7.1.2.2: H+-transporting two-sector ATPase
This is an abbreviated version!
For detailed information about H+-transporting two-sector ATPase, go to the full flat file.
Word Map on EC 7.1.2.2
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7.1.2.2
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acidification
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adp
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bafilomycin
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lysosomal
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electrochemical
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triphosphate
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beta-subunits
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endosomes
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succinate
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bioenergetics
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stalk
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acidify
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osteoclast
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thylakoids
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submitochondrial
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tubule
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proteolipids
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resorption
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beef
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dissipation
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vanadate
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atp-driven
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mtdna
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acidosis
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antiporter
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subcomplexes
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photosystems
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electrogenic
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mgatp
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proteoliposomes
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cristae
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intercalated
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torque
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oxphos
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multisubunit
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presequence
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chromaffin
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endomembrane
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membrane-embedded
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proton-pumping
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supercomplexes
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gamma-subunits
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ceroid
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valinomycin
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b-subunits
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adenosinetriphosphatase
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nigericin
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light-driven
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leigh
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prorenin
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drug development
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synthesis
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molecular biology
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medicine
- 7.1.2.2
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acidification
- adp
- bafilomycin
- lysosomal
-
electrochemical
- triphosphate
- beta-subunits
- endosomes
- succinate
-
bioenergetics
- stalk
-
acidify
- osteoclast
- thylakoids
-
submitochondrial
- tubule
-
proteolipids
- resorption
- beef
-
dissipation
- vanadate
-
atp-driven
- mtdna
- acidosis
-
antiporter
-
subcomplexes
- photosystems
-
electrogenic
- mgatp
-
proteoliposomes
- cristae
-
intercalated
-
torque
-
oxphos
-
multisubunit
- presequence
-
chromaffin
-
endomembrane
-
membrane-embedded
-
proton-pumping
-
supercomplexes
-
gamma-subunits
-
ceroid
- valinomycin
-
b-subunits
- adenosinetriphosphatase
- nigericin
-
light-driven
- leigh
- prorenin
- drug development
- synthesis
- molecular biology
- medicine
Reaction
Synonyms
15 kDa mediatophore protein, 32 kDa accessory protein, 59 kDa membrane-associated GTP-binding protein, A-ATP synthase, A-ATPase, A1A0-ATP synthase, A1AO ATP synthase, A6L, ApNa+-ATPase, ATP synthase, ATP synthase F1, ATP synthase proteolipid P1, ATP synthase proteolipid P2, ATP synthase proteolipid P3, ATP5alpha1, ATPase, ATPaseTb2, atpB, AtpZ, bacterial Ca2+/Mg2+ ATPase, BN59, C7-1 protein, cf1, CF1-ATPase, CGI-11, chloroplast ATP synthase, chloroplast ATPase, chlorpoplast ATP synthase, complex V, coupling factor CF1, coupling factors (F0,F1 and CF1), Dicyclohexylcarbodiimide-binding protein, Ductin, DVA41, EC 3.6.1.34, EC 3.6.3.14, ECF1, Ecto-F1Fo ATP synthase/F1 ATPase, ectopic FoF1 ATP synthase, F-type proton-translocating ATPase, F0F1 ATP synthase, F0F1-ATP synthase, F0F1-ATP synthase alpha, F0F1-ATPase, F0F1ATP synthase, F1, F1 ATPase, F1-ATP synthase, F1-ATPase, F1-ATPase beta subunit, F1-F0 ATP synthase, F1F0 ATP synthase, F1F0 ATPase, F1F0-ATP synthase, F1F0-ATPase, F1F0H+-ATPase, F1Fo, F1Fo ATP synthase, F1FO ATPase, F1FO-ATP synthase, F1FO-ATPase, FoF1, FoF1 ATP synthase, FoF1 ATPase, FoF1-ATP synthase, FoF1-ATPase, FoF1-ATPase/synthase, FoF1H+-ATPase/synthase, Fo·F1-H+-ATPase (synthase), H(+)-transporting ATP synthase, H+ FoF1-ATP synthase, H+-ATP synthase, H+-ATPase, H+-coupled ATP synthase, H+-translocating ATPase, H+-transporting ATP synthase, H+-transporting ATPase, H+-V-ATPase, HATPL, HO57, Invasion protein invC, Isoform HO68, Isoform VA68, Lipid-binding protein, M40, matpase, membrane-associated ATPase, mitochondrial ATPase, mitochondrial F(1)-ATPase, mitochondrial F0F1-ATP synthase, mitochondrial F1F0 ATP hydrolase, mitochondrial F1Fo-ATP synthase, mitochondrial FOF1 ATP synthase, mitochondrial H+-ATP synthase, More, My032 protein, Na+-dependent F1F0-ATP synthase, 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, proton-translocating ATPase, rotary FOF1-ATPase, rotary molecular motor, Spa47, Stv1p, Sul-ATPase, Sul-ATPase alpha, Sul-ATPase beta, SUL-ATPase epsilon, Sul-ATPase gamma, T3SS ATPase, Tbeta, TF1, TF1-ATPase, TFoF1, tonoplast H+-ATPase, type III secretion-associated ATPase, uncB, UV-inducible PU4 protein, V-ATPase, 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-pump, V-type ATPase/synthase, V-type H+-ATPase, V1VO ATPase, vacuolar (H+)-ATPase, vacuolar ATPase, vacuolar H(+)-ATPase, vacuolar H+-ATPase, vacuolar H+-pumping ATPase, vacuolar H+-translocating ATPase, vacuolar H+-transporting adenosine triphosphatase, vacuolar proton-translocating ATPase, vacuolar-type H+-ATPase, vacuolar-type H+-translocating ATPase, vacuolar-type proton pumping ATPase, vacuolar-type, proton-translocating ATPase enzyme complex, VEG100, VEG31, Vegetative protein 100, Vegetative protein 31, VHA, VHA-A, VHA16K, VMA8, Vma8p, Vph1p, YOPS secretion ATPase
ECTree
7.1.2.2 H+-transporting two-sector ATPaseAdvanced search results
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results (Engineering
Engineering on EC 7.1.2.2 - H+-transporting two-sector ATPase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A63S
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site-directed mutagenesis, mutation in the c15 rotor reduces its H+ selectivity against Na+, ion coordination and transfer in wild-type enzyme compared to the wild-type enzyme
S66A
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site-directed mutagenesis, the mutation in the c11 rotor ring increases its proton-binding propensity, consistent with the impaired Na+ binding capacity
S66A/T67L
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site-directed mutagenesis, the double mutant is in its sequence composition identical to the wild-type c15 rotor, and accordingly it is very highly H+ selective
C193S
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alpha(His6 at N terminus/C193S)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
C193S/R364K
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alpha(His6 at N terminus/C193S/R364K)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
D112A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
E190A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
E190D
E190Q
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
K164A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
N173A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant retains full activity compared to the wild-type enzyme
N90A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
Q217A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
R169A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
R364A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
R364K
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alpha-subunit catalytic arginine finger mutant, the mutant shows a 350fold longer catalytic pause than the wild-type enzyme, but highly unidirectional rotation with a coupling ratio of 3 ATPs/turn, the same as wild-type, suggesting that cooperative torque generation by the 3 beta-subunits is not impaired. The alphaR364K mutation causes severe ADP inhibition of TF1
R84C/E190D/E391C
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incorporating of a single copy of the mutant beta-subunit to construct the chimera F1, alpha3beta2beta(E190D/E391C)gamma(R84C) which shows slowed ATP hydrolysis
C193S
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alpha(His6 at N terminus/C193S)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
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C193S/R364K
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alpha(His6 at N terminus/C193S/R364K)3beta(His10 at N terminus)3gamma(S108C/I211C) mutant subcomplex of F1
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D112A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant shows reduced activity compared to the wild-type enzyme
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E190A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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E190D
E190Q
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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K164A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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N173A
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site-directed mutagenesis, mutation of the alpha-subunit residue, the mutant retains full activity compared to the wild-type enzyme
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N90A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
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R169A
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site-directed mutagenesis, mutation of the alpha-subunit residue, inactive mutant
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R364A
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the mutant shows strongly reduced turnover number compared to the wild type enzyme
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R364K
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alpha-subunit catalytic arginine finger mutant, the mutant shows a 350fold longer catalytic pause than the wild-type enzyme, but highly unidirectional rotation with a coupling ratio of 3 ATPs/turn, the same as wild-type, suggesting that cooperative torque generation by the 3 beta-subunits is not impaired. The alphaR364K mutation causes severe ADP inhibition of TF1
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R84C/E190D/E391C
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incorporating of a single copy of the mutant beta-subunit to construct the chimera F1, alpha3beta2beta(E190D/E391C)gamma(R84C) which shows slowed ATP hydrolysis
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alphaC193S
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site-directed mutagenesis, the betaN-terminal His10-tagged mutant is constructed for bulk ATPase assays
alphaF244C
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the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme
alphaG351D
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaR169A
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thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1
alphaR169E
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thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1
alphaR169G/Q217R
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substitutions in the gamma subunit of Fo, the mutation blocks the passive proton translocation
alphaR169X
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thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation
alphaR304C
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the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme
alphaS347F
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaS373F
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaS375F
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mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites
alphaY300C
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the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme
betaE190D
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site-directed mutagenesis, mutation of the beta subunit of F1 mutant alphaC193S/gammaS108C/I211C, the mutant shows a clear pause of the temperature-sensitive reaction below 18°C, the catalytic state of the temperature-sensitive reaction in rotation of the hybrid F1, carrying a single copy of betaE190D is observed at 18°C
gammaE56Q
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substitution of Glu56 in the gamma subunit of Fo, the mutation blocks the passive proton translocation
gammaS107C/E165C
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site-directed mutagenesis, the alphaN-terminal His6-tagged mutant is constructed for single molecule manipulation
D262C
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modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
D262H
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modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
D262T
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modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1
E197C
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modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3
E197D
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modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3
E197S
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modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3
aR210A/aN214R
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site-directed mutagenesis, the subunit a mutant supports proton conduction onyl through EF1-depleted EFo, but not in EfoEF1, nor ATP-driven proton pumping
betaM159A
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homology modeling shows a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaS174F, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network suppressing the ATPase activity as well as subunit rotation of betaS174F
betaM159I
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homology modeling shows a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaS174F, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network suppressing the ATPase activity as well as subunit rotation of betaS174F
betaS174F
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the F1 beta subunit mutation in the hinge domain lowers the gamma subunit rotation speed, and thus decreases the ATPase activity. Homology modeling shows that the amino acid replacement induces a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaPhe174, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network
betaY331W
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the F1 beta subunit mutant shows higher sensitivity to Mg2+ increasing the inhibitory potency of 7-chloro-4-nitrobenz-2-oxa-1,3-diazole
cD61N/cM65D
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site-directed mutagenesis, the subunit c mutant grows on succinate, retains the ability to synthesize ATP, and supports passive proton conduction, but not ATP hydrolysis-driven proton pumping, overview
I28D
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growth on succinate is reduced to 25% of the wild-type value,reduced ATPase activity
M138C
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modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit
S10C
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modification of epsilon-subunit, reduced inhibition of the F1 part of the enzyme EC 3.6.3.14 by the epsilon subunit
S65C
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modification of epsilon-subunit, increases inhibition of ECF1 by the epsilon subunit
F446I
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the mutation in the alpha subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
G419D
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the mutation in the beta subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
F446I
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the mutation in the alpha subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
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G419D
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the mutation in the beta subunit suppresses cell death by the loss of mitochondrial DNA in a Kluyveromyces lactis mutant lacking the gamma rotor subunit
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R563A
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mutation in the a subunit leads to total loss of ATP synthesis activity
R563A/R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
R563K
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mutation in the a subunit leads to total loss of ATP synthesis activity
R563K/R625K
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mutation in the a subunit leads to total loss of ATP synthesis activity
R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
R625K
-
mutation in the a subunit, almost 50% of the ATP synthesis activity is retained compared to the wild type enzyme
R563A
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R563A/R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R563K
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R563K/R625K
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mutation in the a subunit leads to total loss of ATP synthesis activity
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R625A
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mutation in the a subunit leads to total loss of ATP synthesis activity
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betaY345F
site-directed mutagenesis, the mutant shows 72% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
betaY345F/Y368F
site-directed mutagenesis, the mutant shows 99% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
betaY368F
site-directed mutagenesis, the mutant shows 46% reduced inactivation by tyrosine nitration compared to the wild-type enzyme
K30C/A276C
-
alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
K30C/R278C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
V31C/A276C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
V31C/R278C
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alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex
A49T/R60S/W83R/Q132H/V163I/H236N/L296M/T338A
-
the mutant is resistant towards zinc
D46E/F50L/S198R/D217V/Y238F/K298E/T345A/T405M/L418P
-
the mutant is resistant towards zinc
E127V/A168T/L314Q/H344Y/H351Q
-
the mutant is resistant towards zinc
E222K
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
E76V/A79P/N164D/E340D/Q341K/H344Y/I403V
-
the mutant is resistant towards zinc
G133D
modification of beta-subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
G227D
modification of beta-subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
G80D/E220V/M221V
-
the mutant shows 10% of wild type ATPase activity
G80D/K209E
-
the double mutant shows increased coupling efficiency of proton transport and ATPase activity
H88L/I193S/Q209H/V303A/D337Y/I417N
-
the mutant is resistant towards zinc
I188N/I173N/A232T
-
the mutant shows 20% of wild type ATPase activity
L149V/E182D/D249G
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the mutant shows 35% of wild type ATPase activity
M221V
N56T/P110H/I176V/L307I/N372D/N415D
-
the mutant is resistant towards zinc
P179L
modification of beta subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
Q98H/K299R/K310N/H351R/K362N/Q379K
-
the mutant is resistant towards zinc
R293K
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
R735A
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735C
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the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735E
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735K
-
the mutant, although completely inactive for proton transport, retains 24% of wild type ATPase activity
R735L
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735N
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735Q
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R762A
-
the mutant retains full wild type ATPase activity and about 90% of wild type proton transport activity
R762K
-
the mutant retains about 80% of wild type ATPase activity and about 80% of wild type proton transport activity
R762L
-
the mutant retains about 75% of wild type ATPase activity and about 85% of wild type proton transport activity
R799A
-
the mutant is almost totally devoid of proton transport and ATPase activity
R799K
-
the mutant, which is almost completely inactive for proton transport, retains about 10% of wild type ATPase activity
R799L
-
the mutant is totally devoid of proton transport and ATPase activity
V71D/E220V
R735E
Saccharomyces cerevisiae MM112
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
-
R735K
Saccharomyces cerevisiae MM112
-
the mutant, although completely inactive for proton transport, retains 24% of wild type ATPase activity
-
R735N
Saccharomyces cerevisiae MM112
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
-
R735Q
Saccharomyces cerevisiae MM112
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
-
R762A
Saccharomyces cerevisiae MM112
-
the mutant retains full wild type ATPase activity and about 90% of wild type proton transport activity
-
A49G/L87S/R246K/N268Y/V312F
Saccharomyces cerevisiae SF838-1Dalpha
-
the mutant is resistant towards zinc
-
E127V/A168T/L314Q/H344Y/H351Q
Saccharomyces cerevisiae SF838-1Dalpha
-
the mutant is resistant towards zinc
-
Q98H/K299R/K310N/H351R/K362N/Q379K
Saccharomyces cerevisiae SF838-1Dalpha
-
the mutant is resistant towards zinc
-
C163V
the Walker A motif mutant exhibits a similar rate of ATP hydrolysis to the wild type enzyme
D308A
the mutant shows reduced activity compared to the wild type enzyme
D310A
the mutant shows reduced activity compared to the wild type enzyme
E307A
the mutant shows reduced activity compared to the wild type enzyme
F167A
the mutant shows reduced activity compared to the wild type enzyme
F311A
the mutant shows reduced activity compared to the wild type enzyme
L306A
the mutant shows reduced activity compared to the wild type enzyme
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
epsilonDELTAN5
-
mutant loses most of the inhibitory activity towards ATPase in solution, 50% loss of inhibitorty activity on membrane-bound ATPase, interaction with gamma subunits is lowered
A28C/L267C
Thermosynechococcus vestitus
-
the mutant shows strongly reduced activity compared to the wild type enzyme
A35C/A264C
Thermosynechococcus vestitus
-
the mutant shows increased ATP hydrolysis activity compared to the wild type enzyme
V32C/A268C
Thermosynechococcus vestitus
-
the mutant shows by about 4fold increased ATP hydrolysis activity compared to the wild type enzyme
V39C/A264C
additional information
E190D
-
the mutation in the beta-subunit reduces the ATP hydrolysis
E190D
-
reversibility of ATPgammaS hydrolysis and synthesis on F1(betaE190D) , overview
E190D
-
reversibility of ATPgammaS hydrolysis and synthesis on F1(betaE190D) , overview
-
E190D
-
the mutation in the beta-subunit reduces the ATP hydrolysis
-
M221V
-
the mutation leads to significant uncoupling of proton transport and ATPase activity
V71D/E220V
-
the mutations lead to significant uncoupling of proton transport and ATPase activity
V39C/A264C
Thermosynechococcus vestitus
-
the mutant shows by about 2.5fold increased ATP hydrolysis activity compared to the wild type enzyme
V39C/A264C
Thermosynechococcus vestitus
-
the mutant shows greatly increased ATP hydrolysis activity compared to the wild type enzyme
additional information
Alkalihalophilus pseudofirmus
polar deletion of atpI, atpZ or a double atpIZ deletion result in a defect in nonfermentative growth at pH 7.5 that is especially pronounced at suboptimal Mg2+ concentration
additional information
Alkalihalophilus pseudofirmus OF4
-
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
-
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
additional information
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generation of a mutant TFoF1 lacking an inhibitory segment of the epsilon-subunit, preparation of active proteoliposomes and for kinetic analysis of ATP synthesis, overview
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preparation of hybrid F1, alpha(C193S)3beta3gamma(S108C/I211C) subcomplex, of a hybrid F1 that carries a single alpha(R364K) subunit and 2 wild-type alpha subunits: F1(1 x alphaR364K), and of monomer alpha(His6 at N terminus/C193S/R364K) and of hybrid F1 containing one alpha(R364K), alpha(His6 at N terminus/C193S/R364K)alpha(C193S)2beta3gamma(S108C/I211C), termed F1(1xalphaR364K), the mutants are affected in rotation and hydrolysis activities, phenotypes, overview
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subunit beta adopts a different conformation during ATP synthesis in a mutant lacking the C-terminal domain of subunit epsilon, mutation of subunit epsilon C-terminal alpha-helix residues DELSDED leads to highly decreased inhibitory activity of subunit epsilon on ATPase activity, overview
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construction of a F1Fo mutant lacking the alpha-subunit, F1FoDELTAa, the alpha-subunit produced by the in vitro protease-free protein synthesis system is integrated into a preformed Fo a-less F1Fo complex in Escherichia coli membrane vesicles and liposomes. The resulting F1Fo has a H+-coupled ATP synthesis/hydrolysis activity that is approximately half that of the native F1Fo
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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
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mutation of the subunits alpha, beta, gamma and delta and epsilon, mutations of the F0 subunit
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(alpha V371C)3(beta R337C)3 gamma double mutant, steady state ATPase activity is 30% of that of the wild-type
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single cysteine mutations of subunit b expressed from Escherichia coli strain JM109
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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
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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
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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
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single cysteine mutations of subunit b expressed from Escherichia coli strain JM109
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siRNA-mediated downregulation of the beta subunit of the F1Fo-ATPase
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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
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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
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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
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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
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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
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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
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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
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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
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Thermosynechococcus vestitus
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inhibition of ATPase activity by the cyanobacterial epsilon subunit and the chimeric subunits composed of the N-terminal domain from the cyanobacterium and the C-terminal domain from spinach, overview
additional information
Thermosynechococcus vestitus
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construction of a chimeric F1 complex using the cyanobacterial F1, which mimics the regulatory properties of the chloroplast F1-ATPase from Spinacia oleracea introducing the regulatory element of the higher plant F1-ATPase gamma subunit, residues187-210. The redox state of the gamma-subunit does not affect the ATP-binding rate to the catalytic site(s) and the torque for rotation. The long pauses caused by ADP inhibition are frequently observed in the oxidized state. The duration of continuous rotation is relatively shorter in the oxidized recombinant alpha3beta3gammaredox complex. The chimeric complex becomes biotinylated and shows higher stability for purification and assay experiments than the cyanobacterial wild-type, overview
