Information on EC 3.6.3.10 - H+/K+-exchanging ATPase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.3.10
-
RECOMMENDED NAME
GeneOntology No.
H+/K+-exchanging ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + H+/in + K+/out = ADP + phosphate + H+/out + K+/in
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transmembrane transport
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Oxidative phosphorylation
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+/K+-exchanging)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A gastric mucosal enzyme that catalyses the efflux of one H+ and the influx of one K+ per ATP hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
male guinea pigs
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Frog
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
sea urchin
-
-
Manually annotated by BRENDA team
i.e. Syrian hamster
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Turtle
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the ubiquitous Na,K-ATPase and the gastric H,K-ATPase belong to the PIIC subgroup of the extensive class of P-type ATPases, which use ATP hydrolysis for active transport of cations. A lysine residue within the highly conserved center of the fifth transmembrane segment in PIIC-type ATPase alpha-subunits is uniquely found in H,K-ATPases instead of a serine in all Na,K-ATPase, EC 3.6.3.9, isoforms
physiological function
additional information
-
direct H+/K+-ATPase inhibition by trimethyltin chloride in renal intercalated cells reduces urine K+ reabsorption and induces hypokalemia, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyATP + H2O + H+/in + K+/out
2'-deoxyADP + phosphate + H+/out + K+/in
show the reaction diagram
ADP + H2O + H+/in + K+/out
AMP + phosphate + H+/out + K+/in
show the reaction diagram
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
show the reaction diagram
ATP + H2O + H+/in + Rb+/out
ADP + phosphate + H+/out + Rb+/in
show the reaction diagram
-
-
-
-
?
CTP + H2O + H+/in + K+/out
CDP + phosphate + H+/out + K+/in
show the reaction diagram
GTP + H2O + H+/in + K+/out
GDP + phosphate + H+/out + K+/in
show the reaction diagram
ITP + H2O + H+/in + K+/out
IDP + phosphate + H+/out + K+/in
show the reaction diagram
-
a Na+-independent, ouabain-sensitive H+/K+-exchange, low activity with ITP
-
-
?
ITP + H2O + H+/in + K+/out
TDP + phosphate + H+/out + K+/in
show the reaction diagram
-
5% of the activity with ATP
-
?
UTP + H2O + H+/in + K+/out
UDP + phosphate + H+/out + K+/in
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H+
-
activates
H3O+
binds to the E1 conformation of the alpha-subunit of gastric proton pump, interaction similar to K+ interaction
Mn2+
-
77% of the activation with Mg2+, in absence of Mg2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(8-[(2-ethyl-6-methylbenzyl)amino]-2,3-dimethylimidazo[1,2-a]pyrazin-6-yl)methanol
-
-
(CH3)4N+
-
-
(R)-(+)-[(2-n-butyl-6,7-dichloro-2-cyclopentyl-2,3-dihydro-1-oxo-1H-inden-5-yl)oxy]acetic acid
-
a K+-Cl- cotransport, KCC, inhibitor, inhibits the enzyme in intact apical canalicular membranes, not in lealy membranes, via inhibition of the K+-Cl- cotransport
1,3,5,6-tetrahydroxy-2-(3-hydroxy-3-methylbutyl)-xanthone
-
a xanthone isolated from Calophyllum brasiliense leaves
1-(2',6'-dimethylbiphenyl-3-yl)-4-methylpiperazine
-
-
1-(2',6'-dimethylbiphenyl-3-yl)-N-methylmethanamine
-
-
1-hydroxy-3,5,6-tri-O-acetyl-2(3,3-dimethyl-allyl)-xanthone
-
a xanthone isolated from Calophyllum brasiliense leaves
2-(2',6'-diethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-2-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1,4,5-trimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1-methyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1-propyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-4,5-diethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-5-phenyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)pyridin-4-amine
-
-
2-(2-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(4-ethoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(4-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1-propyl-1H-imidazole
-
-
2-(4-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(6-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(biphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(biphenyl-4-yl)-4,5-dimethyl-1H-imidazole
-
-
2-aminopyrazine
-
-
2-Methoxy-2,4-diphenyl-3-dihydrofuranone
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
2-phenyl-6,7-dihydrobenzofuran-4(5H)-one oxime
-
-
-
2-[4-(2,6-dimethylphenyl)furan-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[4-(2,6-dimethylphenyl)thiophen-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[4-(benzyloxy)-2',6'-dimethylbiphenyl-3-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[4-(difluoromethoxy)-2',6'-dimethylbiphenyl-3-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)-1-benzofuran-7-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)-2,3-dihydro-1-benzofuran-7-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)furan-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)thiophen-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-{[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}acetamide
-
-
3'-(4,5-dimethyl-1H-imidazol-2-yl)-3-methylbiphenyl-4-thiol
-
-
3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-ol
-
-
3-({[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}methyl)pyridine
-
-
4,5-dimethyl-2-(2',4,5,6'-tetramethylbiphenyl-3-yl)-1H-imidazole
-
-
-
4,5-dimethyl-2-(2',6,6'-trimethylbiphenyl-3-yl)-1H-imidazole
-
-
4,5-dimethyl-2-(2'-methylbiphenyl-3-yl)-1H-imidazole
-
-
4,5-dimethyl-2-[3-(2-phenylethenyl)phenyl]-1H-imidazole
-
-
4,5-dimethyl-2-[3-(2-phenylethyl)phenyl]-1H-imidazole
-
-
4-(2',6'-dimethylbiphenyl-3-yl)-1,2-dimethyl-1H-imidazole
-
-
4-coumaric acid
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
5-(2',6'-dimethylbiphenyl-3-yl)-1-methyl-1H-imidazole
-
-
6-desoxyjacareubin
-
a xanthone isolated from Calophyllum brasiliense leaves
8-[(2-ethyl-6-methylbenzyl)amino]-2,3-dimethylimidazo[1,2-a]pyrazine-6-carboxamide
-
-
8-[(2-ethyl-6-methylbenzyl)amino]-N,2,3-trimethylimidazo[1,2-a]pyrazine-6-carboxamide
-
-
8-[(2-ethyl-6-methylbenzyl)amino]-N,N,2,3-tetramethylimidazo[1,2-a]pyrazine-6-carboxamide
-
-
8-[(2-ethyl-6-methylbenzyl)amino]-N-(2-hydroxyethyl)-2,3-dimethylimidazo[1,2-a]pyrazine-6-carboxamide
-
-
8-[(2-ethyl-6-methylbenzyl)amino]-N-(2-methoxyethyl)-2,3-dimethylimidazo[1,2-a]pyrazine-6-carboxamide
-
-
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-2,3-dimethylimidazo[1,2-a]pyridine-6-carboxamide
-
-
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-N,2,3-trimethylimidazo[1,2-a]pyridine-6-carboxamide
-
-
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
-
-
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-N-(1-methoxyethyl)-2,3-dimethylimidazo[1,2-a]pyridine-6-carboxamide
-
-
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]oxy]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
-
-
8-[[(1S,2S)-2-hydroxy-7-methoxy-2,3-dihydro-1H-inden-1-yl]oxy]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
-
-
8-[[(1S,2S)-2-hydroxy-7-methyl-2,3-dihydro-1H-inden-1-yl]oxy]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
-
-
aluminum fluoride
antibody 2G11
-
-
-
AR-HO47108
-
-
ATP
-
ATP concentrations over 5 mM induce H+/K+-ATPase activity inhibition, suggesting the existence of ATP-regulatory sites
beryllium fluoride
irreversible inhibition by the fluorinated phosphate analogue, activity is not restored by divalent cations, e.g. Mg2+. Electronmicrospoic structure of BeF-bound H+,K+-ATPase at 8 A resolution, and structural comparison of H+,K+-ATPase in the E2BeF and E2AlF states, overview
BMT-1
-
i.e. 2-(1H-benzimidazol-2-yl)-4,5,6,7-tetrahydro-2H-indazol-3-ol
-
bufalin
-
-
Butanedione
BYK36399
caffeic acid
-
-
Cd2+
-
-
Cinnamic acid
-
-
clotrimazole
-
molecular mechanism of the inhibitory effect is studied by steady-state fluorescence experiments with the electrochromic styryl dye RH421
Cu2+
-
-
diclofenac
-
-
diethyldicarbonate
digitoxin
-
-
digoxigenin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
digoxin
dihydro-ouabain
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
Dipicrylamine
esomeprazole
ferulic acid
-
-
Fluorescein 5'-isothiocyanate
-
fluorescein 5'-isothiocyanate modified enzyme has 0.5-1.5% residual ATPase activity compared to the unmodified enzyme
gallic acid
-
-
gentisic acid
-
-
ginger hydrolysed phenolic fraction
-
of ginger, Zingiber officinale, rhizome, constituted by cinnamic (48%), 4-coumaric (34%) and caffeic (6%) acids as major phenolic acids, as potent inhibitors of gastric cell proton potassium ATPase activity and Helicobacter pylori growth, exhibiting strong antioxidant potency, overview
-
ginger-free phenolic fraction
-
the fraction is constituted by syringic (38%), gallic (18%) and cinnamic (14%) acids, as potent inhibitors of gastric cell proton potassium ATPase activity and Helicobacter pylori growth, exhibiting strong antioxidant potency, overview
-
imidazopyridine
-
-
jacareubin
-
a xanthone isolated from Calophyllum brasiliense leaves
K+
-
activates, required. But in the presence of 200m M KCl, ion binding sites are more than 99% saturated with K+. The enzyme activity under this condition is near zero
lansoprazole
Li+
-
-
lonchocarpin
-
a chalcone isolated from Lonchocarpus guatemalensis roots
luteolin
magnesium fluoride
reversible inhibition by the fluorinated phosphate analogue, activity is restored by divalent cations, e.g. Mg2+
mammea A/BA
-
a coumarin isolated from Calophyllum brasiliense leaves
mammea C/OA
-
a coumarin isolated from Calophyllum brasiliense leaves
methyl {[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}acetate
-
-
minimiflorin
-
a flavonoid isolated from Lonchocarpus oaxacensis roots
Mn2+
-
in presence of Mg2+
mundulin
-
a flavonoid isolated from Lonchocarpus oaxacensis roots
N,N'-dicyclohexylcarbodiimide
N,N'-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
-
N-(2,6-dimethylbenzyl)-3-(4,5-dimethyl-1H-imidazol-2-yl)aniline
-
-
N-(2-ethyl-6-methylbenzyl)-2,3-dimethyl-6-(pyrrolidin-1-ylcarbonyl)imidazo[1,2-a]pyrazin-8-amine
-
-
N-(2-ethyl-6-methylbenzyl)-6-(methoxymethyl)-2,3-dimethylimidazo[1,2-a]pyrazin-8-amine
-
-
N-methyl-BYK36399
N-[3-(4,5-dimethyl-1H-imidazol-2-yl)phenyl]-2,6-dimethylaniline
-
-
N-[3-(4,5-dimethyl-1H-imidazol-2-yl)phenyl]benzamide
-
-
oligomycin
Omeprazole
ouabagenin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
Ouabain
oubain
P-CAB1
-
-
p-chloromercuribenzene sulfonate
pantoprazole
proscillaridin A
-
-
protocatechuic acid
-
-
rabeprazole
SCH 28080
SCH 32651
-
-
SCH28080
Sr2+
-
-
strophanthidin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
syringic acid
-
-
timoprazole
trimethyltin chloride
-
i.e. TMT, trimethyltin chloride directly inhibits the activity of H+/K+-ATPases in renal intercalated cells reducing urine K+ reabsorption and inducing hypokalemia. It increases potassium leakage from the kidney, raises urine pH, and inhibits H+/K+-ATPase activity both in vitro and in vivo. In toxicated rats, H+/K+-ATPase activity is positively correlated with the decrease of plasma K+ and blood pH but is negatively correlated with the increase of urine K+ and urine pH, while trimethyltin chloride does not change the expression of H+/K+-ATPase protein and mRNA
Trypsin
-
vanadate
[(dihydroindenyl)oxy]acetic acid
-
DIOA
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
activates NTPase activity of the enzyme
indomethacin
-
activates by 65%
SC-560
-
i.e. 5-(4-chlorophenyl)-1-(4-methyoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole, activates by 61%
valinomycin
-
increases ATPase activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0245 - 1.2
ATP
0.3 - 20
K+
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.093
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
-
pH 7.4, 37°C
0.064
Ouabain
-
pH 7.4, 37°C
0.000028 - 0.00615
SCH28080
additional information
additional information
-
Ki-values of about 0.001 mM: bufalin, proscillaridin A. Digoxin and digitoxin show Ki-values of about 0.01 mM on ATPase reaction and of about 0.005 mM on phosphatase activity
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.171
(2E)-1-(5-hydroxy-2,2-dimethyl-2H-chromen-6-yl)-3-phenylprop-2-en-1-one
Canis lupus familiaris
-
pH 7.4, 37°C
0.0059
(8-[(2-ethyl-6-methylbenzyl)amino]-2,3-dimethylimidazo[1,2-a]pyrazin-6-yl)methanol
Sus scrofa
-
pH 7.4, 22°C
0.173
1,3,5,6-tetrahydroxy-2-(3-hydroxy-3-methylbutyl)-xanthone
Canis lupus familiaris
-
pH 7.4, 37°C
1.605
1-hydroxy-3,5,6-tri-O-acetyl-2(3,3-dimethyl-allyl)-xanthone
Canis lupus familiaris
-
pH 7.4, 37°C
0.04
4-coumaric acid
Ovis aries
-
pH 6.5, 37°C
1.581
6-desoxyjacareubin
Canis lupus familiaris
-
pH 7.4, 37°C
0.0055
8-[(2-ethyl-6-methylbenzyl)amino]-N,2,3-trimethylimidazo[1,2-a]pyrazine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0064
8-[(2-ethyl-6-methylbenzyl)amino]-N,N,2,3-tetramethylimidazo[1,2-a]pyrazine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.005
8-[(2-ethyl-6-methylbenzyl)amino]-N-(2-hydroxyethyl)-2,3-dimethylimidazo[1,2-a]pyrazine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.006
8-[(2-ethyl-6-methylbenzyl)amino]-N-(2-methoxyethyl)-2,3-dimethylimidazo[1,2-a]pyrazine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0048
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-2,3-dimethylimidazo[1,2-a]pyridine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0053
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-N,2,3-trimethylimidazo[1,2-a]pyridine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0063
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0047
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-N-(1-methoxyethyl)-2,3-dimethylimidazo[1,2-a]pyridine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0057
8-[[(1S,2S)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]oxy]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0057
8-[[(1S,2S)-2-hydroxy-7-methoxy-2,3-dihydro-1H-inden-1-yl]oxy]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0069
8-[[(1S,2S)-2-hydroxy-7-methyl-2,3-dihydro-1H-inden-1-yl]oxy]-N,N,2,3-tetramethylimidazo[1,2-a]pyridine-6-carboxamide
Sus scrofa
-
pH 7.4, 22°C
0.0062
AR-HO47108
Sus scrofa
-
pH 7.4, 22°C
0.0027
caffeic acid
Ovis aries
-
pH 6.5, 37°C
0.015
Cinnamic acid
Ovis aries
-
pH 6.5, 37°C
0.00075
digoxigenin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.00076
digoxin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.027
dihydro-ouabain
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.034
ferulic acid
Ovis aries
-
pH 6.5, 37°C
0.132
gallic acid
Ovis aries
-
pH 6.5, 37°C
0.059
gentisic acid
Ovis aries
-
pH 6.5, 37°C
0.0015
ginger hydrolysed phenolic fraction
Ovis aries
-
pH 6.5, 37°C
-
0.0029
ginger-free phenolic fraction
Ovis aries
-
pH 6.5, 37°C
-
0.0467
jacareubin
Canis lupus familiaris
-
pH 7.4, 37°C
0.0193
lansoprazole
Ovis aries
-
pH 6.5, 37°C
0.03
luteolin
0.1095
mammea A/BA
Canis lupus familiaris
-
pH 7.4, 37°C
0.638
mammea C/OA
Canis lupus familiaris
-
pH 7.4, 37°C
0.0096
minimiflorin
Canis lupus familiaris
-
pH 7.4, 37°C
0.07
mundulin
Canis lupus familiaris
-
pH 7.4, 37°C
0.0069
N-(2-ethyl-6-methylbenzyl)-2,3-dimethyl-6-(pyrrolidin-1-ylcarbonyl)imidazo[1,2-a]pyrazin-8-amine
Sus scrofa
-
pH 7.4, 22°C
0.0055
N-(2-ethyl-6-methylbenzyl)-6-(methoxymethyl)-2,3-dimethylimidazo[1,2-a]pyrazin-8-amine
Sus scrofa
-
pH 7.4, 22°C
0.003
oligomycin
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM NH4+, or 10 mM K+, or 100 mM Na+
0.41
Omeprazole
Canis lupus familiaris
-
pH 7.4, 37°C
0.0028
ouabagenin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.00031 - 0.0017
Ouabain
0.06 - 8
oubain
0.047
protocatechuic acid
Ovis aries
-
pH 6.5, 37°C
0.02 - 4
SCH 28080
0.0059
SCH 32651
Sus scrofa
-
pH 7.4, 22°C
0.00041
SCH28080
Oryctolagus cuniculus
-
IC50: 0.00041 mM for wild-type enzyme
0.00017
strophanthidin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.037
syringic acid
Ovis aries
-
pH 6.5, 37°C
0.0008 - 0.0016
vanadate
0.097
[(dihydroindenyl)oxy]acetic acid
Sus scrofa
-
endogenous Na+,K+-ATPase
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.07
-
native ouabain-insensitive H+/K+-ATPase from colonic apical plasma membranes, pH not specified in the publication, temperature not specified in the publication
0.186
-
partially purified recombinant enzyme, in presence of 10 mM K+
0.544
-
native ouabain-sensitive H+/K+-ATPase from colonic apical plasma membranes, pH not specified in the publication, temperature not specified in the publication
0.611
-
partially purified recombinant enzyme, in presence of 100 mM Na+
0.626
-
ATP hydrolysis in presence of 10 mM K+ and 0.003 mM valinomycin
0.641
-
ATP hydrolysis in presence of 10 mM K+, 0.1 mM ADP, and 0.003 mM valinomycin
0.685
-
partially purified recombinant enzyme, in presence of 10 mM NH4+
2.045
-
purified native ouabain-sensitive H+/K+-ATPase, pH not specified in the publication, temperature not specified in the publication
2.383
-
in the presence of 2 mM K+, with ATP as substrate, at 37°C
6.3
-
purified enzyme, 40 mM HEPES/Tris, 10 mM KCl, 2 mM MgCl2, 25 mM sucrose, 0.1 mM EGTA/Tris, 2 mM ATP/Tris pH 7.0, at 37°C
7.5
-
purified enzyme, 40 mM HEPES/Tris, 10 mM KCl, 2 mM MgCl2, 25 mM sucrose, 0.1 mM EGTA/Tris, 2 mM ATP/Tris pH 7.0, at 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8
-
remarkable reduction in acidification of anterior prostate fluids from 6.38 for wild-type to 6.96 for homozygous mutants
6.5
-
assay at
6.6 - 7.4
-
the optimal pH for the ouabain-sensitive ATPase activity in the presence of K+ is pH 7.4, while the optimum pH for this activity, in the absence of K+, is pH 6.6
7.2 - 7.3
-
assay at
7.2
-
assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
at pH 6.5 30% and at pH 8.5 less than 1% of all binding sites are occupied by H+ ions
6.8 - 7.8
-
pH 6.8: about 60% of maximal activity, pH 7.8: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
limbic system and cerebellum
Manually annotated by BRENDA team
-
expressed both at transcript and protein levels
Manually annotated by BRENDA team
-
tubulovesicle membranes, H+,K+-ATPase is the most representative protein with 85%
Manually annotated by BRENDA team
enzyme expression 2.39fold greater in freshwater-acclimated stingrays than seawater stringrays
Manually annotated by BRENDA team
-
LLC-PK1 cells stably expressing alpha- and beta subunits of the gatric H+,K+-ATPase
Manually annotated by BRENDA team
-
ATP12A mRNA is expressed at different levels in PC-3 and LNCaP prostate cancer cells, with 26fold higher expression in the latter cell type
Manually annotated by BRENDA team
-
ATP12A mRNA is expressed at different levels in PC-3 and LNCaP prostate cancer cells, with 26fold higher expression in the latter cell type
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme expression 39% of that in microvillus detected by Western blot analysis, not detectable by immunocytochemistry
Manually annotated by BRENDA team
-
mutated H+,K+-ATPase alpha/beta1 subunit complex
Manually annotated by BRENDA team
-
and throughout the cis to trans Golgi in resting parietal cells
Manually annotated by BRENDA team
-
labeling density of H+/K+-ATPase is 4fold higher on the intracellular canliculi membrane of histamine stimulated parietal cells than on that of resting parietal cells, in cimetidine-treated glands on the apical microvillar membranes of intracellular canliculi
Manually annotated by BRENDA team
-
in resting parietal cells
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33625
-
x * 33625, calculation from nucleotide sequence
70000
-
x * 70000, beta-subunit ATP4B, SDS-PAGE
94000
-
x * 94000 (alpha) + x * ? (beta), SDS-PAGE
100000
114000
-
Western blot analysis
115000
-
x * 115000, subunit HKalpha1, SDS-PAGE
147346
-
1 * 147346, calculated from amino acid sequence
500000
-
1 * 100000, alpha-subunit, + 1 * 500000, beta-subunit, alpha/beta, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
monomer
-
1 * 147346, calculated from amino acid sequence
oligomer
-
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AlFxADP bound enzyme form, beta-octyl glycoside-solubilized enzyme from SDS-purified membranes by 2D crystallization, dialysis for 12 h to 2 days in presence of Mg2+, glycerol and/or propionate in different compositions, structure determination and analysis by cryoelectron microscopy of the 2D samples, resolution of 14 A
-
three-dimensional structure of negatively stained crystals
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP protects against inactivation by detergents
-
solubilization at pH 4.0 causes rapid loss of ATPase activity, probably due to an increased protease activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified enzyme, loss of over 90% activity without additive, 65% activity remaining with 25% added, over 95% remaining with addtion of 10% DMSO
-
-80°C, EGTA/Tris buffer, pH 7.4
-
-80°C, in glycerol containing buffer, stable for more than 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by SDS-PAGE
-
native enzyme partially by preparation of enzyme-containing membranes
-
native enzyme partially by purification of plama membranes from parietal cells
-
native gastric H+,K+-ATPase partially by enzyme-enriched membrane vesicle preparation using SDS or/and beta-octyl glycoside
-
native gastric H,K-ATPase from gastric mucosa by a method involving differential and density gradient centrifugation, e.g. sucrose step gradient centrifugation, and plasma vesicle formation oriented as in the parietal cell with the cytoplasmic side outward
-
native ouabain-sensitive H+/K+-ATPase 106.5fold from isolated guinea-pig distal colon apical plasma membranes by solubilization with SDS, and discontinuous sucrose gradient centrifugation, separation from the ouabain-insensitive K+-ATPase
-
partially by preparation of enzyme-enriched microsomal vesicles
-
rapid purification by tomato-lectin affinity chromatography
-
recombinant non-gastric enzyme partially from Spodoptera frugiperda Sf9 cells by membrane preparation
-
recombinant wild-type and mutant enzymes partially from Xenopus laevis oocytes by plasma membrane preparation
-
Superose 6 column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-subunit
-
beta-subunit expressed in Xenopus laevis oocytes
-
catalytic subunit of the enzyme, in which several amino acids from Na,K-ATPase are incorporated, expressed with the Na,K-ATPase beta1 subunit in Xenopus laevis oocytes, expression of non-gastric H,K-ATPase-EGPLC and the Na,K-ATPase beta1-subunit in Sf9 cells using the baculovirus expression system
-
co-expression of wild-type and mutant beta- and alpha-subunits
-
efficient formation of the functional Atp1al1-betaHK complex in membranes of Sf-212-insect cells. Atp1al1-betaHK is a complex of the alpha-subunit of human nongastric H,K-ATPase with the gastric H,K-ATPase beta-subunit
-
expressed in Xenopus laevis oocytes
-
expression in HEK-293 cells
-
expression in Xenopus oocytes
-
expression of alpha-subunit of wild-type and mutant enzymes in Spodopera frugiperda Sf9 cell membranes using the baculovirus transfection system
-
expression of non-gastric enzyme in Spodoptera frugiperda Sf9 cells via baculovirus transfection, co-expression with the Rattus norvegicus beta1 subunit of Na,K-ATPase
-
expression of several chimeras between ATP1AL1 and the Na,K-ATPase in MDCK cells
expression of the beta-subunit and a modified form of the alpha-subunit with a single cysteine replacement in the TM5/TM6 extracellular loop, i.e. S806C, in Xenopus laevis oocytes
-
expression of the wild-type H,K-ATPase, alpha- and beta-subunits, and glycosylation-deficient Asn-to-Gln beta-mutants in Xenopus laevis oocytes
-
expression of wild-type and mutant enzymes in HEK-293 cells, expression analysis, overview
-
functional expression of the HKalpha2 subunit in human HEK-293 cells, human GPR4 is transiently transfected into HEK-293 cells stably expressing HKalpha2/NKbeta1, expression levels under different conditions by realtime PCR expression analysis
-
gene HKalpha2, the -144/-135 element is important for HKalpha2 promoter activity, regulation of gene expression and interaction with Sp1 protein, expression analysis, overview
-
into pcDNA3.1(+)-Neo, cotransfection of HEK-293 cells with H+,K+-ATPase alpha subunit plus Na+,K+-ATPase beta1 subunit or beta3 subunit, respectively
-
into pcDNA3.1(+)-Neo, expression in HEK-293 cells, mutant cloned into pEGFP-2C vector
-
overexpression in Sf-21 cells as a control
-
regulation of colonic HKalpha2 transcription and expression, overview
-
transfection of Saccharomyces cerevisiae AH109 with pGBKT7 containing an insert encoding the 84 carboxy-terminal acids of HKalpha2, cotransfection of HEK-293 cells with HKalpha2 plus NKbeta1