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

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
3.6.3.14
-
SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
H+-transporting two-sector ATPase
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SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
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-
-
-
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
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
-
-
SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
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-
transmembrane transport
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-
-
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SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosine ribonucleotides de novo biosynthesis
-
-
Oxidative phosphorylation
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-
Photosynthesis
-
-
Metabolic pathways
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-
SplaateSystematic_Name,Commentary_IUBMB
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.
SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 kDa mediatophore protein
-
-
-
-
32 kDa accessory protein
-
-
-
-
59 kDa membrane-associated GTP-binding protein
-
-
-
-
A-ATP synthase
Pyrococcus horikoshii OT-3
-
-
A-ATPase
Pyrococcus horikoshii OT-3
-
-
A1AO ATP synthase
-
-
A1AO ATP synthase
Methanosarcina mazei DSM 3647
-
-
-
A1AO ATP synthase
-
A1AO ATP synthase
Pyrococcus horikoshii OT-3
-
-
A6L
-
-
-
-
ATP synthase
-
-
-
-
ATP synthase
-
-
ATP synthase
-
-
ATP synthase
-
-
ATP synthase F1
-
-
ATP synthase proteolipid P1
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-
-
-
ATP synthase proteolipid P2
-
-
-
-
ATP synthase proteolipid P3
-
-
-
-
bacterial Ca2+/Mg2+ ATPase
-
-
-
-
BN59
-
-
-
-
C7-1 protein
-
-
-
-
CGI-11
-
-
-
-
chloroplast ATP synthase
-
-
chloroplast ATP synthase
-
chloroplast ATPase
-
-
-
-
chloroplast ATPase
-
-
chlorpoplast ATP synthase
-
-
coupling factors (F0,F1 and CF1)
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-
-
-
Dicyclohexylcarbodiimide-binding protein
-
-
-
-
Ductin
-
-
-
-
DVA41
-
-
-
-
Ecto-F1Fo ATP synthase/F1 ATPase
-
-
ectopic FoF1 ATP synthase
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-
F0F1-ATP synthase
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-
F0F1-ATP synthase
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-
F0F1-ATP synthase
Escherichia coli SWM1
-
-
-
F0F1-ATP synthase
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-
F0F1-ATP synthase alpha
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-
F0F1-ATPase
-
-
-
-
F0F1-ATPase
-
-
F0F1-ATPase
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-
F0F1ATP synthase
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-
F1-ATPase
-
-
-
-
F1-ATPase
-
-
-
F1-ATPase
-
F1-ATPase
-
-
F1-ATPase
-
isolated extrinsic part of ATP synthase, extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
F1-ATPase
Saccharomyces cerevisiae DK8
-
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-
F1-ATPase
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F1-ATPase beta subunit
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-
F1F0 ATP synthase
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F1F0 ATP synthase
Escherichia coli DK8
-
-
-
F1F0-ATP synthase
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-
F1F0-ATP synthase
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-
-
F1F0-ATP synthase
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-
F1F0-ATP synthase
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-
F1F0H+-ATPase
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-
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F1Fo
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-
F1Fo ATP synthase
-
F1Fo ATP synthase
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-
F1Fo ATP synthase
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-
F1FO-ATP synthase
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-
F1FO-ATP synthase
-
-
-
F1FO-ATP synthase
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-
F1FO-ATP synthase
Bacillus amyloliquefaciens FZB42
-
-
-
F1FO-ATP synthase
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-
F1FO-ATP synthase
Bacillus anthracis Ames
-
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-
F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATP synthase
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-
F1FO-ATP synthase
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F1FO-ATP synthase
Bacillus licheniformis ATCC 14580
-
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-
F1FO-ATP synthase
-
F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATP synthase
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-
F1FO-ATP synthase
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-
F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATP synthase
Bacillus subtilis subsp. subtilis 168
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-
F1FO-ATP synthase
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F1FO-ATP synthase
Bacillus thuringiensis Al Hakam
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-
F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATP synthase
Clostridium paradoxum DSM7308
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F1FO-ATP synthase
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-
F1FO-ATP synthase
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F1FO-ATP synthase
Oceanobacillus iheyensis HTE83
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F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATP synthase
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F1FO-ATPase
Clostridium paradoxum DSM7308
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F1FO-ATPase
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F1FO-ATPase
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FoF1
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FoF1 ATP synthase
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FoF1 ATP synthase
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FoF1 ATPase
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FoF1 ATPase
Enterococcus hirae ATCC9790
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FoF1-ATP synthase
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FoF1-ATP synthase
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FoF1-ATP synthase
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FoF1-ATP synthase
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FoF1-ATPase
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FoF1-ATPase
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FoF1-ATPase
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FoF1-ATPase
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FoF1-ATPase/synthase
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FoF1-H+-ATPase (synthase)
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FoF1-H+-ATPase (synthase)
Paracoccus denitrificans Pd 1222
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H(+)-transporting ATP synthase
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H(+)-transporting ATP synthase
Pyrococcus horikoshii OT-3
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H+ FoF1-ATP synthase
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H+-ATPase
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-
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H+-ATPase
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H+-ATPase
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H+-ATPase
Oenococcus oeni IOB84
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H+-ATPase
Pyrococcus horikoshii OT-3
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H+-coupled ATP synthase
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H+-translocating ATPase
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H+-transporting ATP synthase
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H+-transporting ATP synthase
Pyrococcus horikoshii OT-3
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H+-transporting ATPase
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HATPL
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HO57
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Invasion protein invC
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Isoform HO68
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Isoform VA68
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Lipid-binding protein
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M40
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membrane-associated ATPase
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mitochondrial ATPase
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mitochondrial F(1)-ATPase
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mitochondrial F0F1-ATP synthase
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mitochondrial F1F0 ATP hydrolase
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mitochondrial F1Fo-ATP synthase
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mitochondrial F1Fo-ATP synthase
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mitochondrial FOF1 ATP synthase
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My032 protein
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Na+-dependent F1F0-ATP synthase
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Oligomycin sensitivity conferral protein
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OSCP
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P31
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P39
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photosynthetic F1-ATPase
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Physophilin
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PKIWI505
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plasma membrane V-ATPase
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plasma membrane vacuolar H+-ATPase
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Protein bellwether
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proton translocating chloroplast ATP synthase
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proton-translocating ATPase
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proton-translocating ATPase
Paracoccus denitrificans Pd 1222
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rotary FOF1-ATPase
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rotary molecular motor
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Sul-ATPase alpha
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Sul-ATPase beta
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Sul-ATPase beta
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SUL-ATPase epsilon
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Sul-ATPase gamma
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TF1-ATPase
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TFoF1
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tonoplast H+-ATPase
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UV-inducible PU4 protein
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V-ATPase
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V-ATPase
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V-ATPase
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V-ATPase
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V-ATPase
Pyrococcus horikoshii OT-3
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V-ATPase 28 kDa accessory protein
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V-ATPase 40 kDa accessory protein
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V-ATPase 41 KDa accessory protein
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V-ATPase 9.2 kDa membrane accessory protein
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V-ATPase S1 accessory protein
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V-type ATPase/synthase
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V-type H+-ATPase
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V1VO ATPase
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vacuolar ATPase
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vacuolar ATPase
Saccharomyces cerevisiae AH109
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vacuolar H(+)-ATPase
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vacuolar H+-ATPase
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vacuolar H+-ATPase
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vacuolar H+-ATPase
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vacuolar proton-translocating ATPase
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vacuolar proton-translocating ATPase
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vacuolar-type proton pumping ATPase
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VEG100
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VEG31
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Vegetative protein 100
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Vegetative protein 31
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VHA16K
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YOPS secretion ATPase
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F-type proton-translocating ATPase
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F0F1 ATP synthase
additional information
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mitochondrial H+-ATP synthase
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additional information
-
the FOF1-ATP synthase alpha belongs to the family of stress proteins HSP60
SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NASF-1, strain ATCC33020
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-
Manually annotated by BRENDA team
Asian tiger mosquito
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-
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
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-
-
Manually annotated by BRENDA team
Bacillus anthracis Ames
-
-
-
Manually annotated by BRENDA team
Bacillus licheniformis ATCC 14580
DSM 13
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Manually annotated by BRENDA team
strain NRLL B939 and KM
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-
Manually annotated by BRENDA team
strain QM B1551
-
-
Manually annotated by BRENDA team
Bacillus megaterium NRLL B939
strain NRLL B939 and KM
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-
Manually annotated by BRENDA team
strain QM B1551
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-
Manually annotated by BRENDA team
gene atpZ
UniProt
Manually annotated by BRENDA team
strain TA2.A1
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-
Manually annotated by BRENDA team
unc operon
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-
Manually annotated by BRENDA team
bacillus PS3
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-
Manually annotated by BRENDA team
strain TA2.A1
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-
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
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
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-
Manually annotated by BRENDA team
Haloferax volcanii WR 340
-
-
-
Manually annotated by BRENDA team
gene VHA-A encoding the catalytic subunit A
-
-
Manually annotated by BRENDA team
Methanosarcina mazei DSM 3647
-
-
-
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
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-
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
SplaateGeneral_Information, Organism, Commentary, Literature
GENERAL INFORMATION
ORGANISM
UNIPROT
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
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
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 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
-
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
-
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
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
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
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
-
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
low rates of ATP synthesis
-
?
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
Clostridium paradoxum DSM7308
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
-
-
-
?
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
-
-
-
r
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
-
-
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
-
?
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
-
the enzyme synthesizes ATP at the expense of a proton gradient
-
r
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
Haloferax volcanii WR 340
-
the enzyme synthesizes ATP at the expense of a proton gradient
-
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
-
-
-
?
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
-
-
-
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
-
-
-
?
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
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
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
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
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
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
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
-
the function of the ATP synthase is analyzed in an inverted membrane vesicle system of Escherichia coli DK8
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
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
Methanosarcina mazei DSM 3647
-
the function of the ATP synthase is analyzed in an inverted membrane vesicle system of Escherichia coli DK8
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Clostridium paradoxum DSM7308
-
-
?
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
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
Pyrococcus horikoshii OT-3
-
-
?
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 + Na+/in
ADP + phosphate + Na+/out
show the reaction diagram
-
-
?
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
?
-
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
?
-
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
?
-
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
?
-
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
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
-
-
-
SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
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
-
-
-
?
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
-
-
-
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
Haloferax volcanii, Haloferax volcanii WR 340
-
the enzyme synthesizes ATP at the expense of a proton gradient
-
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
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
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
-
-
-
?
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
-
-
-
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
-
-
-
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
O57724
-
-
?
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
Methanosarcina mazei DSM 3647
-
-
-
?
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
-
-
-
r
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Pyrococcus horikoshii OT-3
O57724
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Geobacillus thermodenitrificans NG80-2, Bacillus subtilis subsp. subtilis 168
-
-
-
r
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
-
-
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SplaateCofactor,Organism,Commentary,Literature,Filename
SplaateMetals_Ions,Organism,Commentary, Literature
METALS and IONS
ORGANISM
UNIPROT
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+
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+
KCl
-
like ATP hydrolysis, ATP synthesis can be performed in 1.75 mol/l KCl instead of NaCl
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+
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+
-
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+
-
required for ATPase/ATP synthase activity, stimulates Fe2+ uptake activity
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mg2+
-
in contrast to the ATP hydrolysis reaction, where Mn2+ and Mg2+ can be used almost equally, the ATP synthesis reaction strictly depends on Mg2+. Mn2+ can replace Mg2+, but with a dramatic loss of activity
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
Mn2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Ca2+
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+; stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+
Na+
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
NaCl
-
like ATP hydrolysis, ATP synthesis can be performed in 1.75 mol/l KCl instead of 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+
-
in contrast to the ATP hydrolysis reaction, where Mn2+ and Mg2+ can be used almost equally, the ATP synthesis reaction strictly depends on Mg2+. Mn2+ can replace Mg2+, but with a dramatic loss of activity
additional information
-
no stimulation of ATPase activity by K+
additional information
-
the enzyme activity is not affected by Ni2+ at 1 mM
SplaateInhibitors, Organism, Commentary, Literature,Filename
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3-dicyclohexyl carbodiimide
-
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-
AMP-PNP
-
-
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
-
-
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
-
-
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
concanamycin A
-
-
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
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
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
-
incubation of the membranes overnight at 4C 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-ethylmaleimide
-
a potent V-ATPase inhibitor, causes only a 510% loss of activity if the vesicles are preincubated for 2 h and a concentration of 10 mM is employed
N3-
-
-
N3-
-
inhibits cooperativity but not unisite catalysis in F1-ATPase
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
nigericin
-
50% inhibition at 4 mM
oligomycin
-
binds to F0
oligomycin
-
-
oligomycin
-
inhibits ATP hydrolysis
oligomycin
-
non-selective ATPase inhibitor
oligomycin
-
a specific inhibitor of F1Fo ATP synthase, severely blocks transport of iron
oligomycin
-
-
oligomycin
-
-
p-Trifluoromethoxyphenylhydrazone
-
diminishes ATP synthesis very effectively at 200 mM
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
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
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
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
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
-
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 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)
-
quercetin
-
an F1 inhibitor, also inhibits Fe2+ uptake
regulatory protein IF1
additional information
-
modulates changes in activity
-
SplaateActivating_Compound, Organism, Commentary, Literature,Filename
ACTIVATING COMPOUND
ORGANISM
UNIPROT
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
-
SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
0.57
ADP
-
pH 9.0, 40C
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
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
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
0.6
ATP
-
-
0.7
ATP
-
F1 deltasigma
0.79
ATP
-
pH 8, soluble enzyme
0.9
ATP
-
strain NRLL B939
1
ATP
-
strain KM
1
ATP
-
-
1.8
ATP
-
estimated at pH 8.5 at 40C
2.8
ATP
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
0.15
MgATP2-
-
-
3
Na+/in
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
-
SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16
ADP
Escherichia coli
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
17
ADP
Bacillus sp.
-
pH not specified in the publication, 30C
55
ADP
Escherichia coli
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
5.34
ATP
Bacillus sp. PS3
-
pH 7.0, 23C
217
ATP
Geobacillus stearothermophilus
-
-
285
ATP
Escherichia coli
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
539
ATP
Escherichia coli
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
16
phosphate
Bacillus sp.
-
pH not specified in the publication, 30C
20
phosphate
Escherichia coli
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
66
phosphate
Escherichia coli
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
160
ADP
Escherichia coli
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
13
2200
ADP
Escherichia coli
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
13
3800
ATP
Escherichia coli
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
4
10000
ATP
Escherichia coli
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
4
4.8
phosphate
Escherichia coli
-
recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication
16
21
phosphate
Escherichia coli
-
recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication
16
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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
-
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
42-58 IF1 synthetic peptide
Bos taurus
-
inhibition of H+ uptake
-
0.00197
42-58 IF1 synthetic peptide
Bos taurus
-
inhibition of H+ release
-
0.00047
IF1 protein
Bos taurus
-
inhibition of H+ uptake
-
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0071
-
pH 9.0, 40C, ATP synthesis in presence of Mn2+
0.0182
-
pH 9.0, 40C, ATP synthesis in presence of Mg2+
0.0314
-
pH 9.0, 40C, ATP hydrolysis, purified enzyme
1.77
purified reconstituted recombinant mutant Y345F/Y368F F1-ATP synthase, ATPase activity, pH 7.5, 27C
2.017
purified reconstituted recombinant mutant Y368F F1-ATP synthase, ATPase activity, pH 7.5, 27C
2.149
purified reconstituted recombinant mutant Y345F F1-ATP synthase, ATPase activity, pH 7.5, 27C
2.402
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
-
-
29
-
alpha3beta3EG hybrid complex, shows 53% of the complete F1-ATPase activity
31
-
alpha3beta3EG hybrid complex
54
-
complete F1-ATPase
100
-
-
additional information
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
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.65
-
assay at, pH inside the liposomes
6.5
-
-
6.9 - 7
-
assay at
7
-
assay at
7
-
assay at
7 - 7.5
-
assay at
7.4
-
assay at
7.5
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 - 8.8
-
ATP synthesis activity assay at
8
-
assay at
8
-
assay at
8
-
assay at
8
-
assay at
8
-
ATP hydrolysis assay at
8.8
-
assay at, pH outside the liposomes
9
-
ATP synthesis in washed membranes of Haloferax volcanii
9 - 9.5
-
-
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
pH RANGE
ORGANISM
UNIPROT
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
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
10
-
ATP synthesis in washed membranes of Haloferax volcanii, 75% of the optimal activity
additional information
-
pH-dependence of unisite and multisite catalysis
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
23
-
assay at
27
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
60
-
ATP synthesis in washed membranes of Haloferax volcanii
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 50
-
activity range for Fe2+ uptake and ATPase activity
25 - 70
-
ATP synthesis in washed membranes of Haloferax volcanii, 25C: 10% of the optimal activity, 30C: 30% of the optimal 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
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 8.54
-
enzyme complex subunits, theoretical values for mature proteins without transit peptides, overview
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SOURCE TISSUE
ORGANISM
UNIPROT
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
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
LOCALIZATION
ORGANISM
UNIPROT
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
-
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
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
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
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
Bacillus sp. (strain PS3)