Information on EC 3.6.3.14 - H+-transporting two-sector ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.6.3.14
-
RECOMMENDED NAME
GeneOntology No.
H+-transporting two-sector ATPase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
mechanism of proton conduction through F0, and the catalytic mechanism of F1
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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 + H+/in = ADP + phosphate + H+/out
show the reaction diagram
catalytic mechanism of the enzyme complex
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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 + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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 + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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 + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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
Q9EXJ9
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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 + H+/in = ADP + phosphate + H+/out
show the reaction diagram
model of mechanochemical coupling, overview
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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 + H+/in = ADP + phosphate + H+/out
show the reaction diagram
reaction mechanism and structure-fucntion analysis, overview
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
adenosine ribonucleotides de novo biosynthesis
-
Metabolic pathways
-
Oxidative phosphorylation
-
Photosynthesis
-
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 (archebacterial) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15 kDa mediatophore protein
-
-
-
-
32 kDa accessory protein
-
-
-
-
59 kDa membrane-associated GTP-binding protein
-
-
-
-
A-ATP synthase
O57724
-
A-ATP synthase
Pyrococcus horikoshii OT-3
O57724
-
-
A-ATPase
O57728
-
A-ATPase
Pyrococcus horikoshii OT-3
O57728
-
-
A1AO ATP synthase
O57724
-
A1AO ATP synthase
Pyrococcus horikoshii OT-3
O57724
-
-
A6L
-
-
-
-
ApNa+-ATPase
F2Z9M7, F2Z9M8, F2Z9N4
-
ATP synthase
-
-
-
-
ATP synthase
-
-
ATP synthase
-
-
ATP synthase
-
-
ATP synthase F1
-
-
ATP synthase proteolipid P1
-
-
-
-
ATP synthase proteolipid P2
-
-
-
-
ATP synthase proteolipid P3
-
-
-
-
AtpZ
Q9EXJ9
-
-
bacterial Ca2+/Mg2+ ATPase
-
-
-
-
BN59
-
-
-
-
C7-1 protein
-
-
-
-
CGI-11
-
-
-
-
chloroplast ATP synthase
-
-
chloroplast ATP synthase
P69447
-
chloroplast ATPase
-
-
-
-
chloroplast ATPase
-
-
chlorpoplast ATP synthase
-
-
coupling factors (F0,F1 and CF1)
-
-
-
-
Dicyclohexylcarbodiimide-binding protein
-
-
-
-
Ductin
-
-
-
-
DVA41
-
-
-
-
Ecto-F1Fo ATP synthase/F1 ATPase
-
-
ectopic FoF1 ATP synthase
-
-
F0F1-ATP synthase
-
-
F0F1-ATP synthase
-
-
F0F1-ATP synthase
Escherichia coli SWM1
-
-
-
F0F1-ATP synthase
-
-
F0F1-ATP synthase alpha
-
-
F0F1-ATPase
-
-
-
-
F0F1-ATPase
-
-
F0F1-ATPase
-
-
F0F1ATP synthase
-
-
F1 ATPase
P07251
-
F1-ATPase
-
-
-
-
F1-ATPase
-
-
-
F1-ATPase
P19483
-
F1-ATPase
-
-
F1-ATPase
-
isolated extrinsic part of ATP synthase, extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
F1-ATPase
Saccharomyces cerevisiae DK8
-
-
-
F1-ATPase
-
-
F1-ATPase beta subunit
-
-
F1F0 ATP synthase
-
-
F1F0 ATP synthase
Escherichia coli DK8
-
-
-
F1F0-ATP synthase
-
-
F1F0-ATP synthase
-
-
-
F1F0-ATP synthase
-
-
F1F0-ATP synthase
-
-
-
F1F0H+-ATPase
-
-
-
-
F1Fo
-
-
F1Fo ATP synthase
Q96253
-
F1Fo ATP synthase
-
-
F1Fo ATP synthase
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
Bacillus amyloliquefaciens FZB42
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
Bacillus anthracis Ames
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
Bacillus licheniformis ATCC 14580
-
-
-
F1FO-ATP synthase
Q9EXJ9
-
F1FO-ATP synthase
Q9EXJ9
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
Bacillus subtilis subsp. subtilis 168
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
Bacillus thuringiensis Al Hakam
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
F1FO-ATP synthase
Clostridium paradoxum DSM7308
Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
Oceanobacillus iheyensis HTE83
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
-
-
F1FO-ATP synthase
-
-
F1FO-ATPase
Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
F1FO-ATPase
Clostridium paradoxum DSM7308
Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
-
F1FO-ATPase
-
-
F1FO-ATPase
-
-
FoF1
-
-
FoF1 ATP synthase
-
-
FoF1 ATP synthase
-
-
FoF1 ATPase
-
-
FoF1 ATPase
Enterococcus hirae ATCC9790
-
-
-
FoF1-ATP synthase
-
-
FoF1-ATP synthase
-
-
FoF1-ATP synthase
-
-
FoF1-ATP synthase
-
-
FoF1-ATPase
-
-
FoF1-ATPase
-
-
FoF1-ATPase
-
-
FoF1-ATPase
-
-
-
FoF1-ATPase
P10719
-
FoF1-ATPase/synthase
-
-
FoF1-H+-ATPase (synthase)
-
-
FoF1-H+-ATPase (synthase)
Paracoccus denitrificans Pd 1222
-
-
-
H(+)-transporting ATP synthase
O57728
-
H(+)-transporting ATP synthase
Pyrococcus horikoshii OT-3
O57728
-
-
H+ FoF1-ATP synthase
-
-
H+-ATPase
-
-
-
-
H+-ATPase
-
-
H+-ATPase
-
-
H+-ATPase
Q7WTB6
-
H+-ATPase
Oenococcus oeni IOB84
Q7WTB6
-
-
H+-ATPase
O57728
-
H+-ATPase
Pyrococcus horikoshii OT-3
O57728
-
-
H+-coupled ATP synthase
-
-
H+-translocating ATPase
-
-
-
-
H+-transporting ATP synthase
O57728
-
H+-transporting ATP synthase
Pyrococcus horikoshii OT-3
O57728
-
-
H+-transporting ATPase
-
-
-
-
HATPL
-
-
-
-
HO57
-
-
-
-
Invasion protein invC
-
-
-
-
Isoform HO68
-
-
-
-
Isoform VA68
-
-
-
-
Lipid-binding protein
-
-
-
-
M40
-
-
-
-
membrane-associated ATPase
-
-
mitochondrial ATPase
-
-
-
-
mitochondrial F(1)-ATPase
-
-
mitochondrial F0F1-ATP synthase
-
-
mitochondrial F1F0 ATP hydrolase
-
-
mitochondrial F1Fo-ATP synthase
-
-
mitochondrial F1Fo-ATP synthase
-
-
mitochondrial F1Fo-ATP synthase
-
-
mitochondrial F1Fo-ATP synthase
-
-
mitochondrial FOF1 ATP synthase
-
-
My032 protein
-
-
-
-
Na+-dependent F1F0-ATP synthase
F2Z9M7, F2Z9M8, F2Z9N4
-
Oligomycin sensitivity conferral protein
-
-
-
-
OSCP
-
-
-
-
P31
-
-
-
-
P39
-
-
-
-
photosynthetic F1-ATPase
-
-
Physophilin
-
-
-
-
PKIWI505
-
-
-
-
plasma membrane V-ATPase
-
-
plasma membrane vacuolar H+-ATPase
-
-
Protein bellwether
-
-
-
-
proton translocating chloroplast ATP synthase
P69447
-
proton-translocating ATPase
-
-
proton-translocating ATPase
Paracoccus denitrificans Pd 1222
-
-
-
rotary FOF1-ATPase
-
-
rotary molecular motor
-
-
Sul-ATPase alpha
-
-
-
-
Sul-ATPase beta
-
-
-
-
Sul-ATPase beta
-
-
SUL-ATPase epsilon
-
-
-
-
Sul-ATPase gamma
-
-
-
-
TF1-ATPase
-
-
TFoF1
-
-
tonoplast H+-ATPase
-
-
UV-inducible PU4 protein
-
-
-
-
V-ATPase
-
-
V-ATPase
-
-
V-ATPase
-
-
V-ATPase
-
-
V-ATPase
O57724
-
V-ATPase
Pyrococcus horikoshii OT-3
O57724
-
-
V-ATPase 28 kDa accessory protein
-
-
-
-
V-ATPase 40 kDa accessory protein
-
-
-
-
V-ATPase 41 KDa accessory protein
-
-
-
-
V-ATPase 9.2 kDa membrane accessory protein
-
-
-
-
V-ATPase S1 accessory protein
-
-
-
-
V-type ATPase/synthase
-
-
V-type H+-ATPase
-
-
V1VO ATPase
-
-
vacuolar ATPase
-
-
vacuolar ATPase
Saccharomyces cerevisiae AH109
-
-
-
vacuolar H(+)-ATPase
-
-
vacuolar H+-ATPase
-
-
vacuolar H+-ATPase
-
-
vacuolar H+-ATPase
-
-
vacuolar proton-translocating ATPase
-
-
vacuolar proton-translocating ATPase
-
-
-
vacuolar-type proton pumping ATPase
-
-
VEG100
-
-
-
-
VEG31
-
-
-
-
Vegetative protein 100
-
-
-
-
Vegetative protein 31
-
-
-
-
VHA16K
-
-
-
-
YOPS secretion ATPase
-
-
-
-
F-type proton-translocating ATPase
-
-
F0F1 ATP synthase
additional information
-
-
mitochondrial H+-ATP synthase
-
-
additional information
-
the FOF1-ATP synthase alpha belongs to the family of stress proteins HSP60
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain NASF-1, strain ATCC33020
-
-
Manually annotated by BRENDA team
Asian tiger mosquito
-
-
Manually annotated by BRENDA team
epsilon subunit
UniProt
Manually annotated by BRENDA team
gamma subunit
UniProt
Manually annotated by BRENDA team
epsilon-subunit
UniProt
Manually annotated by BRENDA team
Bacillus amyloliquefaciens FZB42
-
-
-
Manually annotated by BRENDA team
Bacillus anthracis Ames
-
-
-
Manually annotated by BRENDA team
Bacillus licheniformis ATCC 14580
DSM 13
-
-
Manually annotated by BRENDA team
strain NRLL B939 and KM
-
-
Manually annotated by BRENDA team
strain QM B1551
-
-
Manually annotated by BRENDA team
Bacillus megaterium NRLL B939
strain NRLL B939 and KM
-
-
Manually annotated by BRENDA team
strain QM B1551
-
-
Manually annotated by BRENDA team
gene atpZ
UniProt
Manually annotated by BRENDA team
strain TA2.A1
-
-
Manually annotated by BRENDA team
unc operon
-
-
Manually annotated by BRENDA team
bacillus PS3
-
-
Manually annotated by BRENDA team
strain TA2.A1
-
-
Manually annotated by BRENDA team
Bacillus subtilis subsp. subtilis 168
-
-
-
Manually annotated by BRENDA team
Bacillus thuringiensis Al Hakam
-
-
-
Manually annotated by BRENDA team
cw15 arg7-8 mt+ mutant
-
-
Manually annotated by BRENDA team
strain DSM7308
SwissProt
Manually annotated by BRENDA team
Clostridium paradoxum DSM7308
strain DSM7308
SwissProt
Manually annotated by BRENDA team
Enterococcus hirae ATCC9790
-
-
-
Manually annotated by BRENDA team
several strains
-
-
Manually annotated by BRENDA team
strain DK8
-
-
Manually annotated by BRENDA team
strain SWM1 and JM109
-
-
Manually annotated by BRENDA team
Escherichia coli DK8
strain DK8
-
-
Manually annotated by BRENDA team
Escherichia coli SWM1
strain SWM1 and JM109
-
-
Manually annotated by BRENDA team
gene VHA-A encoding the catalytic subunit A
-
-
Manually annotated by BRENDA team
Oceanobacillus iheyensis HTE83
-
-
-
Manually annotated by BRENDA team
a part of the F1F0-ATPase; IOB84
UniProt
Manually annotated by BRENDA team
Oenococcus oeni IOB84
a part of the F1F0-ATPase; IOB84
UniProt
Manually annotated by BRENDA team
a salt-sensitive cultivar Zhonghua No. 11
-
-
Manually annotated by BRENDA team
Paracoccus denitrificans Pd 1222
-
-
-
Manually annotated by BRENDA team
catalytic subunit A
SwissProt
Manually annotated by BRENDA team
subunit E (a component of the peripheral stalk that links the A1 with the AO part of the A-ATP synthase)
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
-
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
catalytic subunit A
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
subunit E (a component of the peripheral stalk that links the A1 with the AO part of the A-ATP synthase)
SwissProt
Manually annotated by BRENDA team
beta-subunit; Sprague-Dawley rats
UniProt
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
gene ATP2 beta-F1-ATPase
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH109
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae DK8
strain DK8
-
-
Manually annotated by BRENDA team
; beta subunit
-
-
Manually annotated by BRENDA team
alpha subunit
SwissProt
Manually annotated by BRENDA team
additional information
goat
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Q9EXJ9
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
Q96253
the general structure and core subunits of the F1FO ATP synthase are highly conserved from bacteria to fungi, plants and animals
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
-
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
-
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
-
deletion of the 3'-UTR in the ATP2 gene leads to deficient protein import and reduced ATP synthesis, mtDNA depletion and respiratory dysfunction
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
-
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
-
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
-
lethal phenotype of the epsilon knock-out mutant
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
-
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
-
the siRNA-mediated downregulation of the beta subunit of the F1Fo-ATPase reduces influenza virion formation and virus growth in cell culture; virion formation/Budding of Influenza virus particles is reduced in F1beta-depleted cells
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
-
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
-
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
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
-
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
-
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
-
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
-
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
-
v-ATPase is a multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells
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
-
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
-, F2Z9M7, F2Z9M8, F2Z9N4
Na+-dependent F1F0-ATP synthase in the cytoplasmic membrane plays a potential role in salt-stress tolerance; Na+-dependent F1F0-ATP synthase in the cytoplasmic membrane plays a potential role in salt-stress tolerance; Na+-dependent F1F0-ATP synthase in the cytoplasmic membrane plays a potential role in salt-stress tolerance
physiological function
Q96253
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
-
F1-ATPase is an ATP-driven rotary motor protein in which the gamma-subunit rotates against the catalytic stator ring
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
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
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
-
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
-
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
-
Asn90 is located in the middle of putative second transmembrane helix and likely to play an important role in H+-translocation
additional information
-
molecular dynamics simulations and free-energy calculations of ion coordination and transfer in wild-type enzyme and mutant A63S, overview
additional information
-
F1-ATPase is the isolated extrinsic part of ATP synthase, the extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
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
-
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
-
ATP2 mRNA is no Puf3p target and belongs to the class of Puf3-independent mitochondria-localized mRNAs
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
Q96253
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
Enterococcus hirae ATCC9790
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxy-ATP + H2O
2'-deoxy-ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
-
-
-
-
r
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
-
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
show the reaction diagram
-
terminal enzyme in oxidative phosphorylation
-
r
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
low rates of ATP synthesis
-
-
?
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
Clostridium paradoxum DSM7308
Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
low rates of ATP synthesis
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
show the reaction diagram
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
show the reaction diagram
Enterococcus hirae, Enterococcus hirae ATCC9790
-
-
-
-
?
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
-
-
-
?
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
-
-
-
r
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
P10719
-
-
-
r
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
the enzyme cannot synthesize ATP in the dark, but may catalyze futile ATP hydrolysis reactions
-
-
r
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
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
show the reaction diagram
-
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
-
-
?
ATP + H2O + Fe2+/in
ADP + phosphate + Fe2+/out
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P00830
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q971B7, -
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P07251
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P69447
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q9EXJ9
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P19483
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
the primary function of the enzyme is H+ pumping for cytoplasmic pH regulation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
the enzyme transports protons, not Na+ ions
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
the side chain at position 28 is part of the ion binding pocket
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
ATP binding is rate limiting at a concentration below 0.002 mM
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
nucleotide binding structure, nucleotide occupancy of the catalytic sites, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q9EXJ9
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
P19483
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus anthracis Ames
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Saccharomyces cerevisiae DK8
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Saccharomyces cerevisiae AH109
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus amyloliquefaciens FZB42
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Paracoccus denitrificans Pd 1222
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Escherichia coli DK8
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus thuringiensis Al Hakam
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Clostridium paradoxum DSM7308
Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q9EXJ9
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Escherichia coli SWM1
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Oceanobacillus iheyensis HTE83
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus licheniformis ATCC 14580
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus megaterium NRLL B939
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus subtilis subsp. subtilis 168
-
-, protonmotive force- or sodium motive force-dependent ATP synthesis by a rotary mechanism, overview
-
-
r
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
O57724
-
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
show the reaction diagram
-, F2Z9M7, F2Z9M8, F2Z9N4
-
-
-
?
ATP + phosphate + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
r
CTP + H2O + H+/in
CDP + phosphate + H+/out
show the reaction diagram
-
poorly hydrolyzed
-
?
CTP + H2O + H+/in
CDP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
-
CTP + H2O + H+/in
CDP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
-
dATP + H2O + H+/in
dADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
17% of the activity with ATP
-
-
-
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
3.3fold slower reaction compared to ATP hydrolysis
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
enzyme shows maximal activity with ITP
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
-
-
-
-
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
-
poorly hydrolyzed
-
-
-
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ATP, ITP, GTP, UTP, CTP
-
-
-
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
-
the rate of nucleotide triphosphate hydrolysis follows the decreasing order: ITP, GTP, ATP, UTP, CTP
-
-
-
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
-
3% of the activity with ATP
-
-
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
17% of the activity with ATP
-
-
?
additional information
?
-
P00830
Gly133 of beta subunit is important for structural stability, Glu222 and Arg293 are important for catalytic cooperativity
-
-
-
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
?
-
-
at steady-state conditions, the F0F1-ATPase hydrolyzes ATP with significant participation of two sites
-
-
-
additional information
?
-
-
sites around residues 70 and/or between 202 and 212 of the gamma subunit are involved in epsilon subunit binding
-
-
-
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
?
-
-, Q7WTB6
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
?
-
-
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
?
-
-
no hydrolysis of UTP nor ADP
-
-
?
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 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 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
structure-function relationship of the R84C/E190D/E391C mutant enzyme, overview
-
-
-
additional information
?
-
-
the enzyme B subunit binds purified polymerized actin from rabbit muscle
-
-
-
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 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
?
-
-
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
?
-
-
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
?
-
P07251
electron density at the catalytic sites of F1 ATPase in the absence of nucleotides, overview
-
-
-
additional information
?
-
-
structure-function analysis, overview
-
-
-
additional information
?
-
-
structure-function relationship of the intrinsic inhibitor subunit epsilon subunit in F1 from photosynthetic organism, overview
-
-
-
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
?
-
-
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
?
-
P69447
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
?
-
-
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
?
-
Oenococcus oeni IOB84
Q7WTB6
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
-
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
show the reaction diagram
-
terminal enzyme in oxidative phosphorylation
-
r
ADP + phosphate + H+/out
ATP + H2O + H+/in
show the reaction diagram
-
-
-
-
?
ADP + phosphate + H+/out
ATP + H2O + H+/in
show the reaction diagram
Enterococcus hirae, Enterococcus hirae ATCC9790
-
-
-
-
?
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
-
-
-
?
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
-
-
-
r
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
P10719
-
-
-
r
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
the enzyme cannot synthesize ATP in the dark, but may catalyze futile ATP hydrolysis reactions
-
-
r
ATP + H2O + Fe2+/in
ADP + phosphate + Fe2+/out
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q971B7, -
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P07251
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P69447
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q9EXJ9
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P19483
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
the primary function of the enzyme is H+ pumping for cytoplasmic pH regulation
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
FoF1-ATP synthase complex regulation, the conformation of subunits determines the reaction direction, overview
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Bacillus weihenstephanensis KBAB4, Bacillus anthracis Ames
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Saccharomyces cerevisiae AH109
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus thuringiensis Al Hakam
-
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q9EXJ9
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Bacillus clausii KSM-K16, Anoxybacillus flavithermus WK1, Oceanobacillus iheyensis HTE83, Bacillus licheniformis ATCC 14580, Geobacillus thermodenitrificans NG80-2, Bacillus subtilis subsp. subtilis 168
-
-
-
-
r
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
O57724
-
-
-
?
ATP + phosphate + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
?
-
-
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
?
-
-, Q7WTB6
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
?
-
-
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 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 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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 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
?
-
-
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
?
-
-
modelling of regulation of FoF1-ATPase activity, overview
-
-
-
additional information
?
-
Oenococcus oeni IOB84
Q7WTB6
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can replace Mg2+ or Co2+
Ca2+
-
trypsin-induced ATPase activity of solubilized CF1 is dependent on the presence of Ca2+
Ca2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Ca2+
Ca2+
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower; can function in place of MgCl2, although the affinity is much lower
Ca2+
-
contributes to significant ATPase activity in trypsin-treated membranes, whereas Ca2+-ATPase activity of reduced thylakoids is very low
Ca2+
-
inhibits Fe2+ uptake by the enzyme by 25%, and the ATPase activity
Cd2+
-
activates
Co2+
-
absolute requirement for a divalent metal ion, Mg2+ or Co2+
Co2+
-
supports activity
Co2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Ca2+
Cu2+
-
inhibits Fe2+ uptake by the enzyme by 56%, and the ATPase activity
Fe2+
-
can replace Mg2+ or Co2+
Mg2+
-
required
Mg2+
-
absolute requirement for a divalent metal ion, Mg2+ or Co2+
Mg2+
-
ATPase activity of membrane bound CF1 is Mg2+-dependent
Mg2+
-
absolute requirement for Mg2+ or Mn2+; activates
Mg2+
-
Km: 0.5 mM; required; supports activity
Mg2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Ca2+
Mg2+
-
MgATP2- complex is the true substrate
Mg2+
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
dependent on; dependent on; dependent on; dependent on; dependent on; dependent on; dependent on; dependent on; dependent on
Mg2+
-
highest enzyme activity at 4-5 mM in the presence of 10 mM ATP
Mg2+
-
restores most oligomycin-sensitive ATPase activity after hypoxia/reoxygenation
Mg2+
-
activates
Mg2+
-
the motor requires a free magnesium ion as an indispensable cofactor to bring into service
Mg2+
-
required
Mg2+
P10719
required
Mg2+
-
required
Mg2+
-
required, analysis of binding of F1 monomer to Mg2+-free and Mg2+-bound adenosine nucleotides using high-precision isothermal titration calorimetry, structural-energetic analysis suggests that Tbeta adopts a more closed conformation when it is bound to Mg-ATP than to ATP or Mg-ADP, in agreement with recently published NMR data, analysis of Mg2+ energetic effects for the free energy change of F1 catalytic sites, in the framework of bi- or tri-site binding models, overview
Mg2+
Q9EXJ9
required
Mg2+
-
required for ATPase/ATP synthase activity, stimulates Fe2+ uptake activity
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
MgADP-
-
the 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
Mn2+
-
can replace Mg2+ or Co2+
Mn2+
-
absolute requirement for Mg2+ or Mn2+; activates
Mn2+
-
supports activity
Na+
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+
Na+
-, F2Z9M7, F2Z9M8, F2Z9N4
ApNa+-ATPase has a putative Na+-binding site in subunit epsilon. The Na+ ion protects the inhibition of Na+-ATPase by N,N-dicyclohexylcarbodiimide; the Na+ ion protects the inhibition of Na+-ATPase by N,N-dicyclohexylcarbodiimide; the Na+ ion protects the inhibition of Na+-ATPase by N,N-dicyclohexylcarbodiimide
NaCl
-
increased relative growth rate/photosynthesis parameters at the optimal salinity of 100 mM NaCl
Ni2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Ca2+
phosphate
-
phosphate in the medium exerts an opposite effect on iron uptake depending on the type of adenosine nucleotide, which is suppressed with ATP, but enhanced with ADP. Mn2+ does not affect the Fe2+ uptake
Selenite
-
one of the activating anions, that stimulates MgATPase activity of EcF1, likely due to a decrease in a relative content of MgADP-inhibited EcF1 because activating anions accelerate reactivation of MgADP-inhibited enzyme
Zn2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Ca2+
Zn2+
-
inhibits Fe2+ uptake by the enzyme by 29%, and the ATPase activity slightly
Mn2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Ca2+
additional information
-
no stimulation of ATPase activity by K+
additional information
-
the enzyme activity is not affected by Ni2+ at 1 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
adenosine-5'-(beta,gamma-imino)-triphosphate
-
inhibits F1 rotation
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
-
competitive to ATP
ADP
-
inhibition mechanism, overview
ADP
-
inhibition of the enzyme causing pauses in the ATP synthesis or hydrolysis, reversible by lauryl dimethylamine-N-oxide
ADP
-
F1 strongly binds ADP lapsing into ADP inhibition, which pauses the 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-
angiostatin
-
-
-
angiostatin
-
competes with pigment epithelium-derived factor
-
ATP
-
free ATP, MgATP2- is the true substrate
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
-
Aurovertin
-
-
aurovertin B
-
non-selective ATPase inhibitor
azide
-
2 mM inhibits 91% ATPase activity
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
azide
-
inhibits F1 rotation
bafilomycin A1
-
-
BeF3-
-
-
-
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
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
cyanide 4-(trifluoromethoxy)phenylhydrazone
-
acts as an uncoupler and abolishes ATP synthesis
-
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
-
Dicyclohexylcarbodiimide
-
DCCD
Dicyclohexylcarbodiimide
-
-
diphosphate
-
location and properties of diphosphate-binding sites
epsilon subunit
-
activity of F1 and FoF1 from Bacillus PS3 is attenuated by the epsilon subunit in an inhibitory extended form, overview. ATP-dependent transition of epsilon in single F1 molecules from extended form to hairpin form by fluorescence resonance energy transfer. Rotation by a larger angle is required for the activation from epsilon inhibition compared to inhibition by ADP, inhibirtion mechanism, overview
-
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 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 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 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
-
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
-
-
Mg2+
-
0.3 mM, 50% inhibition of Ca2+-dependent activity
Mg2+
-
Ca2+-activated enzyme
Mg2+
-
free Mg+ inhibits, MgATP is the true substrate
MgADP-
-
irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after addition of AlCl3 and NaF
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
Mn2+
-
1 mM reduces ATPase activity 50% in the presence of 5 mM MgSO4
N,N'-dicyclohexylcarbodiimide
-
binds to F0
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
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,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
-, F2Z9M7, F2Z9M8, F2Z9N4
-
-
N,N-dicyclohexylcarbodiimide
-, F2Z9M7, F2Z9M8, F2Z9N4
;
-
N3-
-
inhibits cooperativity but not unisite catalysis in F1-ATPase
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
nigericin
-
acts as an uncoupler in the presence of valinomycin, and abolishes ATP synthesis
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
oligomycin
-
-
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
-
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
piceatanol
-
an F1 inhibitor, also inhibits Fe2+ uptake
-
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
-
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
-
-
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
-
sulfate
-
slightly inhibits
Tetranitromethane
-
-
tributyltin
-
-
Tributyltin chloride
-, F2Z9M7, F2Z9M8, F2Z9N4
80% inhibition at 0.1 mM; 80% inhibition at 0.1 mM; 80% inhibition at 0.1 mM
Trypsin
-
-
-
Zn2+
-
1 mM reduces ATPase activity 80% in the presence of 5 mM MgSO4
monensin
-, F2Z9M7, F2Z9M8, F2Z9N4
70% inhibition at 0.1 mM; 70% inhibition at 0.1 mM; 70% inhibition at 0.1 mM
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
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
additional information
-
inhibitior screening, overview
-
additional information
-
strong inhibitory effect of the TF1 epsilon subunit on nucleotide binding
-
additional information
P10719
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
-
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
-
no inhibition of Fe2+ uptake and ATPase activity by ouabain at 0.1 mM, and by ATP at 1 mM
-
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
-
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
-, F2Z9M7, F2Z9M8, F2Z9N4
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
-
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. 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
-
quercetin
-
an F1 inhibitor, also inhibits Fe2+ uptake
regulatory protein IF1
additional information
-
modulates changes in activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-Dinitrophenol
-
stimulates
2,4-Dinitrophenol
-
plant hormone 2,4-dinitrophenol does not influence enzyme expression, but highly increases the enzyme's H+-translocation activity
abscisic acid
-
plant hormone abscisic acid slightly induces the enzyme expression and highly increases the enzyme's H+-translocation activity
apoA-I
-
the enzyme binds apoA-I which activates the ATPase activity. 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
-
cyclosporin A
-
cyclosporin A stimulates both ATP hydrolysis and synthesis, and displaces cyclophilin D from MgATP-submitochondrial particles
lauryl dimethylamine-N-oxide
-
-
-
Lauryldimethylamine oxide
-
stimulates ATP hydrolysis activity of F1-wt or F1 deltasigma 30-45fold, respectively
Lauryldimethylamine oxide
-
LDAO, stimulates F1-ATPase
N,N'-dicyclohexylcarbodiimide
-
0.1 mM increases ATPase activity by 20%
sulfate
-
ATP hydrolysis-driven H+ translocation is stimulated by sulfate, but sulfate is a partial inhibitor at low and a nonessential activator at high ATP concentrations of the ATPase activity of F1
sulfite
-
50 mM stimulates 4fold
sulfite
-
10 mM stimulates both proton uptake and ATP hydrolysis of Mg2+-ATPase activity of trypsin-treated thylakoids
Trypsin
-
elicits higher rates of ATPase activity, Mg2+-ATPase activity of trypsinized thylakoids is only partially inhibited by the uncouplers
-
light
-
promotes ATP hydrolysis
-
additional information
-
activity is latent and must be unmasked by mild proteolysis with trypsin
-
additional information
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
additional information
-
salt stress stimulates the expression of VHA subunit E and of the Na+/H+ antiporter NHX
-
additional information
-
transgenic expression of the vacuolar Na+/H+ antiporter SsNHX1 from Suaeda salsa in rice leads to increased V-ATPase activity and increased salt tolerance in the transgenic plants, overview
-
additional information
-
ATP-binding rate of F1 increases upon the forward rotation of the rotor, and its binding affinity to ATP is enhanced by rotation
-
additional information
-
deletion of the extra amino acid segment of FoF1 ATPase gamma subunit results in a high ATP hydrolysis activity
-
additional information
-
by reduction, both the alpha3beta3gammaredox complex and the purified CF1 show a 2.7fold activation
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.013
-
ADP
-
pH not specified in the publication, 30C
0.025
-
ADP
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
0.1
-
ADP
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
0.00104
-
ATP
-
pH 7.0, 23C
0.052
-
ATP
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
0.053
-
ATP
-
pH 8.0, 37C, MgATPase activity of EcF1, in absence of selenite
0.073
-
ATP
-
pH 8.0, 37C, MgATPase activity of EcF1, in presence of selenite
0.078
-
ATP
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
0.097
-
ATP
-
-
0.11
-
ATP
-
2-(N-morpholino)ethane sulfonic acid buffer
0.12
-
ATP
-
pH 8.0, 30C, recombinant mutant epsilonDELTAC, ATP hydrolysis
0.14
-
ATP
-
pH 8.0, 30C, recombinant wild-type enzyme, ATP hydrolysis
0.315
-
ATP
-
pH 8, membrane-bound enzyme
0.48
-
ATP
-
F1-wt
0.5
-
ATP
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0; purified enzyme stimulated with Na+ at pH 7.0 and 9.0
0.55
-
ATP
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1; purified enzyme, Mg2+/ATP ratio maintained at 2:1
0.7
-
ATP
-
F1 deltasigma
0.79
-
ATP
-
pH 8, soluble enzyme
0.9
-
ATP
-
strain NRLL B939
1
-
ATP
-
strain KM
1
-
ATP
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
1.8
-
ATP
-
estimated at pH 8.5 at 40C
2.8
-
ATP
-, F2Z9M7, F2Z9M8, F2Z9N4
apparent value, recombinant enzyme, in 20 mM Tris-HCl, pH 7.6, 5mM MgCl2, 10 mM NaCl, temperature not specified in the publication; apparent value, recombinant enzyme, in 20 mM Tris-HCl, pH 7.6, 5mM MgCl2, 10 mM NaCl, temperature not specified in the publication; apparent value, recombinant enzyme, in 20 mM Tris-HCl, pH 7.6, 5mM MgCl2, 10 mM NaCl, temperature not specified in the publication
3
-
Na+/in
-, F2Z9M7, F2Z9M8, F2Z9N4
apparent value, recombinant enzyme, in 20 mM Tris-HCl, pH 7.6, 5mM MgCl2, 10 mM NaCl, temperature not specified in the publication; apparent value, recombinant enzyme, in 20 mM Tris-HCl, pH 7.6, 5mM MgCl2, 10 mM NaCl, temperature not specified in the publication; apparent value, recombinant enzyme, in 20 mM Tris-HCl, pH 7.6, 5mM MgCl2, 10 mM NaCl, temperature not specified in the publication
0.55
-
phosphate
-
pH not specified in the publication, 30C
3.2
-
phosphate
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
4.2
-
phosphate
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
0.78
-
MgATP2-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
effect of pH on kinetic parameters
-
additional information
-
additional information
-
kinetics, in presence and absence of sulfate, overview
-
additional information
-
additional information
-
steady-state Michaelis-Menten kinetics, investigation of the systematic kinetics of the holoenzyme FoF1-ATPase by a tri-site filled, random binding order, and stochastic mechanochemical tight coupling model, reaction dynamics, detailed overview
-
additional information
-
additional information
-
binding kinetics of pigment epithelium-derived factor to cell surface F1-ATP synthase, overview
-
additional information
-
additional information
-
reaction kinetics, overview
-
additional information
-
additional information
-
kinetics, wild-type and mutant enzymes, overview
-
additional information
-
additional information
-
kinetic model of the F1-ATPase, dependence of kinetic behaviour on the ATP concentration, overview
-
additional information
-
additional information
-
Michaelis-Menten kinetics, kinetic analysis of ATP synthesis, driven by acid-base transition and K+-diffusion potential, using active proteoliposomes
-
additional information
-
additional information
-
Michaelis-Menten kinetics of rotation
-
additional information
-
additional information
-
kinetics relevant to ATP and ATPgammaS hydrolysis and synthesis and phosphate or thiophosphate release and binding, overview
-
additional information
-
additional information
-
molecular basis of positive cooperativity among three catalytic sites, acceleration of the ATP docking process occurs via thermally agitated conformational fluctuations, overview. Rate constants of ATP binding and hydrolysis are determined as functions of the rotary angle
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
16
-
ADP
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
17
-
ADP
-
pH not specified in the publication, 30C
55
-
ADP
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
5.34
-
ATP
-
pH 7.0, 23C
285
-
ATP
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
539
-
ATP
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
16
-
phosphate
-
pH not specified in the publication, 30C
20
-
phosphate
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
66
-
phosphate
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
160
-
ADP
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
6504
2200
-
ADP
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
6504
3800
-
ATP
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
22040
10000
-
ATP
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
22040
4.8
-
phosphate
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
27500
21
-
phosphate
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
27500
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0255
-
ADP
-
pH 7.0, 23C, versus ATP
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
rate constants of the epsilon-binding obtained from epsilon-inhibition, overview
-
additional information
-
additional information
-
inhibition kinetics, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0001
-
42-58 IF1 synthetic peptide
-
inhibition of H+ uptake
-
0.00197
-
42-58 IF1 synthetic peptide
-
inhibition of H+ release
-
0.00047
-
IF1 protein
-
inhibition of H+ uptake
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.77
-
P10719
purified reconstituted recombinant mutant Y345F/Y368F F1-ATP synthase, ATPase activity, pH 7.5, 27C
2.017
-
P10719
purified reconstituted recombinant mutant Y368F F1-ATP synthase, ATPase activity, pH 7.5, 27C
2.149
-
P10719
purified reconstituted recombinant mutant Y345F F1-ATP synthase, ATPase activity, pH 7.5, 27C
2.402
-
P10719
purified reconstituted recombinant wild-type F1-ATP synthase, ATPase activity, pH 7.5, 27C
3.05
-
-
purified reconstituted enzyme complex, ATP hydrolysis, pH 8.0
3.25
-
-
purified reconstituted enzyme complex, ATP hydrolysis, pH 6.5
11
-
-
subunits alpha and beta of the F1-ATPase
12.9
13.5
-
-
25.2
-
-
-
29
-
-
alpha3beta3EG hybrid complex, shows 53% of the complete F1-ATPase activity
31
-
-
alpha3beta3EG hybrid complex
54
-
-
complete F1-ATPase
100
-
-
-
additional information
-
P10719
activity of nitrated purified reconstituted recombinant wild-type and mutant F1-ATP synthases, overview
additional information
-
-
measurement of ATP synthesis driven by acid-base transition and the K+-valinomycin diffusion potential, wild-type and mutant enzymes, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.65
-
-
assay at, pH inside the liposomes
6.5
-
-
-
6.5
-
-
assay at
6.75
-
-
assay at
6.9
7
-
assay at
7
7.5
-
assay at
7
-
-
assay at
7
-
-
assay at
7.4
-
-
assay at
7.5
8.8
-
ATP synthesis activity assay at
7.5
-
P10719
ATPase activity assay at
7.5
-
-
ATPase assay at
7.5
-
-
assay at
7.5
-
-
ATP hydrolysis activity assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
ATP hydrolysis assay at
7.6
8.5
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
ATP hydrolysis assay at
8.4
-
-
assay at
8.8
-
-
assay at, pH outside the liposomes
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
at pH 7.5 H+ efflux is stimulated in fhlA mutant, with defective transcriptional activator of Hyd-3 or Hyd-4, and lowered in hyaB or hybC mutants, with defective Hyd-1 or Hyd-2. At pH 5.5 H+ efflux in wild-type cells is lowered compared with that at pH 7.5, but is increased in fhlA mutant and absent in hyaB/hybC mutant, overview
6.5
8
-
-
7
9
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0; enzyme retains ca. 20% of its maximum activity at below pH 7.0
7
9.5
-
ATPase activity decreases markedly above or below this range
additional information
-
-
pH-dependence of unisite and multisite catalysis
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
23
-
-
assay at
25
-
-
assay at
25
-
-
ATP hydrolysis assay at
27
-
P10719
ATPase activity assay at
30
-
-
ATP synthase assay at
30
-
-
assay at
30
-
-
ATP hydrolysis assay at
35
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
optimum for Fe2+ uptake and ATPase activity
37
-
-
assay at
37
-
-
assay at
37
-
-
ATP hydrolysis assay at
42
-
-
assay at
45
-
-
ATPase assay at
50
-
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
50
-
activity range for Fe2+ uptake and ATPase activity
additional information
-
-
highly temperature-sensitive reaction step of F1-ATPase from thermophilic Bacillus PS3 below 9C as an intervening pause before the 80 substep at the same angle for ATP binding and ADP release. Temperature dependence of the rotation in wild-type and mutant enzymes, overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
8.54
-
enzyme complex subunits, theoretical values for mature proteins without transit peptides, overview
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
downregulation of beta-F1-ATPase is a hallmark of most human carcinomas. Translational silencing is usually mediated by 3'UTR-mediated sequestration of the mRNA into RNPs
Manually annotated by BRENDA team
-
Enterococcus hirae grows well under anaerobic conditions at alkaline pH 8.0
Manually annotated by BRENDA team
Enterococcus hirae ATCC9790
-
Enterococcus hirae grows well under anaerobic conditions at alkaline pH 8.0
-
Manually annotated by BRENDA team
-
HCT-116-derived carcinoma cell lines expressing different levels of beta-F1-ATPase
Manually annotated by BRENDA team
-
healthy and ischemic
Manually annotated by BRENDA team
-
vacuolar H+-ATPase
Manually annotated by BRENDA team
-
E1 isozyme
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
physiological growth temperature of Bacillus PS3 is 60C or above
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the ectopic expression of ATP synthase is a consequence of translocation from the mitochondria
Manually annotated by BRENDA team
-
progressive declining enzyme activity at supra-optimal salinities
Manually annotated by BRENDA team
-, F2Z9M7, F2Z9M8, F2Z9N4
-
-
Manually annotated by BRENDA team
-
detergent-resistant membrane microdomains enriched in cholesterol and sphingolipid, association with F1-ATPase, overview
-
Manually annotated by BRENDA team
-
exclusively internal location
Manually annotated by BRENDA team
-
the transmembrane domain of subunit b of F1F0 ATP synthase is sufficient for H+-translocating activity together with subunits a and c
Manually annotated by BRENDA team
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
Manually annotated by BRENDA team
Anoxybacillus flavithermus WK1, Bacillus amyloliquefaciens FZB42, Bacillus anthracis Ames, Bacillus clausii KSM-K16, Bacillus halodurans C-125, Bacillus licheniformis ATCC 14580, Bacillus megaterium NRLL B939, Bacillus pseudofirmus OF4, Bacillus pumilus SAFR-032, Bacillus sp. TA2.A1, Bacillus subtilis subsp. subtilis 168, Bacillus thuringiensis Al Hakam, Bacillus weihenstephanensis KBAB4, Candidatus Desulforudis audaxviator MP104C, Carboxydothermus hydrogenoformans Z-2901, Clostridium paradoxum DSM7308, Desulfotomaculum reducens MI-1, Enterococcus hirae ATCC9790, Escherichia coli BW25113, Escherichia coli DK8, Exiguobacterium sibiricum 255-15, Geobacillus thermodenitrificans NG80-2, Oceanobacillus iheyensis HTE83, Pelotomaculum thermopropionicum SI
-
-
-
Manually annotated by BRENDA team
-
the F1 moiety of the complex protrudes at the inner side of the membrane, the Fo sector spans the membrane reaching the outer side
Manually annotated by BRENDA team
-
the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. 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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
inner membrane
Manually annotated by BRENDA team
-
in vitro the subunit 8 of F1F0-ATPase can be inserted post-translationally across the inverted mitochondrial membrane vesicles with the correct trans-cis topology depending on the mitochondrial matrix fraction but independently of ATP, membrane potential, or protein components exposed to the matrix space
Manually annotated by BRENDA team
-
progressive declining enzyme activity at supra-optimal salinities
Manually annotated by BRENDA team
-
mitochondrial FOF1 ATP synthase
Manually annotated by BRENDA team
-
mitochondrial translation of the Saccharomyces cerevisiae Atp6p subunit of F1-F0 ATP synthase is regulated by the F1 ATPase
Manually annotated by BRENDA team
-
stimulated enzyme activity at intense salinities
Manually annotated by BRENDA team
-
high enzyme content in the ruffled membrane facing the the bone surface
Manually annotated by BRENDA team
-
ectopic FOF1 ATP synthase complexes
Manually annotated by BRENDA team
-
F1beta is present at the bottom ege of budding virions at the plasma membrane
Manually annotated by BRENDA team
Paracoccus denitrificans Pd 1222
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
increase of enzyme activity up to 300 mM NaCl
Manually annotated by BRENDA team
-
vacuolar H+-ATPase
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH109
-
-
-
Manually annotated by BRENDA team
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
-
Manually annotated by BRENDA team
Clostridium paradoxum DSM7308
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae DK8
-
-
-
Manually annotated by BRENDA team
additional information
-
enzyme localization study, overview
-
Manually annotated by BRENDA team
additional information
-
enzyme localization study, overview
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus sp. (strain PS3)
Bacillus sp. (strain PS3)
Bacillus sp. (strain PS3)
Brucella suis biovar 1 (strain 1330)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Geobacillus kaustophilus (strain HTA426)
Geobacillus kaustophilus (strain HTA426)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermosynechococcus elongatus (strain BP-1)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22880
-
O57724
calculated from sequence
66000
-
-
subunit A, gel filtration
280000
-
-
equilibrium sedimentation
325000
-
-
equilibrium ultracentrifugation
347000
-
-
F1, sedimentation equilibrium ultracentrifugation
360000
384000
-
equilibrium sedimentation
360000
-
-
purified F1-ATP synthase, gel filtration
379000
-
-
strain KM, sedimentation equilibrium centrifugation
385000
-
-
sedimentation equilibrium analysis
390000
-
-
gel filtration
400000
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
?
-
x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
?
-
x * alpha, 52000-53000 + x * beta, 51000 + x * gamma, 40000, SDS-PAGE
?
-
x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
?
-
x * 51526, calculated for beta subunit
?
Q971B7, -
x * 66009, calculated for alpha subunit
?
-
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 * 62800, recombinant His3-tagged subunit A of V1VO ATPase, SDS-PAGE
?
-
x * 60000, F1-ATP synthase beta-subunit, SDS-PAGE
?
-
x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
-
dimer
-
complex V exhibits an increased stability of its dimeric form
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
multimer
-
FOF1-ATP synthase is a multi-subunit protein
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
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
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
dodecamer
-
alpha6,beta6, 6 * 47000 + 6 * 51000, SDS-PAGE
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
-
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 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
-
-
additional information
-
structure-function relationship of the proton conductor F0
additional information
-
molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
-
size of major subunits
additional information
-
the stoichiometry of subunits in F1 is alpha3beta3gamma1delta1epsilon1, the stoichiometry of F0 subunits is not yet settled
additional information
-
-
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
-
-
additional information
-
interaction between delta and epsilon subunits; the tryptophan residue, located within the N-terminal region of the epsilon subunit is involved in deltaepsilon interaction
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
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence
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
-
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
-
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
-
comparison of amino acid sequence with alpha subunit and with alpha and beta subunits of Escherichia coli F1-ATPase
additional information
Q971B7, -
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
-
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 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
-
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
-
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
-
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
-
homology modeling of the immobilized enzyme, structure, overview
additional information
-
structure analysis F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state
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
-
the ATP synthase beta subunit hinge domain dramatically changes in conformation upon nucleotide binding, structure and modelling, overview
additional information
P10719
three-dimensional structures of wild-type and mutant beta-subunits, overview
additional information
-
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
-
transduction of the conformation signal between catalytic and noncatalytic sites, overview
additional information
-
transduction of the conformation signal between catalytic and noncatalytic sites, linking of catalytic and noncatalytic sites of F1, overview
additional information
Q9EXJ9
subunit organisation model, overview
additional information
P07251
structure analysis, 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
P69447
structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase, 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
-
F1 is a rotary chemical motor and generator, structure modelling, overview
additional information
-
beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
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
Q96253
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
P19483
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
Anoxybacillus flavithermus WK1, Bacillus amyloliquefaciens FZB42, Bacillus anthracis Ames, Bacillus clausii KSM-K16, Bacillus halodurans C-125, Bacillus licheniformis ATCC 14580
-
subunit organisation model, overview
-
additional information
Bacillus megaterium NRLL B939
-
size of major subunits
-
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; subunit organisation model, overview
-
additional information
-
subunit organisation model, overview
-
additional information
Clostridium paradoxum DSM7308
-
9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence; 9 subunits as calculated from DNA sequence
-
additional information
-
subunit organisation model, overview
-
additional information
Saccharomyces cerevisiae DK8
-
subunits alpha, beta, gamma, delta and sigma of the purified chimeric enzyme, with the stoichiometry of 3:3:1:1:1, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
tests for glucosamine, galactosamine and fatty acids in F1 are negative
additional information
P10719
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. Mechanism and stoichiometry of the reaction of Tyr residues with tetranitromethane, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
complex F1 deltasigma by micro-batch sreening, to 3.1 A resolution, no crystals obtained with complex F1-wt
-
mutant beta subunit
-
nucleotide-free alpha3beta3 subcomplex
-
asymmetric crystal structure of bovine mitochondrial F1
-
crystals of BeF3-F1 grown by microdialysis in the presence of BeCl2 and NaF and crystallization buffer without AmP-PNP, solved by molecular replacement to 2.2 A resolution, ADP-F1 crystals grown by microdialysis, AMP-PNP omitted from both the inside and outside buffer, ADP concentration increased to 2 mM in the outside buffer, solved by molecular replacement to 2.85 A resolution
-
orthorhombic crystals of F1-ATPase, grown during 4 weeks from 5 mg/ml protein solution mixed with an equal volume of crystallization solution containing 50 mM Tris-HCl, pH 8.0, 200 mM NaCl, 20 mM MgSO4, 0.02% w/v NaN3, 0.004% w/v PMSF, 1 mM ATP and 9-12% w/v PEG 6000 in D2O, are subjected to controlled dehydration resulting in a decrease in relative humidity surrounding the crystals to 90%, in reduced unit-cell volume by 22%, and significantly improved diffraction limit and mosaic spread of the crystals, X-ray diffraction and structure analysis at 1.8 A resolution, radiation damage limits the resolution of a complete data set to 1.95 A, overview
-
purified mitochondrial membrane F1-ATPase in complex with ADP and Mg2+, 10 mg/ml protein in solution containing 200 mM Tris-DCl, pH 7.2, 400 mM NaCl, and 1 mM ADP, and prepared with D2O, mixed with precipitation solution containing 100 mM Tris-DCl, pH 7.2, 400 mM NaCl, 4 mM MgCl2, 1 mM ADP, and 14% w/v PEG 6000, followed by dialysis against 3 mL of buffer consisting of 100 mM Tris-DCl, pH 8.2, 400 mM NaCl, 4 mM MgCl2, 1 mM ADP, 5 mM phosphorous acid, and 9% w/v PEG 6000 adding PEG is 0.25% steps, room temperature, 1-4 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement and modeling
P19483
to 1.95 A resolution, crystals grown in the presence of ADP, 5'-adenylyl-imidodiphosphate and azide in microdialysis buttons, diffraction properties of crystals improved by controlled dehydration
-
catalytic site at the alphaTP-betaTP interface with bound MgADP- in crystal structures represents a catalytic site containing inhibitory MgADP-
-
site-directed tryptophan fluorescence technique can provide valuable support for F1 crystallography studies
-
crystal structure of the entire subunit E (a component of the peripheral stalk that links the A1 with the AO part of the A-ATP synthase) at 3.6 A resolution. The structure reveals an extended S-shaped N-terminal alpha-helix with 112.29 A in length, followed by a globular head group
O57724, -
crystallographic analysis of subunit E, microbatch method using PEG 4000 as a precipitant
O57724
the catalytic subunit A of the archaeal-type H+-ATPase is crystallized by hanging-drop vapour-diffusion method with 2-methyl-2,4-pentanediol as a precipitant. X-ray intensity data are collected to 2.55 A resolution. The crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 128.0, c = 104.7 A, and contain one molecule per asymmetric unit
-
X-ray structure of the catalytic nucleotide-binding subunit A of an A(1)-ATPase is described and determined at 2.55 A resolution
-
by sitting drop method at 23C, to better than 2.8 A resolution
-
purified native nucleotide-free F1 ATPase, enzyme in 0.25 M sucrose, 0.2 M NaCl, 0.05 M Tris-Cl, 1mM EDTA, 2 mM sodium diphosphate, pH 8.0, 0.5 mM phenylmethylsulfonyl fluoride, crystallization buffer with PEG 6000 concentration 6.25% and 2 mM Na diphosphate replacing the nucleotides, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement
P07251
purified native chloroplast enzyme, hanging drop vapour diffusion method, 0.002 ml protein solution containing 10 mg/ml protein is mixed at 15C with 0.002 ml crystallization buffer containing 30% v/v PEG 400, 100 mM sodium acetate, pH 4.6, 100 mM cadmium chloride, and 100 mM lithium chloride, and 1 mM ADP to stabilize the F1F0 complex, X-ray diffraction structure determination and analysis at 3.8-4.0 A resolution
P69447
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
10
-
dissociation and loss of activity at low temperatures is accelerated in increasing order by I-, NO3-, Br-, Cl-, SO42-
0
-
-
rapid loss of activity, phosphate, nitrate and thiocyanate accelerate inactivation
4
-
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days; stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days
22
-
-
enzyme concentration 0.5 mg/ml, 20 mM potassium phosphate, 5 mM EDTA, pH 7.5, stable for up to 24 h
30
-
-
the recombinant hybrid enzyme Vo subunit a epitope is exposed to the corresponding antibody at 37C, but becomes inaccessible at 30C, showing apparent uncoupling between ATPase and proton transport
30
-
-
the recombinant hybrid enzyme Vo subunit a epitope is exposed to the corresponding antibody at 37 C, but becomes inaccessible at 30 C, showing apparent uncoupling between ATPase and proton transport
additional information
-
-
enzyme is stable in the cold
additional information
-
-
dissociation of the enzyme molecule at low temperatures, protection by chloroplast lipids
additional information
-
-
cold lability
additional information
-
-
no cold lability
additional information
-
-
cold lability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
F1 part of the enzyme EC 3.6.3.14 treated with trypsin at pH 7.0 still binds purified epsilon subunit, while enzyme treated with the protease at pH 8.0 does not
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, Tris-SO4 buffer, pH 8.5, 8 days
-
22C, 0.25 M sucrose, 2 mM EDTA, 4 mM ATP, 50 mM Tris-sulfate, pH 8, stable for several days
-
-20C, 200 mM potassium phosphate, 5.0 mM EDTA, pH 7.5, stable for up to 6 months
-
-70C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
51fold by chromatographies, purified ATPase does not contain the F0-portion
-
recombinant soluble His3-tagged V1VO ATPase subunit A from Escherichia coli by immobilized metal affinity and ion exchange chromatography to homogeneity
-
alpha and beta subunits of F1-ATPase
-
complexes F1-wt and F1 deltasigma, purified in high yield and purity by high affinity chromatography, anionic exchange chromatography and GPC
-
recombinant N-terminally His10-tagged wild-type and mutant F1Fo from Escherichia coli and the in vitro protease-free protein synthesis, PURE, system by nickel affinity chromatography
-
recombinant F1Fo-ATP synthase in membrane vesicles from enzyme-deficient Escherichia coli mutant strain DK8
-
recombinant His-tagged F1-ATPase from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His10-tagged FoF1, from Echerichia coli strain DK8 by nickel affinity chromatography
-
recombinant monomeric Tbeta from F1Fo enzyme-deficient Escherichia coli strain DK 8 to homogeneity
-
recombinant wild-type and mutant enzymes
-
F0 membrane domain
-
native H+ FoF1-ATP synthase complex from bovine heart mitochondria by detergent solubilization, ultracentrifugation, and ultrafiltration
-
30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation; 30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
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
-
His-tagged cysteine-less F1F0 ATP synthase, 80 fold by Ni-NTA affinity chromatography
-
recombinant wild-type enzyme and subunit epsilon mutant EFoF1 from Escherichia coli strain RA1
-
single cysteine mutations of subunit b
-
native enzyme from mitochondria
-
native enzymes from plasma membranes and mitochondria, solubilization by Triton X-100
-
recombinant His-tagged wild-type and mutant enzyme alpha, beta, and gamma subunits from Escherichia coli strain M15 by nickel affinity chromatography
P10719
by Ni-chelate affinity chromatography and gel filtration
-
native enzyme by gel filtration
P07251
recombinant wild-type and mutant V-ATPase B subunits as maltose-binding protein fusion proteins from Escherichia coli
-
native enzyme from thylakoid membranes by ammonium sulfate fractionation, sucrose density centrifugation, and anion exchange chromatography
P69447
recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration
-
deltaepsilon complex
-
large-scale purification
-
native enzyme from thylakoid membranes by ammonium sulfate fractionation, dye-ligand affinity and anion exchange chromatography
-
recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
strain ATCC3020 in Escherichia coli-derived in vitro transcription-translation system
-
expression of the soluble His3-tagged V1VO ATPase subunit A of in Escherichia coli
-
expressed in Escherichia coli mutant DK8 deficient in ATP synthase and in Synechococcus sp. strain PCC 7942; expressed in Escherichia coli mutant DK8 deficient in ATP synthase and in Synechococcus sp. strain PCC 7942; expressed in Escherichia coli mutant DK8 deficient in ATP synthase and in Synechococcus sp. strain PCC 7942
-, F2Z9M7, F2Z9M8, F2Z9N4
beta and epsilon subunits
-
gene atpZ, encoded in the atp operon, sequence comparison, overview
Q9EXJ9
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
-
expression of His-tagged enzyme mutants R364K, C193S, and C193S/R364K and of His-tagged hybrid mutants in Escherichia coli
-
F1 moiety from the atp operon into vector pTrc99A, overexpressed in Escherichia coli RNE41 in the two variant complexes F1-wt and F1 deltasigma
-
sequence comparison, overview
-
expression in enzyme-deficient Escherichia coli mutant strain DK8
-
expression of FoF1, tagged with His10 at the beta-subunit N-terminus, in Escherichia coli strain DK8
-
expression of His-tagged F1-ATPase in Escherichia coli strain Bl21(DE3)
-
expression of monomeric Tbeta in F1Fo enzyme-deficient Escherichia coli strain DK 8
-
expression of recombinant TF0F1 with a histidine tag of 10 residues at the N terminus of the beta subunit in Escherichia coli
-
expression of subunit F1beta in Escherichia coli strain JM103, and of the beta subunit and fragments in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant enzymes
-
sequence comparison, overview
-
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
-
expression of His-tagged holoenzyme in Escherichia coli strain DK8
-
expression of wild-type and mutant enzymes complex in strain DK8
-
expression of wild-type and mutant enzymes in Escherichia coli strain DK8
-
expression of wild-type FoF1 and subunit epsilon mutant EFoF1 in Escherichia coli strain RA1
-
mutant plasmids expressed in Escherichia coli strain JM103
-
sequence comparison, overview
-
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
-
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
-
gene VHA-A encoding the catalytic subunit A, expression analysis
-
subunit E, DNA and amino acid sequence determination and anaylsis, phylogenetic analysis, expession analysis under salt stress, overview
-
expression of a hybrid enzyme, formed by a mouse E1 isozyme and Saccharomyces cerevisiae subunits, in DELTAvma4 cells
-
transient overexpression of FOF1-ATP synthase alpha in human neuroblastoma SH-SY5Y cells
-
sequence comparison, overview
-
overexpressed in Escherichia coli
O57724
the catalytic subunit A of the archaeal-type H+-ATPase is cloned and expressed in Escherichia coli
-
alpha-subunit, expression in Escherichia coli
-
expression of His-tagged wild-type and mutant enzyme alpha, beta, and gamma subunits in Escherichia coli strain M15
P10719
ATP2 gene, coding for the beta subunit of the mitochondrial F1-ATPase
P00830
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
-
expression of a hybrid enzyme, formed by a mouse E1 isozyme and yeast subunits, in DELTAvma4 cells
-
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 wild-type and mutant V-ATPase B subunits as maltose-binding protein fusion proteins in Escherichia coli
-
phylogenetic analysis
-
expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex
-
overexpression of mutant enzymes in Escherichia coli and reconstitution of recombinant epsilon proteins with CF1(-epsilon) and epsilon-deficient thylakoid membranes
-
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
Q971B7, -
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
-
expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex
-
expression of the the cyano-epsilon, CF1-epsilon and the chimeric epsilon subunits in Escherichia coli strain BL21(DE3) as soluble proteins
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
repression of beta-F1-ATPase expression in development and in cancer, translational silencing is usually mediated by 3'UTR-mediated sequestration of the mRNA into RNPs. Role of 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-ATPase mRNA 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
-
expression of the catalytic subunit beta-F1-ATPase is tightly regulated at post-transcriptional levels during mammalian development and in the cell cycle
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A63S
-
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
-
site-directed mutagenesis, the mutation in the c11 rotor ring increases its proton-binding propensity, consistent with the impaired Na+ binding capacity
C193S
-
alpha(His6 at N terminus/C193S)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
C193S/R364K
-
alpha(His6 at N terminus/C193S/R364K)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
D112A
-
site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
E190D
-
the mutation in the beta-subunit reduces the ATP hydrolysis
N173A
-
site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant retains full activity compared to the wild-type enzyme
N90A
-
site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
Q217A
-
site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
R169A
-
site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
R364K
-
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
-
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
alphaC193S
-
site-directed mutagenesis, the betaN-terminal His10-tagged mutant is constructed for bulk ATPase assays
alphaC193S/gammaS108C/I211C
-
site-directed mutagenesis
alphaF244C
-
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
-
mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaR169A
-
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
-
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
-
substitutions in the gamma subunit of Fo, the mutation blocks the passive proton translocation
alphaR169X
-
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
-
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
-
mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaS373F
-
mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaS375F
-
mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaW463F/betaY341W
-
site-directed mutagenesis,
alphaY300C
-
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
-
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 18C, the catalytic state of the temperature-sensitive reaction in rotation of the hybrid F1, carrying a single copy of betaE190D is observed at 18C
gammaE56Q
-
substitution of Glu56 in the gamma subunit of Fo, the mutation blocks the passive proton translocation
gammaS107C/E165C
-
site-directed mutagenesis, the alphaN-terminal His6-tagged mutant is constructed for single molecule manipulation
D262C
-
modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
D262H
-
modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
D262T
-
modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
E197C
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
growth on succinate is abolished, reduced ATPase activity
I28D
-
growth on succinate is reduced to 25% of the wild-type value,reduced ATPase activity
I28D/D61G
-
growth on succinate is abolished, reduced ATPase activity
I28E
-
reduced ATPase activity
I28E/D61G
-
growth on succinate is abolished, reduced ATPase activity
S10C
-
modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit
betaY345F
P10719
site-directed mutagenesis, the mutant shows 72% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
betaY345F/Y368F
P10719
site-directed mutagenesis, the mutant shows 99% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
betaY368F
P10719
site-directed mutagenesis, the mutant shows 46% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
K30C/A276C
-
alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
V31C/A276C
-
alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
V31C/R278C
-
alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
E222K
P00830
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
G133D
P00830
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
P179L
P00830
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
R293K
P00830
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
epsilonC6S
-
mutant inhibits ATPase activita as potently as the epsilon-wild-type
epsilonDELTAC10
-
mutant loses more than 80% of the inhibitory activity towards soluble ATPase
epsilonDELTAC6
-
mutant loses 40% of the inhibitory activity towards soluble ATPase
epsilonDELTAC7
-
mutant loses about 70% of the inhibitory activity towards soluble ATPase
epsilonDELTAC8
-
mutant loses about 70% of the inhibitory activity towards soluble ATPase
epsilonDELTAC9
-
mutant loses about 70% of the inhibitory activity towards soluble ATPase
epsilonDELTAN1
-
deletion has only marginal effect on the maximum ATPase-inhibitory activity
epsilonDELTAN2
-
deletion has only marginal effect on the maximum ATPase-inhibitory activity
epsilonDELTAN3
-
mutation decreases its inhibitory activity towards ATPase activity significantly
epsilonDELTAN4
-
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
S66A/T67L
-
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
additional information
Q9EXJ9
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
-
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
-
E190D
-
reversibility of ATPgammaS hydrolysis and synthesis on F1(betaE190D) , overview
additional information
-
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
-
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
-
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
-
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
M138C
-
modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit
additional information
-
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
-
mutation of the subunits alpha, beta, gamma and delta and epsilon, mutations of the F0 subunit
additional information
-
(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
S65C
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modification of epsilon-subunit, increases inhibition of ECF1 by the epsilon subunit
additional information
Escherichia coli SWM1
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single cysteine mutations of subunit b expressed from Escherichia coli strain JM109
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K212Q
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site-directed mutagenesis for generation of mutation F1betaK212Q
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
K30C/R278C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
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
G227D
P00830
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
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
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
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
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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
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stripping of F1 and Fo from recombinant membrane fragments, and functional purified FoF1s reconstitutions in proteoliposomes, suspended in 10 mM HEPES/NaOH, pH 7.5, 0.25 M sucrose, and 5 mM MgSO4, at 25C
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purified native H+ FoF1-ATP synthase complex after purification
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reconstitution of purified recombinant mutant EFoF1 into liposomes using L-alpha-phosphatidylcholine from soybean suspended in 10 mM HEPES-NaOH, 5 mM MgSO4, and 1 mM KCl, pH 7.5
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F1 is reconstituted by using 3:3:1 molar ratios of recombinant alpha-, beta-, and gamma-subunits with a total protein concentration of 0.1 mg/ml, in the reconstitution dissolving buffer containing 10 mM Tris/succinate, pH 6.0, 0.2 mM 2-mercaptoethanol, 10% glycerol and 1% CHAPS, followed by dialysis against the reconstitution dialysis buffer containing 50 mM Tris/succinate, pH 6.0, 0.05 mM deferoxamine mesylate, 5 mM ATP, 2 mM MgCl2, 0.2 mM 2-mercaptoethanol, 10% glycerol and 1% CHAPS under constant stirring at room temperature
P10719
reconstitution of the purified enzyme in proteoliposomes
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denaturation of recombinant the cyano-epsilon, CF1-epsilon and the chimeric epsilon subunits, expressed from Escherichia coli strain BL21(DE3) as soluble proteins, using 8 M urea, and subsequent refolding
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purified native enzyme is reconstituted into liposomes
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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concomitant increase in shoot Na+ accumulation and leaf succulence of plants, at optimal salinity increased CO2 assimilation, stomatal conductance, sub-stomatal CO2 concentration, transpiration rate, Rubisco specific activity and both high nitrogen-use efficiency and photosynthetic nitrogen-use efficiency, higher salt levels impair photosynthetic capacity via a stomatal limitation
medicine
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when hyperemia is induced before ischemic preconditioning, a steep increase in synthase capacity, followed by a deep decrease can be observed, hyperemia does not affect synthase capacity when applied after ischemic preconditioning, similar effects in vitro by treatment of heart biopsy samples with anoxia, which down-regulates, or high salt or high pH buffers, which up-regulates
molecular biology
-, Q0ZS18, Q0ZS19, Q0ZS20, Q0ZS21, Q0ZS22, Q0ZS23, Q0ZS24, Q0ZS25, Q0ZS26
F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes
medicine
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ATP hydrolysis by F1FO-ATPase is well preserved after hypoxia/reoxygenation as long as Mg2+ is available, indicating that function of the enzyme is largely intact, but ATP hydrolysis by F1FO-ATPase does not restore mitochondrial membrane potential as much as expected from the rate of ATP utilization, it is likely that uncoupling plays a major role in the mitochondrial dysfunction in proximal tubules during hypoxia/reoxygenation
additional information
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formation of an active alpha3beta3EG hybrid complex by co-reconstitution of subunits alpha and beta of the F1-ATPase and of subunits E and G of Saccharomyces cerevisiae V-ATPase, the coupling subunit gamma inside the alpha3beta3 oligomer of F1 can be effectively replaced by subunit E of the V-ATPase, the E and gamma subunit are structurally similiar, but their genes do not show homology
molecular biology
Clostridium paradoxum DSM7308
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F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes; F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes
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additional information
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the catalytic site at the alphaTP-betaTP interface is loaded first upon addition of nucleotides to nucleotide-depleted F1-ATPases
additional information
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incorporation of F1F0 into soybean liposomes yields well-coupled and highly active proteoliposomes
additional information
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site-specific spin-labeling of single cysteine mutations within mutant of subunit b of the ATP-synthase and employed electron spin resonance indicate tight binding interaction between b2 and F1, different binding interactions of b to F1 in the presence or absence of sigma, b preperations spin-labeled between amino acid position 101 and 114 are indicative of either two populations of b subunits with different packing interactions or to helical bending within this region
additional information
Escherichia coli DK8
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incorporation of F1F0 into soybean liposomes yields well-coupled and highly active proteoliposomes
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additional information
Escherichia coli SWM1
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site-specific spin-labeling of single cysteine mutations within mutant of subunit b of the ATP-synthase and employed electron spin resonance indicate tight binding interaction between b2 and F1, different binding interactions of b to F1 in the presence or absence of sigma, b preperations spin-labeled between amino acid position 101 and 114 are indicative of either two populations of b subunits with different packing interactions or to helical bending within this region
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medicine
additional information
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F0F1 ATP synthase activity transiently increases during nonpreconditioned coronary reactive hyperemia, decreases 4 min after nonpreconditioned coronary reactive hyperemia and returns to control 2 min later, it is lower after ischemic preconditioning and does not change during and after preconditioned coronary reactive hyperemia, postischemic long-lasting inhibition of the enzyme activity may be a feature of the preconditioned heart
drug development
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the enzyme is a target for development of specific inhibitors
additional information
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simple and inexpensive method to grow yeast to high density and purify the mitochondrial F1-ATPase quickly and efficiently
drug development
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the enzyme is a target for development of specific inhibitors
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additional information
Saccharomyces cerevisiae DK8
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simple and inexpensive method to grow yeast to high density and purify the mitochondrial F1-ATPase quickly and efficiently
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additional information
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cleavage of the gamma subunit of the ATP synthase by trypsin prevents inhibition of ATPase activity by the sigma subunit, but only partially overcomes Mg2+-ADP inhibition during assay