Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,3-dicyclohexyl carbodiimide
-
2-[[4-(trifluoromethoxy)phenyl]hydrazinylidene]propanedinitrile
-
acts as an uncoupler and abolishes ATP synthesis
42-58 IF1 synthetic peptide
-
inhibits both H+ uptake and H+ release of the enzyme complex
-
7-chloro-4-nitrobenz-2-oxa-1,3-diazole
-
i.e. NBD-Cl, MgADP at low concentrations promotes the inhibition, whereas at higher concentrations EcF1 is protected from inhibition, that need to be higher for the mutant betaY331W, than for the wild-type enzyme. In absence of added MgATP, selenite slows down inhibition of EcF1 by 0.2 mM NBD-Cl
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
adenosine-5'-(beta,gamma-imino)-triphosphate
-
inhibits F1 rotation
AlCl3
-
irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP-
ATP
-
free ATP, MgATP2- is the true substrate
ATPase inhibitor factor 1
-
ATPase inhibitory factor 1
-
physiological inhibitor
-
aurovertin B
-
non-selective ATPase inhibitor
BMS-199264
-
a benzopyran analogue, selectively inhibits F1F0 ATP hydrolase activity with no effect on ATP synthase activity, BMS-199264 has no effect on ATP before ischemia, but reduces the decline in ATP during ischemia
cyclophilin D
-
cyclophilin D associates to the FOF1-ATP synthase complex in bovine heart mitochondria. The ATP synthase-cyclophilin D interactions have functional consequences on enzyme catalysis and are modulated by phosphate, leading to increased CyPD binding and decreased enzyme activity, and by cyclosporin A, leading to decreased CyPD binding and increased enzyme activity
-
diphosphate
-
location and properties of diphosphate-binding sites
F1-ATPase inhibitor
-
-
-
Fluorescein 5'-isothiocyanate
iejimalide A
-
a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
iejimalide B
-
a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
IF1-H49K protein
-
the F1-ATpase specific inhibitor inhibits the ATPase activity, the IF1 mutant shows inhibitory activity at neutral pH
-
inhibitor protein IF1
-
F1 in mitochondria is associated with a small regulatory protein, IF1, which inhibits its ATPase activity and the ecto-FOF1 activity, overview
-
intrinsic inhibitory peptide IF1
-
from Saccharomyces cerevisiae, the N-terminal part of the inhibitory peptide IF1 interacts with the central gamma subunit of mitochondrial isolated extrinsic part of ATP synthase in the inhibited complex. Kinetics of inhibition of the isolated and membrane-bound enzymes with IF1 modified in N-terminal extremity, i.e. IF1-Nter, overview. IF1-Nter plays no role in the recognition step but contributes to stabilize the inhibited complex. Its binding to the enzyme is not affected by truncations or fusion with PsaE, a 8 kDa globular-like protein
-
m-chlorophenylhydrazone
-
-
Mn2+
-
1 mM reduces ATPase activity 50% in the presence of 5 mM MgSO4
monensin
70% inhibition at 0.1 mM; 70% inhibition at 0.1 mM; 70% inhibition at 0.1 mM
N,N'-dicyclohexylcarbodiimide
N,NÂ’-dicyclohexylcarbodiimide
-
NaCl
-
inhibits ATPase activity
NaF
-
irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP-
NEM
-
modification of the Cys at position 10 with NEM or fluorescein maleimide further reduces the binding affinity of, and the maximal inhibition by the epsilon subunit
Ni2+
-
1 mM reduces ATPase activity 47% in the presence of 5 mM MgSO4
p-Trifluoromethoxyphenylhydrazone
-
diminishes ATP synthesis very effectively at 200 mM
piceatanol
-
an F1 inhibitor, also inhibits Fe2+ uptake
pigment epithelium-derived factor
-
quercetin
-
an F1 inhibitor, also inhibits Fe2+ uptake
regulatory protein IF1
-
the only significant modulator of enzyme activity, 1300-1400 mM of IF1 is predicted to fully inactivate 1000 mM of synthase, both in vivo and in vitro, thus excluding significant binding numbers of non-inhibitory binding sites for IF1 in the F0 sector
-
resveratrol
-
an F1 inhibitor, also inhibits Fe2+ uptake
SidK
-
a protein of Legionella pneumophila, an intracellular pathogen, specifically targets host v-ATPase. SidK interacts via an N-terminal portion with VatA, a key component of the proton pump leading to the inhibition of ATP hydrolysis and proton translocation. SidK inhibits vacuole acidification and impairs the ability of the cells to digest non-pathogenic Escherichia coli
-
Sodium dodecyl sulfate
-
-
sulfate
-
slightly inhibits
Trialkyltin derivatives
-
Tributyltin chloride
80% inhibition at 0.1 mM; 80% inhibition at 0.1 mM; 80% inhibition at 0.1 mM
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
ADP
-
-
ADP
-
F1 strongly binds ADP lapsing into ADP inhibition, which pauses the rotation
ADP
-
inhibition mechanism, overview
ADP
-
negative allosteric effector
ADP
-
incubation prior to assay abolishes Mg2+-ATPase activity of reduced thylakoids, has no effect on Mg2+-ATPase activity of trypsinized thylakoids
ADP
Thermosynechococcus vestitus
-
inhibition of the enzyme causing pauses in the ATP synthesis or hydrolysis, reversible by lauryl dimethylamine-N-oxide
ADP
Thermosynechococcus vestitus
-
-
angiostatin
-
-
-
angiostatin
-
competes with pigment epithelium-derived factor
-
ATPase inhibitor factor 1
-
i.e. IF1, intrinsic peptide inhibitor, up-regulated in human breast, colon and lung carcinomas. The binding of IF1 to beta-F1-ATPase is regulated by the energetic state of mitochondria. siRNA-mediated silencing of IF1 in cells expressing high levels of IF1 triggers the down-regulation of aerobic glycolysis and an increase in the activity of the H+-ATP synthase
-
ATPase inhibitor factor 1
-
i.e. IF1
-
ATPase inhibitor factor 1
-
i.e. IF1
-
Aurovertin
-
-
azide
-
2 mM inhibits 91% ATPase activity
azide
-
inhibits F1 rotation
azide
-
interacts with the beta-phosphate of ADP and with residues in the ADP-binding catalytic subunit, occupying a position between the catalytically essential amino acids beta-Lys-162 in the P loop and the arginine finger residue alpha-Arg-373, tightens the binding of the side chains to the nucleotide, enhancing its affinity and thereby stabilizing the state with bound ADP
bafilomycin A1
-
completely inhibited by less than 50 nM bafilomycin A1
Ca2+
-
-
Ca2+
-
extracellular, inhibits the enzym ein osteoclast membranes, Ca2+ behaves as a negative feedback signal for osteoclast function
Cu2+
-
1 mM reduces ATPase activity 99% in the presence of 5 mM MgSO4
Cu2+
-
Cu2+ affects the FoF1 ATPase directly, inhibits the enzyme, causes conformational changes in the FoF1 ATPase complex, and thereby affects growth of wild-type strain ATCC9790 and of atpD mutant strain MS116, overview
Dicyclohexylcarbodiimide
-
DCCD
Dicyclohexylcarbodiimide
Thermosynechococcus vestitus
-
-
Efrapeptin
-
-
-
Ethidium bromide
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
Hg2+
-
-
I2
-
-
IF1 protein
-
the IF1 component of the mitochondrial complex is a basic 10 kDa protein, which inhibits the FoF1-ATP hydrolase activity, and both H+ uptake and H+ release. IF1, and in particular its central 42-58 segment, displays different inhibitory affinity for proton conduction from the F1 to the Fo side and in the opposite direction. Cross-linking of IF1 toF1-a/b subunits inhibits the ATP-driven H+ translocation but enhances H+ conduction in the reverse direction
-
IF1 protein
-
the ability of IF1 to inhibit F1-ATPase activity depends on pH with a better efficiency at pH below 6.5
-
IF1 protein
-
the hydrolytic activity of the mitochondrial F1F0 ATP hydrolase, but not the synthase, is naturally inhibited by an 84 residue, heat-stable protein IF-1, which binds to F1F0 ATP hyrolase at the F1 domain with a 1:1 stoichiometry. In the absence of a proton motive force, IF-1 is a reversible, non-competitive inhibitor of ATPase hydrolase activity and is optimally functional at a pH below 7.0. The mechanism of IF-1 inhibition is via trapping of adenine nucleotides within the catalytic sites of F1
-
Mg2+
-
Ca2+-activated enzyme
Mg2+
-
free Mg+ inhibits, MgATP is the true substrate
Mg2+
-
0.3 mM, 50% inhibition of Ca2+-dependent activity
MgADP-
-
the enzyme is inhibited by tightly binding MgADP- and the inhibited fraction accumulates gradually until a steady state is reached that represents a dynamic equilibrium between active and MgADP-inhibited forms
MgADP-
-
irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after addition of AlCl3 and NaF
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
binds to F0
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
70% inhibition of the purified enzyme, 75% inhibition of the enzyme from mebrane vesicles
N,N'-dicyclohexylcarbodiimide
-
a nonspecific FOF1-ATPase inhibitor, inhibits ATPase activity and also other membrane mechanisms involved in H+ translocation, in a pH-dependent manner in hya mutants, overview
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
incubation of the membranes overnight at 4°C in the presence of 1 mM N,N'-dicyclohexylcarbodiimide results in a residual activity of 18% of the ATP synthesis rate measured with vesicles that are stored under the same conditions without N,N'-dicyclohexylcarbodiimide. Lower concentrations of N,N'-dicyclohexylcarbodiimide and short incubation times have only negligible effects
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%; 0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%
N-ethylmaleimide
-
-
N-ethylmaleimide
-
a potent V-ATPase inhibitor, causes only a 5–10% loss of activity if the vesicles are preincubated for 2 h and a concentration of 10 mM is employed
N3-
-
-
N3-
-
inhibits cooperativity but not unisite catalysis in F1-ATPase
nigericin
-
acts as an uncoupler in the presence of valinomycin, and abolishes ATP synthesis
nigericin
-
50% inhibition at 4 mM
nitrate
-
more than 81% inhibition at 1 mM
NO3-
-
-
NO3-
-
50 mM NO3- inhibits 90% of the hydrolytic activity, while H+ transport activity is decreased by 50%
oligomycin
-
binds to F0
oligomycin
-
inhibits ATP hydrolysis
oligomycin
-
non-selective ATPase inhibitor
oligomycin
-
a specific inhibitor of F1Fo ATP synthase, severely blocks transport of iron
peptide IF1
-
the inhibitory effect might be mediated through interaction of IF1 with the betaDELSEED sequence of the F1 domain of the mitochondrial enzyme, the alpha-helical IF1 N-terminus can penetrate into the alpha3beta3-hexamer between alpha and beta subunits, overview
-
peptide IF1
-
a natural inhibitor of the F1-ATPase, which binds at acidic pH, at cell surfaces
-
peptide IF1
-
a natural inhibitor of the F1-ATPase, which binds at acidic pH, at cell surfaces
-
phosphate
-
-
phosphate
-
phosphate in the medium exerted an opposite effect on iron uptake depending on the type of adenosine nucleotide, which is suppressed with ATP, but enhanced with ADP
pigment epithelium-derived factor
-
-
-
pigment epithelium-derived factor
-
competes with angiostatin. Human PEDF significantly reduces the amount of extracellular ATP produced by endothelial cells, in agreement with direct interactions between cell-surface ATP synthase and PEDF, 53% inhibition at 10 nM
-
subunit epsilon
-
subunit epsilon is required for inhibitory activity on F1 ATPase activity, mechanism, subunit epsilon can extend its C-terminus further inside the alpha3beta3-hexamer up to the N-terminus of subunit gamma, which has an anisotropic effect and enhances ATP hydrolysis inhibition to about 80% without affecting ATP synthesis, the C-terminal alpha-helix residues DELSDED are involved in inhibition, overview
-
subunit epsilon
-
subunit epsilon is required for inhibitory activity on F1 ATPase activity, the C-terminal alpha-helix residues DELSEED are involved in inhibition, mechanism, overview
-
Trialkyltin derivatives
-
-
-
Trialkyltin derivatives
-
-
-
Trialkyltin derivatives
-
-
-
Venturicidin
-
-
Venturicidin
-
noncompetitively inhibits ATP synthesis and coupled ATP hydrolysis
Zn2+
-
1 mM reduces ATPase activity 80% in the presence of 5 mM MgSO4
additional information
-
relatively resistant to vanadate, N,N'-dicyclohexylcarbodiimide and nitrate, 1 mM Fe3+, Ca2+ and Na+ do not affect ATPase activity in the presence of 5 mM MgSO4
-
additional information
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
-
not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine; not inhibited by carbonyl cyanide m-chlorophenyl hydrazine
-
additional information
-
not inhibited by azide or vanadate
-
additional information
-
strong inhibitory effect of the TF1 epsilon subunit on nucleotide binding
-
additional information
-
in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety. Subunit Asa7 plays a role in the sensitivity to oligomycin
-
additional information
-
in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety
-
additional information
-
the epsilon subunit of FoF1-ATP synthase inhibits the FoF1 ATP hydrolysis activity. The inhibitory effect is modulated by the conformation of the C-terminal alpha-helices of epsilon, and the extended but not hairpin-folded state is responsible for inhibition
-
additional information
-
the enzyme is autoinhibited by the subunit epsilon C-terminal domain. Nucleotide hydrolysis is required to form the epsilon-inhibited state
-
additional information
-
the ATP synthase activity is inhibited neither by the F-ATPase inhibitors 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (up to 1 mM) and phlorizin (up to 2 mM) nor by the V-ATPase inhibitor bafilomycin (0.1 mM)
-
additional information
-
both inhibitors, iejimalides A and B, sequentially neutralize the pH of lysosomes, induce S-phase cell-cycle arrest, and trigger apoptosis in MCF-7 cells, overview
-
additional information
tyrosine nitration is a covalent post-translational protein modification associated with various diseases related to oxidative/nitrative stress, that leads to inactivation of the ATPase activity of the enzyme
-
additional information
-
no inhibition of Fe2+ uptake and ATPase activity by ouabain at 0.1 mM, and by ATP at 1 mM
-
additional information
-
inhibitor screening, overview
-
additional information
-
the addition of 0.05 mM acetazolamide has practically no effect on the rate of ATP hydrolysis
-
additional information
-
the FoF1 ATPase epsilon subunit strongly inhibits ATP hydrolysis activity
-
additional information
-
in vivo, Chlamydomonas reinhardtii cells are insensitive to oligomycins, which are potent inhibitors of proton translocation through the FO moiety
-
additional information
Thermosynechococcus vestitus
-
ATP synthase contains an intrinsic inhibitor subunit epsilon, that acts as an endogenous inhibitor of chloroplast F1-ATPase, structure-function analysis, overview. Inhibition of ATPase activity by the cyanobacterial epsilon subunit and the chimaeric subunits composed of the N-terminal domain from the cyanobacterium and the C-terminal domain from spinach, overview
-
additional information
Thermosynechococcus vestitus
-
the epsilon subunit of the enzyme inhibits ATP hydrolysis activity, while the global conformational change of the gamma subunit indirectly regulates complex activity by changing both ADP inhibition and epsilon inhibition
-
additional information
-
subunit F might be involved in intramolecular regulation of ATPase activity
-
regulatory protein IF1
additional information
-
modulates changes in activity
-