shows reduced activity compared to the wild type enzyme
D313A
the mutation leads to abrogation of the ATPase activity
E307A
the mutant shows reduced activity compared to the wild type enzyme
F167A
the mutant shows reduced activity compared to the wild type enzyme
F311A
the mutant shows reduced activity compared to the wild type enzyme
K165A
the mutation leads to abrogation of the ATPase activity
L305A
the mutation leads to abrogation of the ATPase activity
L305D
the mutation leads to abrogation of the ATPase activity
L305I
the mutation leads to abrogation of the ATPase activity
L306A
the mutant shows reduced activity compared to the wild type enzyme
R350A
the mutation leads to abrogation of the ATPase activity
epsilonC6S
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mutant inhibits ATPase activita as potently as the epsilon-wild-type
epsilonDELTAC10
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mutant loses more than 80% of the inhibitory activity towards soluble ATPase
epsilonDELTAC6
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mutant loses 40% of the inhibitory activity towards soluble ATPase
epsilonDELTAC7
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mutant loses about 70% of the inhibitory activity towards soluble ATPase
epsilonDELTAC8
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mutant loses about 70% of the inhibitory activity towards soluble ATPase
epsilonDELTAC9
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mutant loses about 70% of the inhibitory activity towards soluble ATPase
epsilonDELTAN1
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deletion has only marginal effect on the maximum ATPase-inhibitory activity
epsilonDELTAN2
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deletion has only marginal effect on the maximum ATPase-inhibitory activity
epsilonDELTAN3
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mutation decreases its inhibitory activity towards ATPase activity significantly
epsilonDELTAN4
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mutant loses most of the inhibitory activity towards ATPase in solution, 45% loss of inhibitory activity on membrane-bound ATPase, interaction with gamma subunits is lowered
epsilonDELTAN5
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mutant loses most of the inhibitory activity towards ATPase in solution, 50% loss of inhibitorty activity on membrane-bound ATPase, interaction with gamma subunits is lowered
A28C/L267C
Thermosynechococcus vestitus
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the mutant shows strongly reduced activity compared to the wild type enzyme
A35C/A264C
Thermosynechococcus vestitus
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the mutant shows increased ATP hydrolysis activity compared to the wild type enzyme
V32C/A268C
Thermosynechococcus vestitus
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the mutant shows by about 4fold increased ATP hydrolysis activity compared to the wild type enzyme
E190D
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the mutation in the beta-subunit reduces the ATP hydrolysis
E190D
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reversibility of ATPgammaS hydrolysis and synthesis on F1(betaE190D) , overview
E190D
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reversibility of ATPgammaS hydrolysis and synthesis on F1(betaE190D) , overview
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E190D
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the mutation in the beta-subunit reduces the ATP hydrolysis
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M221V
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the mutant shows 50% of wild type ATPase activity
M221V
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the mutation leads to significant uncoupling of proton transport and ATPase activity
V71D/E220V
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the mutant shows 20% of wild type ATPase activity
V71D/E220V
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the mutations lead to significant uncoupling of proton transport and ATPase activity
V39C/A264C
Thermosynechococcus vestitus
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the mutant shows by about 2.5fold increased ATP hydrolysis activity compared to the wild type enzyme
V39C/A264C
Thermosynechococcus vestitus
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the mutant shows greatly increased ATP hydrolysis activity compared to the wild type enzyme
additional information
Alkalihalophilus pseudofirmus
polar deletion of atpI, atpZ or a double atpIZ deletion result in a defect in nonfermentative growth at pH 7.5 that is especially pronounced at suboptimal Mg2+ concentration
additional information
Alkalihalophilus pseudofirmus OF4
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polar deletion of atpI, atpZ or a double atpIZ deletion result in a defect in nonfermentative growth at pH 7.5 that is especially pronounced at suboptimal Mg2+ concentration
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additional information
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subunit beta adopts a different conformation during ATP synthesis in a mutant lacking the C-terminal domain of subunit epsilon, mutation of subunit epsilon C-terminal alpha-helix residues DELSDED leads to highly decreased inhibitory activity of subunit epsilon on ATPase activity, overview
additional information
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construction of a F1Fo mutant lacking the alpha-subunit, F1FoDELTAa, the alpha-subunit produced by the in vitro protease-free protein synthesis system is integrated into a preformed Fo a-less F1Fo complex in Escherichia coli membrane vesicles and liposomes. The resulting F1Fo has a H+-coupled ATP synthesis/hydrolysis activity that is approximately half that of the native F1Fo
additional information
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generation of a mutant TFoF1 lacking an inhibitory segment of the epsilon-subunit, preparation of active proteoliposomes and for kinetic analysis of ATP synthesis, overview
additional information
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preparation of hybrid F1, alpha(C193S)3beta3gamma(S108C/I211C) subcomplex, of a hybrid F1 that carries a single alpha(R364K) subunit and 2 wild-type alpha subunits: F1(1 x alphaR364K), and of monomer alpha(His6 at N terminus/C193S/R364K) and of hybrid F1 containing one alpha(R364K), alpha(His6 at N terminus/C193S/R364K)alpha(C193S)2beta3gamma(S108C/I211C), termed F1(1xalphaR364K), the mutants are affected in rotation and hydrolysis activities, phenotypes, overview
additional information
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generation of a mutant TFoF1 lacking an inhibitory segment of the epsilon-subunit, preparation of active proteoliposomes and for kinetic analysis of ATP synthesis, overview
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additional information
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preparation of hybrid F1, alpha(C193S)3beta3gamma(S108C/I211C) subcomplex, of a hybrid F1 that carries a single alpha(R364K) subunit and 2 wild-type alpha subunits: F1(1 x alphaR364K), and of monomer alpha(His6 at N terminus/C193S/R364K) and of hybrid F1 containing one alpha(R364K), alpha(His6 at N terminus/C193S/R364K)alpha(C193S)2beta3gamma(S108C/I211C), termed F1(1xalphaR364K), the mutants are affected in rotation and hydrolysis activities, phenotypes, overview
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additional information
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subunit beta adopts a different conformation during ATP synthesis in a mutant lacking the C-terminal domain of subunit epsilon, mutation of subunit epsilon C-terminal alpha-helix residues DELSDED leads to highly decreased inhibitory activity of subunit epsilon on ATPase activity, overview
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additional information
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construction of a F1Fo mutant lacking the alpha-subunit, F1FoDELTAa, the alpha-subunit produced by the in vitro protease-free protein synthesis system is integrated into a preformed Fo a-less F1Fo complex in Escherichia coli membrane vesicles and liposomes. The resulting F1Fo has a H+-coupled ATP synthesis/hydrolysis activity that is approximately half that of the native F1Fo
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additional information
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modification of the Cys at position 10 with NEM or fluorescein maleimide further reduces the binding affinity of, and the maximal inhibition by, the epsilon subunit
additional information
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mutation of the subunits alpha, beta, gamma and delta and epsilon, mutations of the F0 subunit
additional information
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(alpha V371C)3(beta R337C)3 gamma double mutant, steady state ATPase activity is 30% of that of the wild-type
additional information
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single cysteine mutations of subunit b expressed from Escherichia coli strain JM109
additional information
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deletion of 8-20 amino acid residues from the N-terminus of subunit gamma leads to decreased inhibitory effect of subunit epsilon, subunit gamma adopts a different conformation in a mutant lacking subunit epsilon and showing loss of activity, mutation of the acidic residues in the betaDELSEED motif to alanines leads to highly decreased inhibitory activity of subunit epsilon on ATPase activity, while exchange of DELSEED to DCLSEED increases ATPase activity, overview
additional information
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His-tagged enzyme immobilization on a glass support and labeling with biotinylated, fluorescently labeled F-actin by engineered Strep tags via streptactin/biotin
additional information
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generation of a EFoF1 mutant lacking the C-terminal domain of the epsilon subunit, the mutant shows severalfold lower turnover numbers and higher Michaelis constants compared to the wild-type enzyme in ATP synthesis driven by acid-base transition, overview. The dependence of the activities of FoF1 wild-type and FoF1 DELTAepsilon on various combinations of DELTApH and DELTAPsi is similar
additional information
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single cysteine mutations of subunit b expressed from Escherichia coli strain JM109
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additional information
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siRNA-mediated downregulation of the beta subunit of the F1Fo-ATPase
additional information
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hybrid vacuolar H+-ATPase containing the mouse testis-specific E1 isoform and yeast subunits shows a defective assembly, reversible defect of the hybrid V-ATPase. Glucose depletion, known to dissociate V1 from Vo in yeast, has only a slight effect on the hybrid at acidic pH. The domain between Lys26 and Val83 of E1, which contains eight residues not conserved between E1 and E2, is responsible for the unique properties of the hybrid, while the E2 domain in E2/VMA4-2 chimera corresponding to between Lys26 and Val83 of E1 has no effect on the assembly of the V-ATPase. The mutant shows a temperature-sensitive defect
additional information
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pairs of cysteine residues were introduced into the twisted N- and C-terminal helices of the gamma subunit of the chloroplast F1-ATPase to test, via disulfide cross-linking, potential inter-helical movements involved in catalysis of ATP hydrolysis. Significant disulfide formation of 50-75% is observed between cysteines introduced at positions 30 and 31 in the N-terminal helix and 276 and 278 in the C-terminal helix, cross-linking has no apparent effect on catalysis
additional information
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mutations at the C-terminal part of the gamma-subunit of chloroplast F1 reconstituted with the F1 alpha and beta subunits of the photosynthesizing bacterium affect conformation signal transduction between the catalytic and noncatalytic sites
additional information
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hybrid vacuolar H+-ATPase containing the mouse testis-specific E1 isoform and yeast subunits shows a defective assembly, reversible defect of the hybrid V-ATPase. Glucose depletion, known to dissociate V1 from Vo in yeast, has only a slight effect on the hybrid at acidic pH. The domain between Lys26 and Val83 of E1, which contains eight residues not conserved between E1 and E2, is responsible for the unique properties of the hybrid, while the E2 domain in E2/VMA4-2 chimera corresponding to between Lys26 and Val83 of E1 has no effect on the assembly of the V-ATPase. The mutant shows a temperature-sensitive defect
additional information
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mutations in the profilin-like region, actin-binding domain, of the B subunit reduced or eliminated the actin-binding activity. Mutants assemble properly with endogenous yeast subunits when expressed in B subunit-null yeast, and bafilomycin-sensitive ATPase activity is not significantly different from yeast transformed with wild-type B subunit. Yeast containing the mutant subunits grow as well at pH 7.5 as wild-type. Mutant B subunits are more sensitive to cycloheximide and wortmannin than those transformed with wild-type B subunits
additional information
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human pigment epithelium-derived factor is immobilized on the surface of a CM5 sensor chip revealing binding response units for the yeast F1-ATPase showing specific, reversible and concentration-response binding of F1 to PEDF
additional information
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construction of a chimeric F1 complex using cyanobacterial F1 from Thermosynechoccus elongatus, which mimics the regulatory properties of the chloroplast F1-ATPase introducing the regulatory element of spinach F1-ATPase gamma subunit, residues 187-210. The redox state of the gamma-subunit does not affect the ATP-binding rate to the catalytic site(s) and the torque for rotation. The long pauses caused by ADP inhibition are frequently observed in the oxidized state. The duration of continuous rotation is relatively shorter in the oxidized recombinant alpha3beta3gammaredox complex. The chimeric complex becomes biotinylated and shows higher stability for purification and assay experiments than the cyanobacterial wild-type, overview
additional information
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construction of mutant strains with a C-terminally truncated epsilon subunit, i.e. epsilonDELTAC, or with a gamma subunit lacking the inserted sequence of residues 198-222, i.e. gammaDELTA198-222, or a double mutant of both. All mutant strains show a lower intracellular ATP level and lower cell viability under prolonged dark incubation compared with the wild-type. Thylakoid membranes from the epsilonDELTAC strain showed higher ATP hydrolysis and lower ATP synthesis activities than those of the wild-type, but no significant difference is observed in growth rate and in intracellular ATP level both under light conditions and during light-dark cycles. The maximal ATPase activity of the epsilonDELTAC mutant is 2fold or more higher than for the wild-type, both show a similar drop in activity after transfer to the dark, phenotypes, overview
additional information
Thermosynechococcus vestitus
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inhibition of ATPase activity by the cyanobacterial epsilon subunit and the chimeric subunits composed of the N-terminal domain from the cyanobacterium and the C-terminal domain from spinach, overview
additional information
Thermosynechococcus vestitus
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construction of a chimeric F1 complex using the cyanobacterial F1, which mimics the regulatory properties of the chloroplast F1-ATPase from Spinacia oleracea introducing the regulatory element of the higher plant F1-ATPase gamma subunit, residues187-210. The redox state of the gamma-subunit does not affect the ATP-binding rate to the catalytic site(s) and the torque for rotation. The long pauses caused by ADP inhibition are frequently observed in the oxidized state. The duration of continuous rotation is relatively shorter in the oxidized recombinant alpha3beta3gammaredox complex. The chimeric complex becomes biotinylated and shows higher stability for purification and assay experiments than the cyanobacterial wild-type, overview
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A1AO ATP synthase is functionally produced in the F1FO ATP synthase-negative strain Escherichia coli DK8
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alpha-subunit, expression in Escherichia coli
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ATP2 gene, coding for the beta subunit of the mitochondrial F1-ATPase
ATPase genetically modified to include a His6 Ni affinity tag on the amino end of the mature beta-subunit, imported into mitochondrion, expression of the the purified chimeric enzyme in Escherichia coli DMY301
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beta and epsilon subunits
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construction of an expression plasmid and overexpression of the alpha-subunit, beta-subunit, gamma-subunit, delta-subunit with glutathione S-transferase fused at the amino terminus and the epsilon-subunit with glutathione S-transferase fused at the amino terminus
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expressed in Escherichia coli BL21 strain T7 Express lysY
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expressed in Escherichia coli BL21(DE3) cells
Thermosynechococcus vestitus
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expressed in Escherichia coli mutant DK8 deficient in ATP synthase and in Synechococcus sp. strain PCC 7942
expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli XL1-Blue MRF' cells
expressed in seedlings of Nicotiana tabacum cultivar NC89
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expression in enzyme-deficient Escherichia coli mutant strain DK8
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expression of a hybrid enzyme, formed by a mouse E1 isozyme and Saccharomyces cerevisiae subunits, in DELTAvma4 cells
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expression of a hybrid enzyme, formed by a mouse E1 isozyme and yeast subunits, in DELTAvma4 cells
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expression of at subunit beta N-terminally His10-tagged wild-type and mutant F1Fo in Escherichia coli and by the in vitro protease-free protein synthesis, PURE, system
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expression of Atp6p in HeLa cells depleted of the F1 beta subunit. Instead of being translationally downregulated, HeLa cells lacking F1 degrade Atp6p, thereby preventing proton leakage across the inner membrane
expression of C-terminally c-Myc-tagged wild-type F1b eta or F1betaK212Q mutants in HEK-293 cells
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expression of FoF1, tagged with His10 at the beta-subunit N-terminus, in Escherichia coli strain DK8
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expression of His-tagged enzyme mutants R364K, C193S, and C193S/R364K and of His-tagged hybrid mutants in Escherichia coli
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expression of His-tagged F1-ATPase in Escherichia coli strain Bl21(DE3)
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expression of His-tagged holoenzyme in Escherichia coli strain DK8
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expression of His-tagged wild-type and mutant enzyme alpha, beta, and gamma subunits in Escherichia coli strain M15
expression of monomeric Tbeta in F1Fo enzyme-deficient Escherichia coli strain DK 8
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expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex
expression of recombinant TF0F1 with a histidine tag of 10 residues at the N terminus of the beta subunit in Escherichia coli
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expression of subunit F1beta in Escherichia coli strain JM103, and of the beta subunit and fragments in Escherichia coli strain BL21(DE3)
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expression of the soluble His3-tagged V1VO ATPase subunit A of in Escherichia coli
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expression of the the cyano-epsilon, CF1-epsilon and the chimeric epsilon subunits in Escherichia coli strain BL21(DE3) as soluble proteins
Thermosynechococcus vestitus
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expression of wild-type and mutant enzymes
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expression of wild-type and mutant enzymes complex in strain DK8
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expression of wild-type and mutant enzymes in Escherichia coli strain DK8
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expression of wild-type and mutant V-ATPase B subunits as maltose-binding protein fusion proteins in Escherichia coli
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expression of wild-type FoF1 and subunit epsilon mutant EFoF1 in Escherichia coli strain RA1
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F1 moiety from the atp operon into vector pTrc99A, overexpressed in Escherichia coli RNE41 in the two variant complexes F1-wt and F1 deltasigma
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gene atpZ, encoded in the atp operon, sequence comparison, overview
Alkalihalophilus pseudofirmus
gene VHA-A encoding the catalytic subunit A, expression analysis
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genomic library construction, cloning of the gene encoding the alpha-subunit of the enzyme, DNA and amino acid sequence determination and analysis, sequence comparisons to F1-ATPAses, overview
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genomic library construction, cloning of the gene encoding the beta-subunit of the enzyme, DNA and amino acid sequence determination and analysis, sequence comparisons to the alpha-subunit sequence, and other F1-ATPase alpha-and beta-subunits, overview
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His-tagged enzyme is expressed in FoF1-deficient Escherichia coli B834(DE)cells
mutant enzymes are expressed in Kluyveromyces lactis mutant lacking the gamma rotor
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mutant plasmids expressed in Escherichia coli strain JM103
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overexpressed in Escherichia coli
overexpression of mutant enzymes in Escherichia coli and reconstitution of recombinant epsilon proteins with CF1(-epsilon) and epsilon-deficient thylakoid membranes
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sequence comparison, overview
strain ATCC3020 in Escherichia coli-derived in vitro transcription-translation system
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subunit E, DNA and amino acid sequence determination and anaylsis, phylogenetic analysis, expession analysis under salt stress, overview
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the catalytic subunit A of the archaeal-type H+-ATPase is cloned and expressed in Escherichia coli
transient expression of GFP-tagged ATP5B protein on cell surface and mitochondria in carcinoma cell lines, i.e. Hep-G2 cells, A-549 cells, 95-D cells, L-02 cells, and HEK-293 cells, the ectopic expression of ATP synthase is a consequence of translocation from the mitochondria
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transient overexpression of FOF1-ATP synthase alpha in human neuroblastoma SH-SY5Y cells
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expression of Atp6p in HeLa cells depleted of the F1 beta subunit. Instead of being translationally downregulated, HeLa cells lacking F1 degrade Atp6p, thereby preventing proton leakage across the inner membrane
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expression of Atp6p in HeLa cells depleted of the F1 beta subunit. Instead of being translationally downregulated, HeLa cells lacking F1 degrade Atp6p, thereby preventing proton leakage across the inner membrane
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expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex
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expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex
Thermosynechococcus vestitus
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phylogenetic analysis
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sequence comparison, overview
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sequence comparison, overview
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sequence comparison, overview
Halalkalibacterium halodurans
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sequence comparison, overview
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sequence comparison, overview
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sequence comparison, overview
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sequence comparison, overview
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