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Information on EC 7.1.2.2 - H+-transporting two-sector ATPase
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7.1.2.2 H+-transporting two-sector ATPaseIUBMB Comments
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120_degree_ angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
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Word Map
- 7.1.2.2
- adp
-
acidification
- bafilomycin
- lysosomal
-
electrochemical
- succinate
- synthases
- triphosphate
- stalk
-
bioenergetics
- thylakoids
-
submitochondrial
-
rotor
- beta-subunits
- endosomes
-
proteolipids
- osteoclast
- mtdna
-
electrogenic
- photosystems
-
subcomplexes
-
dissipation
- spinach
-
atp-driven
- vanadate
-
protonophore
-
antiporter
- acidosis
-
intercalated
-
proteoliposomes
- mgatp
-
oxphos
- cristae
-
gamma-subunits
-
ceroid
- valinomycin
-
membrane-embedded
-
multisubunit
-
torque
-
proton-pumping
- m-chlorophenylhydrazone
-
supercomplexes
-
chromaffin
-
nuclear-encoded
- nigericin
- presequence
- leigh
-
b-subunits
- adenosinetriphosphatase
-
light-driven
- synthesis
- drug development
- molecular biology
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
15 kDa mediatophore protein, 32 kDa accessory protein, 59 kDa membrane-associated GTP-binding protein, A-ATP synthase, A-ATPase, A1A0-ATP synthase, A1AO ATP synthase, A6L, ApNa+-ATPase, ATP synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
15 kDa mediatophore protein
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-
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32 kDa accessory protein
-
-
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59 kDa membrane-associated GTP-binding protein
-
-
-
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A-ATP synthase
A-ATPase
A1AO ATP synthase
A6L
-
-
-
-
ATP synthase
ATP synthase proteolipid P1
-
-
-
-
ATP synthase proteolipid P2
-
-
-
-
ATP synthase proteolipid P3
-
-
-
-
ATPase
AtpZ
bacterial Ca2+/Mg2+ ATPase
-
-
-
-
BN59
-
-
-
-
C7-1 protein
-
-
-
-
CGI-11
-
-
-
-
chloroplast ATP synthase
chloroplast ATPase
complex V
coupling factors (F0,F1 and CF1)
-
-
-
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Dicyclohexylcarbodiimide-binding protein
-
-
-
-
Ductin
-
-
-
-
DVA41
-
-
-
-
Ecto-F1Fo ATP synthase/F1 ATPase
F0F1-ATP synthase
F0F1-ATPase
F1
F1-ATP synthase
F1-ATPase
F1-F0 ATP synthase
F1F0 ATP synthase
F1F0 ATPase
-
-
-
-
F1F0-ATP synthase
F1F0H+-ATPase
-
-
-
-
F1Fo
F1Fo ATP synthase
F1FO ATPase
F1FO-ATP synthase
F1FO-ATPase
FoF1
FoF1 ATP synthase
FoF1 ATPase
FoF1-ATP synthase
FoF1-ATPase
FoF1H+-ATPase/synthase
Fo·F1-H+-ATPase (synthase)
H(+)-transporting ATP synthase
H+-ATP synthase
-
the multisubunit complex is built by two major functional domains: the membrane-embedded Fo-ATPase (a and 8c subunits) and the membrane extrinsic catalytic F1-ATPase (3alpha, 3beta, gamma, delta and epsilon subunits) domains
H+-ATPase
H+-translocating ATPase
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-
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H+-transporting ATP synthase
H+-transporting ATPase
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-
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HATPL
-
-
-
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HO57
-
-
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Invasion protein invC
-
-
-
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Isoform HO68
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-
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Isoform VA68
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Lipid-binding protein
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-
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M40
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mitochondrial ATPase
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-
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mitochondrial F1Fo-ATP synthase
mitochondrial H+-ATP synthase
My032 protein
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Oligomycin sensitivity conferral protein
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OSCP
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-
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P31
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-
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P39
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-
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Physophilin
-
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PKIWI505
-
-
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Protein bellwether
-
-
-
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proton-translocating ATPase
rotary molecular motor
Stv1p
Sul-ATPase alpha
-
-
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Sul-ATPase beta
SUL-ATPase epsilon
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-
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Sul-ATPase gamma
-
-
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TFoF1
UV-inducible PU4 protein
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-
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V-ATPase
V-ATPase 28 kDa accessory protein
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V-ATPase 40 kDa accessory protein
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-
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V-ATPase 41 KDa accessory protein
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V-ATPase 9.2 kDa membrane accessory protein
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-
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V-ATPase S1 accessory protein
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-
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vacuolar (H+)-ATPases
vacuolar ATPase
vacuolar H+-ATPase
vacuolar H+-translocating ATPase
vacuolar H+-transporting adenosine triphosphatase
vacuolar proton-translocating ATPase
vacuolar-type H+-ATPase
vacuolar-type, proton-translocating ATPase enzyme complex
VEG100
-
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VEG31
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Vegetative protein 100
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Vegetative protein 31
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VHA16K
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-
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VMA8
Vma8p
Vph1p
YOPS secretion ATPase
-
-
-
-
F0F1 ATP synthase
ATP synthase
-
-
-
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chloroplast ATPase
-
-
-
-
F0F1-ATPase
-
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F1-ATPase
-
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F1-ATPase
-
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F1-ATPase
catalytic sector in FoF1-ATP synthase
F1-ATPase
-
isolated extrinsic part of ATP synthase, extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
F1FO-ATP synthase
-
F1FO-ATP synthase
-
-
F1FO-ATPase
-
F1FO-ATPase
-
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H+-ATPase
-
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Sul-ATPase beta
-
-
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V-ATPase
-
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vacuolar-type, proton-translocating ATPase enzyme complex
Saccharomyces cerevisiae SF838-1Dalpha
-
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additional information
-
the FOF1-ATP synthase alpha belongs to the family of stress proteins HSP60
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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]
-
-
-
-
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]
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]
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
-
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]
model of mechanochemical coupling, 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]
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
Bacillus clausii DSM 23117
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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]
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
-
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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
Bacillus sp. (in: Bacteria) TA2.A1
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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
Carboxydothermus hydrogenoformans Z-2901 / DSM 6008
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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
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+-transporting)
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120_degree_ angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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
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
low rates of ATP synthesis
-
-
?
ADP + phosphate + H+
ATP + H2O
low rates of ATP synthesis
-
-
?
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
-
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
-
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
-
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]
-
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]
-
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 + 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
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Bacillus clausii DSM 23117
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
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
-
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
-
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
-
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
-
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
-
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
Bacillus sp. (in: Bacteria) TA2.A1
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
-
210232, 210233, 210234, 210237, 210244, 210248, 210250, 210257, 210262, 673318, 684136, 685315, 696051, 698676, 733403, 733516
-
-
?
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
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Carboxydothermus hydrogenoformans Z-2901 / DSM 6008
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
Carboxydothermus hydrogenoformans Z-2901 / DSM 6008
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
-
210228, 210230, 210234, 210236, 210238, 210242, 210246, 210247, 210248, 210258, 210260, 210262, 210263, 674416, 685326, 734256, 734299
-
-
?
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
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
-
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
-
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
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
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
-
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
-
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
-
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
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
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
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the enzyme transports protons, not Na+ ions
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
Saccharomyces cerevisiae SF838-1Dalpha
-
-
-
-
?
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
-
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
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
-
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
-
enzyme shows maximal activity with ITP
-
-
?
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
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
subunit D plays an important role in coupling of proton transport and ATP hydrolysis
-
-
-
additional information
?
-
Saccharomyces cerevisiae KHY105
-
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
?
-
-
the enzyme shows a nucleotide specificity of ATP >> GTP > NTP
-
-
-
additional information
?
-
-
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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
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
-
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
-
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]
-
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]
-
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 + 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
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, 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
-
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
Carboxydothermus hydrogenoformans Z-2901 / DSM 6008
-
-
-
-
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
-
-
-
-
?
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
-
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
-
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
-
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
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
Saccharomyces cerevisiae SF838-1Dalpha
-
-
-
-
?
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
?
-
-
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
-
-
-