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Information on EC 7.2.2.19 - H+/K+-exchanging ATPase
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7.2.2.19 H+/K+-exchanging ATPaseIUBMB Comments
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.
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Word Map
- 7.2.2.19
-
parietal
- mucosa
- omeprazole
- stomach
- na,k-atpase
- alpha-subunits
- ulcer
- histamine
- beta-subunits
- helicobacter
- atpases
- gastritis
- pylori
- gastrin
-
antisecretory
-
basolateral
-
tubulovesicles
- reflux
- benzimidazole
- lansoprazole
-
oxyntic
- fundic
-
histamine-stimulated
- pepsinogen
-
k+-stimulated
-
pernicious
- cimetidine
-
k+-dependent
-
acid-related
-
h2-receptor
-
antiulcer
- rabeprazole
- pentagastrin
-
h-atpase
- phosphoenzyme
-
acid-secreting
-
tubulovesicular
-
hypergastrinemia
-
gastroprotective
-
bcecf
- ranitidine
-
canaliculus
-
ouabain-insensitive
-
pylorus-ligated
-
ion-transporting
- achlorhydria
-
thymectomy
- hypochlorhydria
- pharmacology
- medicine
-
14caminopyrine
-
zollinger-ellison
The enzyme appears in viruses and cellular organisms
Synonyms
h,k-atpase, h+,k+-atpase, h+/k+-atpase, h(+),k(+)-atpase, h-k-atpase, h+-k+-atpase, gastric proton pump, gastric h,k-atpase, h+/k+ atpase, atp4a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(H++K+)-ATPase
-
-
-
-
Atp12a
ATP1al1
EC 3.6.1.36
-
-
formerly
-
EC 3.6.3.10
-
-
formerly
-
electroneutral H+/K+-ATPase
gastric H+,K+-ATPase
gastric H+/K+-ATPase
gastric H,K-ATPase
gastric HK-ATPase
H+, K+-ATPase
H+,K+-adenosine triphosphatase
H+,K+-ATPase
H+-K+-adenosinetriphosphatase
-
-
-
-
H+-K+-ATPase
H+/K+-ATPase
H,K-ATPase
HKA
HKalpha1
HKalpha2
non-gastric H,K-ATPase
nongastric H,K-ATPase
Proton pump
-
-
-
-
additional information
H+-K+-ATPase
-
-
-
-
H,K-ATPase
-
-
-
-
additional information
-
the enzyme is a member of the P2-type ATPase family
additional information
-
the enzyme is a member of the P2-type ATPase family
additional information
-
the enzyme is a member of the P2-type ATPase family
additional information
-
the enzymes belong to the X+,K+-ATPase superfamily
additional information
the enzyme belongs to the the cation-transporting P-type ATPase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
mechanistic modeling of the physiological events linking subcellular processes to largescale patterning involving the enzyme
-
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
mechanistic modeling of the physiological events linking subcellular processes to largescale patterning involving the enzyme
-
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview
-
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview
-
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview
-
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview
-
ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type,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.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyATP + H2O + H+/in + K+/out
2'-deoxyADP + phosphate + H+/out + K+/in
-
70% of the activity with ATP
-
-
?
2'-deoxyATP + H2O + H+/in + K+/out
2'-deoxyADP + phosphate + H+/out + K+/in
-
37% of the activity with ATP
-
-
?
ADP + H2O + H+/in + K+/out
AMP + phosphate + H+/out + K+/in
-
14% of the activity with ATP
-
-
?
ADP + H2O + H+/in + K+/out
AMP + phosphate + H+/out + K+/in
-
7.5% of the activity with ATP
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
a Na+-independent, ouabain-sensitive H+/K+-exchange. K+ can be replaced by H+ in the enzyme reaction cycle, however pH-induced conformational changes cannot be discarded
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the known requirement for H+/K+-ATPase function in chick asymmetry does not function through effects on the circumferential expression pattern of Connexin43, physiological function, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
H+,K+-ATPase family of ion pumps is an essential component of the kidneys K+ and H+ transporting machinery, under normal circumstances as well as during adaption to physiological stress
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
isoform HKalpha(1) and HKalpha(4) are present in the collecting ducts of the human kidney and might contribute to H+ and K+ transport by the kidney
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the enzyme can function as Na/K exchanger
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
K+-Cl- cotransporter KCC4 and H+,K+-ATPase are the main machineries for basal HCl secretion in the apical canalicular membrane of the resting parietal cell, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
it is also involved in maintainance of chronic metabolic alkalosis due to upregulation in hypokalemia, regulation of colonic HKalpha2 transcription and expression, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H+/K+-ATPase alpha2 gene of renal collecting duct and distal colon plays a central role in potassium and acid-base homeostasis, regulation, overview. Sp1 plays an important and positive role in controlling basal HKalpha2 gene expression in mIMCD3 cells in vivo and in vitro
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
involved in urinary acidification
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
acid-secretory role of the enzyme is coupled to K+ movement, enzyme activity is increased under conditions of chronic metabolic acidosis
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
gastric H,K-ATPase is an electroneutral transmembrane pump that moves protons from the cytoplasm of the parietal cell into the gastric lumen in exchange for potassium ions. The mechanism of transport against the established electrochemical gradients includes intermediate conformations in which the transferred ions are trapped within the membrane domain of the pump. The pump cycle involves switching between the E1 and E2P states. Molecular dynamics simulations on homology models of the E2P and E1 states amd K+ transport mechanism, overview. Movement of the M1M2 transmembrane segments, and the displacement of residues Q159, E160, Q110, and T152 during the conformational change, as well as the motions of E343 and L346, acted as the cytoplasmic-side gate
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the enzyme is involved in acid secretion in gastric mucosa
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
involved in urinary acidification
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
ir
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the enzyme could contribute to potassium and pH i regulation in cardiomyocytes
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the enzyme participates in K+ absorption and H+ secretion in the renal medulla, it is highly regulated in response to acid-base and electrolyte disturbances, colonic HKalpha2 plays a role in K+ and acid-base homeostasis as well as in early growth and development, it is also involved in maintainance of chronic metabolic alkalosis due to upregulation in hypokalemia, regulation of colonic HKalpha2 transcription and expression, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
cation binding sites in the transmembrane domains TM42 to TM6, E2-conformation-specific salt bridge between the side chains of Lys791 in TM5 and Glu820 in TM6 of the cation binding pocket
-
-
ir
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
protons are charge-transferred from the enzyme's alpha-subunit cytosolic side to H2O in sites 2 and 1, the H2O comes from cytosolic medium, and H3O+ in the sites are transported into lumen during the conformational transition from E1P to E2P, charge transfer pathway charge transfer pathway from hydronium ion in cytosolic medium to Glu345 in cation binding site 2: H3O+-Lys164-Gln161-Glu345
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
the electroneutral exchange of two cytoplasmic protons for two luminal potassium ions is achieved by the hydrolysis of one ATP molecule
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
The second ion species that can bind to the H,K-ATPase in the E1 conformation is K+ that competes with H+. Experimental activity measurement begins with the ion pump in the E1 state after treatment with nigericin
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
Turtle
-
primary role may be in active potassium reabsorption
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the Kir4.1 potassium channel, while symmetrically expressed in a dynamic fashion during early cleavages, is required for normal LR asymmetry of frog embryos. Thus, Kir4.1 is an ideal candidate for the K+ ion exit path needed to allow the electroneutral H+/K+-ATPase to generate voltage gradients, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H+,K+-ATPase is electroneutral, exchanging two positive charges in each cycle
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
?
CTP + H2O + H+/in + K+/out
CDP + phosphate + H+/out + K+/in
-
a Na+-independent, ouabain-sensitive H+/K+-exchange, low activity with CTP
-
-
?
CTP + H2O + H+/in + K+/out
CDP + phosphate + H+/out + K+/in
-
20% of the activity with ATP
-
?
CTP + H2O + H+/in + K+/out
CDP + phosphate + H+/out + K+/in
-
13.2% of the activity with ATP
-
-
?
GTP + H2O + H+/in + K+/out
GDP + phosphate + H+/out + K+/in
-
a Na+-independent, ouabain-sensitive H+/K+-exchange, low activity with GTP
-
-
?
GTP + H2O + H+/in + K+/out
GDP + phosphate + H+/out + K+/in
-
6% of the activity with ATP
-
?
ITP + H2O + H+/in + K+/out
IDP + phosphate + H+/out + K+/in
-
a Na+-independent, ouabain-sensitive H+/K+-exchange, low activity with ITP
-
-
?
ITP + H2O + H+/in + K+/out
IDP + phosphate + H+/out + K+/in
-
5% of the activity with ATP
-
?
UTP + H2O + H+/in + K+/out
UDP + phosphate + H+/out + K+/in
-
a Na+-independent, ouabain-sensitive H+/K+-exchange, low activity with UTP
-
-
?
UTP + H2O + H+/in + K+/out
UDP + phosphate + H+/out + K+/in
-
40% of the activity with ATP
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the enzyme is phosphorylated from [32P]-gamma-ATP, forming an acyl-phosphate bond, in an Mg2+-dependent, vanadate-sensitive process
-
-
?
additional information
?
-
-
the enzyme can transport Na+ in exchange for K+
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the K+-Cl- cotransport by KCC4 is tightly coupled with H+/K+ antiport by H+,K+-ATPase
-
-
?
additional information
?
-
-
the Atp1al1-betaHK complex exhibits significant ATPase activity in nominally K+-free medium. The addition of K+ stimulates the ATPhydrolysis up to 3fold
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the enzyme is involved in acid secretion from gastric mucosa, overview
-
-
?
additional information
?
-
-
the H+-K+-ATPase is associated with the sonic hedgehog protein in membranes of gastric parietal cells. Stimulation of acid secretion in parietal cells is characterized by a change in the distribution of the H+-K+-ATPase fron the P3 microsomal membrane fraction to the P1 plasma membrane fraction, mechanism, overview
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the enzyme is involved in acid secretion from gastric mucosa, overview
-
-
?
additional information
?
-
activity tests of the recombinantly expressed enzyme by Rb+ uptake measurements, and voltage clamp fluorometry for site-specific labeling of H,KATPase-expressing TMRM-labeled oocytes
-
-
?
additional information
?
-
-
enzyme behaves as a passive cationic antiport in the absence of ATP
-
-
?
additional information
?
-
-
enzyme reconstituted into artificial phosphatidylcholine/cholesterol vesicles catalyzes an electroneutral H+-Rb+ exchange
-
-
?
additional information
?
-
-
the enzyme also performs K+-dependent NTP hydrolysis, utilizing ATP, GTP, CTP, UTP, and ITP, and an NTP/ADP exchange reaction, overview
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the potassium channel KCNQ1, a 6-transmembrane member of the K+ channel family, provides an exit path for K+ ions brought in by the H+,K+-ATPase, overview. The KCNQ1 channel is also required for gastric acid secretion, where it works together with the H+/K+-ATPase
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the known requirement for H+/K+-ATPase function in chick asymmetry does not function through effects on the circumferential expression pattern of Connexin43, physiological function, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
H+,K+-ATPase family of ion pumps is an essential component of the kidneys K+ and H+ transporting machinery, under normal circumstances as well as during adaption to physiological stress
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
isoform HKalpha(1) and HKalpha(4) are present in the collecting ducts of the human kidney and might contribute to H+ and K+ transport by the kidney
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
K+-Cl- cotransporter KCC4 and H+,K+-ATPase are the main machineries for basal HCl secretion in the apical canalicular membrane of the resting parietal cell, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
it is also involved in maintainance of chronic metabolic alkalosis due to upregulation in hypokalemia, regulation of colonic HKalpha2 transcription and expression, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H+/K+-ATPase alpha2 gene of renal collecting duct and distal colon plays a central role in potassium and acid-base homeostasis, regulation, overview. Sp1 plays an important and positive role in controlling basal HKalpha2 gene expression in mIMCD3 cells in vivo and in vitro
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
involved in urinary acidification
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
acid-secretory role of the enzyme is coupled to K+ movement, enzyme activity is increased under conditions of chronic metabolic acidosis
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
gastric H,K-ATPase is an electroneutral transmembrane pump that moves protons from the cytoplasm of the parietal cell into the gastric lumen in exchange for potassium ions. The mechanism of transport against the established electrochemical gradients includes intermediate conformations in which the transferred ions are trapped within the membrane domain of the pump. The pump cycle involves switching between the E1 and E2P states. Molecular dynamics simulations on homology models of the E2P and E1 states amd K+ transport mechanism, overview. Movement of the M1M2 transmembrane segments, and the displacement of residues Q159, E160, Q110, and T152 during the conformational change, as well as the motions of E343 and L346, acted as the cytoplasmic-side gate
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the enzyme is involved in acid secretion in gastric mucosa
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
involved in urinary acidification
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
ir
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the enzyme could contribute to potassium and pH i regulation in cardiomyocytes
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the enzyme participates in K+ absorption and H+ secretion in the renal medulla, it is highly regulated in response to acid-base and electrolyte disturbances, colonic HKalpha2 plays a role in K+ and acid-base homeostasis as well as in early growth and development, it is also involved in maintainance of chronic metabolic alkalosis due to upregulation in hypokalemia, regulation of colonic HKalpha2 transcription and expression, overview
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the H,K-ATPase is the final step of acid secretion
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
the electroneutral exchange of two cytoplasmic protons for two luminal potassium ions is achieved by the hydrolysis of one ATP molecule
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
Turtle
-
primary role may be in active potassium reabsorption
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
-
the Kir4.1 potassium channel, while symmetrically expressed in a dynamic fashion during early cleavages, is required for normal LR asymmetry of frog embryos. Thus, Kir4.1 is an ideal candidate for the K+ ion exit path needed to allow the electroneutral H+/K+-ATPase to generate voltage gradients, overview
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
?
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
-
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the K+-Cl- cotransport by KCC4 is tightly coupled with H+/K+ antiport by H+,K+-ATPase
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the enzyme is involved in acid secretion from gastric mucosa, overview
-
-
?
additional information
?
-
-
the H+-K+-ATPase is associated with the sonic hedgehog protein in membranes of gastric parietal cells. Stimulation of acid secretion in parietal cells is characterized by a change in the distribution of the H+-K+-ATPase fron the P3 microsomal membrane fraction to the P1 plasma membrane fraction, mechanism, overview
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the enzyme is involved in acid secretion from gastric mucosa, overview
-
-
?
additional information
?
-
-
a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion
-
-
?
additional information
?
-
-
the potassium channel KCNQ1, a 6-transmembrane member of the K+ channel family, provides an exit path for K+ ions brought in by the H+,K+-ATPase, overview. The KCNQ1 channel is also required for gastric acid secretion, where it works together with the H+/K+-ATPase
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cs+
H3O+
binds to the E1 conformation of the alpha-subunit of gastric proton pump, interaction similar to K+ interaction
K+
Mg2+
Na+
NH4+
Rb+
Tl+
additional information
Cs+
-
activates, Km: 1.25 mM, monovalent cations stimulate in the order of decreasing efficacy: Tl+, K+, Rb+, NH4+, Cs+
K+
-
activates, activation by K+ is independent of the accompanying anion, obtaining maximal activity at about 0.5 mM and pH 7.4, Km is 1.9 mM, not effective at pH 6.6
K+
-
maximum activation at 5-10 mM, Km: 0.34 mM, monovalent cations stimulate in the order of decreasing efficacy: Tl+, K+, Rb+, NH4+, Cs+
K+
-
activates, with 0.11 mM as half saturating K+ concentration for both luminal binding sites, above 10 mM reduction of enzyme activity
K+
-
stabilizes both oligomeric assembly and enzyme activity in C12E8-solubilized gastric H/K-ATPase, 20-40 mM protects
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
Mg2+
-
dependent on, optimally at 5 mM, Km is 3.4 mM or 0.5 mM with optimal ATP concentration
NH4+
-
activates, Km: 3.64 mM, monovalent cations stimulate in the order of decreasing efficacy: Tl+, K+, Rb+, NH4+, Cs+
Rb+
-
activates, Km: 0.43 mM, monovalent cations stimulate in the order of decreasing efficacy: Tl+, K+, Rb+, NH4+, Cs+
Rb+
-
uptake supported by both H+,K+-ATPase alpha subunit-Na+,K+-ATPase beta1 subunit complex or beta3 subunit complex, respectively, higher uptake in cells with H+,K+-ATPase alpha subunit-Na+,K+-ATPase beta1 subunit complex
Tl+
-
activates, Km: 0.03 mM, monovalent cations stimulate in the order of decreasing efficacy: Tl+, K+, Rb+, NH4+, Cs+
additional information
-
H+/K+-ATPase is Na+-independent, Mg2+-dependent, and activated by K+, Rb+, Cs+, and NH4 + but not by Na+, Li+, or N-methyl-glucamine
additional information
-
no protective effect during C12E8-solubilization of gastric H/K-ATPase by Na+ and Li+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(7R,8R,9R)-2,3,10-trimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol
-
(7R,8R,9R)-2,3-dimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol
high-affinity K+-competitive inhibitor
(8-[(2-ethyl-6-methylbenzyl)amino]-2,3-dimethylimidazo[1,2-a]pyrazin-6-yl)methanol
-
-
(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-hydroxy-3,5,6-tri-O-acetyl-2(3,3-dimethyl-allyl)-xanthone
-
a xanthone isolated from Calophyllum brasiliense leaves
2-[(4-[4-[4-(azidomethyl)phenoxy]butoxy]-3-methylpyridin-2-yl)methanesulfinyl]-1H-benzimidazole
inhibits ATPase activity by approximately 50% at 0.01 mM
2-[5-(2,6-dimethylphenyl)-2,3-dihydro-1-benzofuran-7-yl]-4,5-dimethyl-1H-imidazole
-
-
2-{[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}acetamide
-
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'-(3,4,5-trihydroxybenzylidene)propanehydrazide
-
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'-(3,4,5trimethoxybenzylidene)propanehydrazide
-
-
3-({[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}methyl)pyridine
-
-
4-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'(3,4,5trimethoxybenzylidene)butanehydrazide
-
-
4-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'-(3,4,5-trihydroxybenzylidene)butanehydrazide
-
-
4-([2-[(1H-benzimidazole-2-sulfinyl)methyl]-3-methylpyridin-4-yl]oxy)butyl [4-(1,2,4,5-tetrazin-3-yl)phenyl]acetate
inhibits ATPase activity by approximately 50% at 0.01 mM
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
-
-
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
BYK73
i.e. (7R,8R,9R)-2,3,10-trimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol
BYK99
i.e. (7R,8R,9R)-2,3-dimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol, high-affinity K+-competitive inhibitor
clotrimazole
-
molecular mechanism of the inhibitory effect is studied by steady-state fluorescence experiments with the electrochromic styryl dye RH421
digoxigenin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
dihydro-ouabain
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
Fluorescein 5'-isothiocyanate
-
fluorescein 5'-isothiocyanate modified enzyme has 0.5-1.5% residual ATPase activity compared to the unmodified enzyme
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
-
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
lonchocarpin
-
a chalcone isolated from Lonchocarpus guatemalensis roots
magnesium fluoride
reversible inhibition by the fluorinated phosphate analogue, activity is restored by divalent cations, e.g. Mg2+
methyl {[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}acetate
-
-
minimiflorin
-
a flavonoid isolated from Lonchocarpus oaxacensis roots
N'-(2,3-dibromobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
-
-
N'-(2,3-dibromobenzyliden)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-(2,4-dichlorobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
-
-
N'-(2,4-dichlorobenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-(2,4-difluorobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
-
-
N'-(2,4-difluorobenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-(2-chloro-6-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)butane hydrazide
-
-
N'-(2-chloro-6-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
-
-
N'-(2-fluoro-5-nitrobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
-
-
N'-(2-fluoro-5-nitrobenzyliden)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-(3,4-dihydroxy-5-methoxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
N'-(3,4-dihydroxy-5-methoxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-(4-hydroxy-3-methoxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
N'-(4-hydroxy-3-methoxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl) butanehydrazide
-
-
N'-(4-hydroxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
N'-(4-methoxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
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
-
-
ouabagenin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
potato galactan polysaccharide
-
potent inhibitory activity with an IC50 value of 0.42 mg/ml in vitro
-
strophanthidin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
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
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
-
i.e. SCH28080
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
-
i.e. SCH28080
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
-
i.e. SCH28080
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
-
i.e. SCH28080
aluminum fluoride
reversible inhibition by the fluorinated phosphate analogue, activity is restored by divalent cations, e.g. Mg2+. Structural comparison of H+,K+-ATPase in the E2BeF and E2AlF states, overview
Ba2+
-
is a known inhibitor of K+ channels, and completely inhibits the whole-cell currents
digoxin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
oligomycin
-
increases the phosphorylation of the enzyme and the sensitivity of the phosphorylated intermediate to AD inhibiting the conversion of E1P to E2P
Omeprazole
-
binding at Cys813 and Cys892 is reversible both in vivo and in vitro
Omeprazole
-
no effect in the presence of K+ alone or NH4+. Inhibitory action can be fully reversed by addition of beta-mercaptoethanol
Ouabain
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
oubain
-
binding affinity of wild-type is 2000fold lower than that of mutated enzyme in NH4+-stimulated Sf9 cells
SCH28080
-
i.e., 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
SCH28080
strictly competitive with respect to K+ or NH4+, binds near the M5-6 luminal loop, preventing K+ access to the ion binding domain
SCH28080
low concentrations decrease phosphorylation levels of mutants with an E2 preference, whereas it hardly changes with E1-prefering mutants, even increases phosphorylation levels in the E820Q mutant
SCH28080
a K+-competitive inhibitor, SCH28080 is specific for both E2 and E2P conformations
SCH28080
i.e., 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
SCH28080
i.e. 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
Trypsin
-
limited proteolysis, determination of peptide fragment sequences, overview
-
additional information
-
H+/K+-ATPase inhibition does not affect Cx43 expression in chicken
-
additional information
-
chlorofom extract of Baccharis illinita flowers inhibits the H+-K+-ATPase and gastric acid secretion in rabbit stomach, no inhibition by naringenin and kaempferol
-
additional information
-
determination of minimal inhibitory concentration, MIC, values
-
additional information
-
chlorofom extract of Baccharis illinita flowers inhibits the H+-K+-ATPase and gastric acid secretion in rat stomach
-
additional information
-
wild-type non-gastric H,K-ATPase shows a very low affinity for ouabain
-
additional information
-
addition of trimethyltin chloride alters the whole-cell current and opens K+ channels in renal cells, overview
-
additional information
-
development of 6-substituted imidazo[1,2-a]pyrazines inhibitors of the gastric H+/K+-ATPase, no inhibition by 8-[(2-ethyl-6-methylbenzyl)amino]-2,3-dimethylimidazo[1,2-a]pyrazine-6-carboxamide
-
additional information
-
development of indanyl-substituted imidazo[1,2-a]pyridines as potent reversible inhibitors of the gastric H+/K+-ATPase, overview
-
additional information
-
pharmacophore modelling against known imidazopyridine and azaindole templates for detection and development of structure-based enzyme inhibitors, overview
-
additional information
mechanism, by which divalent cations, e.g. Mg2+, reactivate the fluorinated phosphate analogue-inhibited H+,K+-ATPase. Mg2+ interacts with the outside of the vesicles, namely the cytoplasmic side of the enzyme, overview. Prevention of the Mg2+-induced reactivation by K+ binding. The magnitude of the Mg2+-induced reactivation is highly pH dependent, whereas the BeF-inhibited enzyme is not affected
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SC-560
-
i.e. 5-(4-chlorophenyl)-1-(4-methyoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole, activates by 61%
NH4+
-
stimulates ATPase activity of non-gastric H,K-ATPase-EGPLC by 40% as compared to wild-type
additional information
-
Sp1 protein, a member of the Sp/Krüppel-like factor transcription factors. Sp1, but not Sp3, binds to this promoter region of the HKalpha2 gene in mIMCD3 cells in vivo and transactivates the gene expression. siRNA knockdown of Sp1 inhibits endogenous HKalpha2 mRNA expression
-
additional information
-
no activation by DFU, i.e. 5,5-dimethyl-3-(3-fluorophenyl)-4-(4-methylsulfonyl)phenyl-2-(5H)-furanone
-
additional information
-
upregulation of HKalpha2 protein is a robust phenomenon, induced by multiple means of decreasing extracellular pH. Critical role for PKA in the maturation and function of the H+-K+-ATPase alpha-subunit and H+-ATPase, a mechanism that involves phosphorylation at key serine residues
-
additional information
-
no protective effect during C12E8-solubilization of gastric H/K-ATPase by choline
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0245
ATP
-
pH 7.4, temperature not specified in the publication, with optimal concentration of ATP, Mg2+ and K+
0.0494
ATP
-
pH 7.0, temperature not specified in the publication, with optimal concentration of ATP, Mg2+ and K+
additional information
additional information
-
kinetics, wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics at different pH, overview
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0049
(7R,8R,9R)-2,3,10-trimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol
wild type enzyme, at pH 7.6 and 37°C
0.0015
(7R,8R,9R)-2,3-dimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol
wild type enzyme, at pH 7.6 and 37°C
0.093
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
-
pH 7.4, 37°C
0.0000058
8-(benzyloxy)-2-methylimidazo[1,2-a]pyridine
wild type enzyme, at pH 7.6 and 37°C
0.011
[8-(benzyloxy)-2-methylimidazo[1,2-a]pyridin-3-yl]acetonitrile
wild type enzyme, at pH 7.6 and 37°C
0.0032
[8-(benzyloxy)imidazo[1,2-a]pyridin-3-yl]acetonitrile
wild type enzyme, at pH 7.6 and 37°C
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
-
0.000151
SCH28080
pH 7.4, 37°C, mutant enzyme G918E and mutant enzyme Y922I
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
0.029
(7R,8R,9R)-2,3,10-trimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol
Sus scrofa
wild type enzyme, at pH 7.6 and 37°C
0.000077
(7R,8R,9R)-2,3-dimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol
Sus scrofa
wild type enzyme, at pH 7.6 and 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
0.015
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'-(3,4,5-trihydroxybenzylidene)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.022
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'-(3,4,5trimethoxybenzylidene)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.014
4-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'(3,4,5trimethoxybenzylidene)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.01
4-(4-oxo-3,4-dihydroquinazolin-2-yl)-N'-(3,4,5-trihydroxybenzylidene)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.11
8-(benzyloxy)-2-methylimidazo[1,2-a]pyridine
Sus scrofa
wild type enzyme, at pH 7.6 and 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
0.151
N'-(2,3-dibromobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.139
N'-(2,3-dibromobenzyliden)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.146
N'-(2,4-dichlorobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.131
N'-(2,4-dichlorobenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.18
N'-(2,4-difluorobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.169
N'-(2,4-difluorobenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.144
N'-(2-chloro-6-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)butane hydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.16
N'-(2-chloro-6-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.129
N'-(2-fluoro-5-nitrobenzyliden)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.142
N'-(2-fluoro-5-nitrobenzyliden)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.029
N'-(3,4-dihydroxy-5-methoxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.024
N'-(3,4-dihydroxy-5-methoxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.152
N'-(4-chlorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.134
N'-(4-chlorobenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.037
N'-(4-hydroxy-3-methoxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.032
N'-(4-hydroxy-3-methoxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl) butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.06
N'-(4-hydroxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.051
N'-(4-hydroxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.054
N'-(4-methoxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.041
N'-(4-methoxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.14
N'-(4-nitrobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.127
N'-(4-nitrobenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.21
N'-benzylidene-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.197
N'-benzylidene-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 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
0.16
N-(4-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)butane hydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.17
N-(4-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
Ovis aries
-
at pH 7.5 and 37°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+
0.00017
strophanthidin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.011
[8-(benzyloxy)-2-methylimidazo[1,2-a]pyridin-3-yl]acetonitrile
Sus scrofa
wild type enzyme, at pH 7.6 and 37°C
0.054
[8-(benzyloxy)imidazo[1,2-a]pyridin-3-yl]acetonitrile
Sus scrofa
wild type enzyme, at pH 7.6 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
0.544
-
native ouabain-sensitive H+/K+-ATPase from colonic apical plasma membranes, pH not specified in the publication, temperature not specified in the publication
0.641
-
ATP hydrolysis in presence of 10 mM K+, 0.1 mM ADP, and 0.003 mM valinomycin
2.045
-
purified native ouabain-sensitive H+/K+-ATPase, pH not specified in the publication, temperature not specified in the publication
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3 - 8
-
remarkable reduction in acidification of anterior prostate fluids from 6.38 for wild-type to 6.96 for homozygous mutants
6.6 - 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
6.8
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
246855, 246857, 246859, 246860, 246864, 654601, 656051, 675189, 696771, 697414, 699742, 700593, 734286
-
-
brenda
isozymes colonic HKalpha2, showing 3 splicing variants, and gastric HKalpha1
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
tubulovesicle membranes, H+,K+-ATPase is the most representative protein with 85%
brenda
enzyme expression 2.39fold greater in freshwater-acclimated stingrays than seawater stringrays
brenda
-
LLC-PK1 cells stably expressing alpha- and beta subunits of the gatric H+,K+-ATPase
brenda
-
ATP12A mRNA is expressed at different levels in PC-3 and LNCaP prostate cancer cells, with 26fold higher expression in the latter cell type
brenda
-
ATP12A mRNA is expressed at different levels in PC-3 and LNCaP prostate cancer cells, with 26fold higher expression in the latter cell type
brenda
additional information
-
isoform Hkalpha(1) and Hkalpha(4) are present in the collecting ducts of the human kidney
brenda
-
high activity in the late distal and collecting tubules, undetectable in the proximal convoluted tubule and early distal tubule
brenda
-
high activity in the late distal and collecting tubules, undetectable in the proximal convoluted tubule and early distal tubule
brenda
-
stimulation-associated vesicles of apical canalicular membrane
brenda
-
healthy, benign and malignant prostate tissue, ATP12A expression levels, overview
brenda
-
-
246848, 246854, 246865, 246866, 246868, 672636, 685586, 700593, 711245, 711398, 734202, 735163, 750685, 752233
brenda
-
secretion does not vary significantly along the longitudinal axis of the stomach
brenda
additional information
-
colonic HKalpha2 splicing variant colonic HKalpha2C is upregulated in newborn rats and undetectable in adult rats
brenda
additional information
-
chronic acidosis does not alter the expression of HKalpha2 mRNA, but PKA activity and HKalpha2 protein abundance increase when media pH decreases from pH 7.4 to pH 6.8
brenda
additional information
-
oxynticopeptic cells, not present in pyloric glands
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme expression 39% of that in microvillus detected by Western blot analysis, not detectable by immunocytochemistry
brenda
-
mutated H+,K+-ATPase alpha/beta1 subunit complex
brenda
-
and throughout the cis to trans Golgi in resting parietal cells
brenda
-
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
brenda
additional information
-
coinciding of the nongastric H-K-ATPase alpha subunit with the beta1 subunit of Na-K-ATPase
brenda
-
H+/K+-ATPase localization along two axes is dependent on intracellular transport machinery, overview
brenda
-
H+/K+-ATPase localization along two axes is dependent on intracellular transport machinery, overview
brenda
-
apical membrane, cytoplasmic tubular membranes in the resting state
brenda
-
healthy prostate tissue displays a membrane-bound ATP12A staining with focal accumulated pattern, whereas in the benign prostate hyperplasia and cancerous prostate tissue (tumor grade I-III) the protein appears to be displaced in the luminal cells of the glandular epithelium
brenda
-
membrane localization and topology model of HKalpha2, overview
brenda
-
apical membrane, cytoplasmic tubular membranes in the resting state
brenda
-
-
brenda
-
gastric vesicles are prepared from mucosa in the fundic region of hog stomaches
brenda
-
microvilli of the expanded secretory canaliculus in the stimulated state of the parietal cell
brenda
-
microvilli of the expanded secretory canaliculus in the stimulated state of the parietal cell
brenda
additional information
-
the H+/K+-ATPase and Na+/K+-ATPase, EC 3.6.3.9, are not located at the same sub-cellular fraction. The ouabain-insensitive K+-ATPase resembles better the distribution of the Na+/K+-ATPase, suggesting that can be associated with the colonocyte basolateral plasma membrane
-
brenda
additional information
-
enzyme exists in two distinct compartments. Stimulation of the parietal cells leads to translocation of H+-K+-ATPase from an inactive compartment to a spontaneously active compartment
-
brenda
additional information
-
in resting parietal cells specifically in mircrovesicles within tubulovesicles, additionally also on diverging tubulovesicles, on concentric multilaminae and on coated vesicles
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
physiological function
-
distal colon absorbs K+ through a Na+-independent, ouabain-sensitive H+/K+-exchange, associated to an apical ouabain-sensitive H+/K+-ATPase
physiological function
the gastric proton pump, H+,K+-ATPase is the major membrane protein responsible for the gastric acid H+ secretion
physiological function
-
possible involvement of the non-gastric H+/K+ ATPase ATP12A in prostate cancer
physiological function
-
the H+-K+-ATPase alpha-subunit, HKalpha2, participates importantly in systemic acid-base homeostasis and defends against metabolic acidosis, showing pH-dependent regulation, overview. Regulatory role of pH-activated G protein-coupled receptor GPR4 in homeostatic regulation of HKalpha2 and acid-base balance
physiological function
-
enzyme activity is continuously required during biomineralization
physiological function
-
H+,K+-ATPase is responsible for the acidification of the gastric fluid
physiological function
-
the enzyme in stria vascularis contributes to pH regulation of cochlear endolymph but not to K+ secretion
physiological function
-
the enzyme plays an important role in drought tolerance in barley cultivar XZ5
Show AA Sequence and Transmembrane Helices (188 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
35000
500000
-
1 * 100000, alpha-subunit, + 1 * 500000, beta-subunit, alpha/beta, SDS-PAGE
95000
100000
-
1 * 100000, alpha-subunit, + 1 * 500000, beta-subunit, alpha/beta, SDS-PAGE
35000
-
alphabeta composition of HKalpha1 and HKalpha2, 1 * 35000, beta-subunit of HKalpha1
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
additional information
dimer
-
1 * 100000, alpha-subunit, + 1 * 500000, beta-subunit, alpha/beta, SDS-PAGE
dimer
-
alphabeta composition of HKalpha1 and HKalpha2, 1 * 35000, beta-subunit of HKalpha1
heterodimer
-
alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison
heterodimer
-
alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison
heterodimer
-
alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison
heterodimer
-
alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison
heterodimer
-
alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison
additional information
-
a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase
additional information
-
H+/K+-ATPase is an alpha/beta-heterodimer, whose subunits, identified by Tandem-mass spectrometry, seem to correspond to HKalpha2 and Na+/K+-ATPase beta1-subunit, respectively
additional information
-
beta1 is not only a subunit of the Na,K-ATPase, but also serves as an authenthic subunit of nongastric H,K-ATPase
additional information
-
nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different beta-subunits. The type of beta-subunit associated has a global structural influence on nongastric H+-K+-ATPase alpha-subunit. Beta-Subunits influence to a lesser extent the transport properties of nongastric H+-K+-ATPases than that of Na+-K+-ATPase
additional information
-
a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase
additional information
-
functional role of the beta-subunit in the H+-K+-ATPase activity especially the K+-induced conformational states
additional information
-
a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase
additional information
-
structure analysis and H,K-ATPase homology modeling, overview
additional information
-
the enzyme consists of an alpha and a beta subunit
additional information
-
beta1-Na+,K+-ATPase is the physiologic beta-subunit of colonic HKalpha2
additional information
-
a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase
additional information
-
the beta-subunit of H,K-ATPase has an important function in maturation and plasma membrane targeting of the catalytic alpha-subunit but also modulate the transport activity of the holoenzymes
additional information
homology model of the gastric H,K-ATPase in the E2 state
additional information
-
homology modeling of wild-type and mutant gastric H+,K+-ATPase beta-subunit and molecular dynamics simulation, simulations of charge transfer in wild-type and mutant enzymes, structure comparisons, overview
additional information
-
a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phosphoprotein
glycoprotein
-
the beta-subunit is synthesized as a 52000 Da glycoprotein with seven N-linked precursor high-mannose oligosaccharides that mature into complex oligosaccharides
glycoprotein
-
seven potential N-linked glycosylation sites are located in the putative extracellular regions of the protein
glycoprotein
-
N-linked glycosylation of beta-subunit, the absence of the huge N-linked oligosaccharide moiety on the beta-subunit in the glycosylation-deficient Asn-to-Gln beta-mutants does not affect alpha/beta co-assembly, plasma membrane delivery or functional activity of the holoenzyme, differences in neither the voltage-dependent E1P/E2P ratio nor the kinetics of the E1P/E2P transition between holoenzymes comprising glycosylated and glycosylation-deficient beta-subunits, overview
glycoprotein
-
the beta-subunit contains five asparagine-linked oligosaccharide chains
phosphoprotein
-
the enzyme is phosphorylated from [32P]-gamma-ATP, forming an acyl-phosphate bond, in an Mg2+-dependent, vanadate-sensitive process, and inhibited by hydroxylamine
phosphoprotein
-
the steady-state phopshorylation level of the enzyme decreases with increasing pH, K+ and Na+ concentration, but nearly doubles in presence of oligomycin, Na+, K+, and NH4+ stimulate enzyme dephosphorylation
phosphoprotein
-
critical role for PKA in the maturation and function of the H+-K+-ATPase alpha-subunit and H+-ATPase, a mechanism that involves phosphorylation at key serine residues
phosphoprotein
reversible phosphorylation of a highly conserved Asp residue, a hallmark of all P-type ATPases, is coupled to the transition between two principal conformational states and the corresponding phosphointermediates
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K791S
C10S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S/C152S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S/C152S/C162S/C178S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S/C152S/C162S/C178S/C201s/C263S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C152S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C162S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C162S/C178S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C178S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C201S/C263S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C210S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C21S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C263S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C58S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C813A
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
C813S
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
C813T
mutant enzyme shows 9fold loss of SCH28080 affinity
D824A
D824E
NH4+-independent H,K-ATPase activity is 2.8fold higher than the wild-type value
D824N
NH4+-independent H,K-ATPase activity is 46% of the wild-type value
E343A
complete loss of NH4+-stimulated H,K-ATPase activity, NH4+-independent H,K-ATPase activity is 80% of the wild-type value
E343D
complete loss of NH4+-stimulated H,K-ATPase activity, NH4+-independent H,K-ATPase activity is 39% of the wild-type value
E343Q
the apparent Km-value for NH4+ is increased about 4fold, the Ki value for SCH28080 is increased about 2fold, NH4+-independent H,K-ATPase activity is 83% of the wild-type value
E774A
IC50 for SCH28080 is 2.2fold higher than that of the wild-type enzyme
E774Q
IC50 for SCH28080 is nearly identical to that of the wild-type enzyme
E795D
the apparent Km-value for NH4+ is increased about 3fold, the Ki value for SCH28080 is increased about 11fold, NH4+-independent H,K-ATPase activity is 29% of the wild-type value
E795Q
the Ki value for SCH28080 is increased 1.3fold, NH4+-independent H,K-ATPase activity is 2.3fold higher than the wild-type value
E797Q
IC50 for SCH28080 is 4.3fold higher than that of the wild-type enzyme
E820A
complete loss of NH4+-stimulated H,K-ATPase activity
E820D
the Ki value for SCH28080 is increased 2.7fold, NH4+-independent H,K-ATPase activity is 1.5fold higher than the wild-type value
E914Q
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
E936D
the apparent Km-value for NH4+ is increased about 2fold. the Ki value for SCH28080 is increased 2.5fold, NH4+-independent H,K-ATPase activity is 1.7fold higher than the wild-type value
E936Q
NH4+-independent H,K-ATPase activity is 2.95fold higher than the wild-type value
E936V
complete loss of NH4+-stimulated H,K-ATPase activity
E938A
IC50 for SCH28080 is 8.2fold lower than that of the wild-type enzyme
E938Q
IC50 for SCH28080 is 1.6fold higher than that of the wild-type enzyme
F818C
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
F917Y
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
F932L
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
G918E
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
I803L
mutation has no effect on inhibitor kinetics of SCH28080
I814F
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
I814V
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
I816L
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
I819L
mutant enzyme shows mixed inhibition with SCH28080, no change in inhibitor affinity
I940A
mutation reduces affinity to the inhibitor SCH28080 by about 10fold and results in mixed inhibition
K791A
complete loss of NH4+-stimulated H,K-ATPase activity, NH4+-independent H,K-ATPase activity is 17% of the wild-type value
K791S
L809F
mutation results in a about 100fold decrease in affinity towards SCH28080
L809V
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
L811F
mutation reduces affinity to the inhibitor SCH28080 by about 10fold and results in mixed inhibition
L811V
mutation has no effect on inhibitor kinetics of SCH28080
M937V
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
P798C
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
P810A
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
P810G
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
Q905N
mutation has no effect on inhibitor kinetics of SCH28080
Q923V
mutant enzyme shows mixed inhibition with SCH28080, no change in inhibitor affinity
S806N
mutation has no effect on inhibitor kinetics of SCH28080
T823V
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
T825A
IC50 for SCH28080 is nearly identical to that of the wild-type enzyme
T825L
IC50 for SCH28080 is 4.5fold lower than that of the wild-type enzyme
T929L
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
V807I
mutation has no effect on inhibitor kinetics of SCH28080
Y799F
mutation has no effect on inhibitor kinetics of SCH28080
Y802F
mutation has no effect on inhibitor kinetics of SCH28080
Y802L
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
Y922I
mutation reduces affinity to the inhibitor SCH28080 by about 10fold and results in mixed inhibition
Y925A
mutant enzyme shows mixed inhibition with SCH28080, no change in inhibitor affinity
Y925F
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
Y928H
mutation has no effect on inhibitor kinetics of SCH28080
A778P/C781T
-
expression level rather similar to that of the recombinant enzyme, ability of binding 3(H)ouabain with high affinity
A778P/C781T/Y786F/V788I/G790N/L791I/I795L/I798V/F802C
-
expression level and 3(H)ouabain binding level rather similar to that of the recombinant enzyme
D312E/S319G/A778P/I795L/F802C
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a ouabain-sensitive mutant of the non-gastric H,K-ATPase, with the mutant enzyme, strophanthidin and dihydroouabain have a higher and digoxin has a lower affinity than ouabain
E820A
site-directed mutagenesis, shows altered pH dependence compared to the wild-type enzyme
E820D
site-directed mutagenesis, charge-conserving mutation, slight preference of the mutants for the E2P state, shows no altered pH dependence compared to the wild-type enzyme
E820K
site-directed mutagenesis, charge-inverting mutation, no shift in the conformational distribution toward E1P
E820Q
I795L/I798V/F802C
-
expression level rather similar to that of the recombinant enzyme, ability of binding 3(H)ouabain with high affinity
K791A
K791E
site-directed mutagenesis, charge-inverting mutation, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type
K791R
K791R/E343D
no K+-independent ATPase activity, no K+-stimulated dephosphorylation activity
K791R/E820Q
some K+-independent ATPase activity, no K+-stimulated dephosphorylation activity
K791S
N103Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N130Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N146Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N161Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N193Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N225Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N99Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
S806C
Y309T/V310W/D312E/I314V/S319G
-
expression level rather similar to that of the recombinant enzyme, ability of binding 3(H)ouabain with high affinity
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
-
expression level rather similar, but 3(H)ouabain binding level significantly higher than that of the recombinant enzyme
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/C802F
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/E312D
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/G319S
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/L795I
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/P778A
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3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/T309Y
-
3(H)ouabain binding level not significantly different from that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/T781C
-
3(H)ouabain binding level not significantly different from that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/V314I
-
3(H)ouabain binding level not significantly different from that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/V798I
-
3(H)ouabain binding level not significantly different from that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/W310V
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3(H)ouabain binding level significantly higher that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/Y786F/V788I/G790N/L791I
-
expression level and 3(H)ouabain binding level rather similar to that of the recombinant enzyme
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/Y786F/V788I/G790N/L791I/I795L/I798V/F802C
-
expression level rather similar, but 3(H)ouabain binding level significantly higher than that of the recombinant enzyme
Y309T/V310W/D312E/I314V/S319G/Y786F/V788I/G790N/L791I/I795L/I798V/F802C
-
expression level and 3(H)ouabain binding level rather similar to that of the recombinant enzyme
Y44W/Y48W
-
beta-subunit mutation, tryptophan replacement of two highly conserved tyrosines in the transmembrane domain of gastric H,K-ATPase beta-subunits results in considerable shifts of the voltage-dependent E1P/E2P distributions toward the E1P state. Reverse binding of extracellular protons and subsequent E2P-E1P conversion is accelerated by the H,K-ATPase beta-Y44W/Y48Wmutation, and H+ secretion is strongly impaired
Y786F/V788I/G790N/L791I
-
expression level rather similar to that of the recombinant enzyme
D136A
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
D136F
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
D136I
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
D136L
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
D137A
the mutant shows strongly increased sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, BYK99 and BYK73)
D137F
the mutant shows strongly increased sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-CN-, BYK99 and BYK73)
D137I
the mutant shows strongly increased sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, and BYK99)
D137L
the mutant shows strongly increased sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
D138I
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
E345D
-
site-directed mutagenesis, the mutant shows no charge transport pathway, the mutant shows unaltered cell surface expression compared to the wild-type enzyme
E345L
-
site-directed mutagenesis, the mutant shows no charge transport pathway, the mutant shows unaltered cell surface expression compared to the wild-type enzyme
E345Q
-
site-directed mutagenesis, the mutant shows an alternative charge transport pathway H3O+-Arg105-Gln161-Gln345, the mutant shows unaltered cell surface expression compared to the wild-type enzyme
E795Q
-
the mutant shows increased affinity for K+ compared to the wild type enzyme
E820Q
-
the mutant has K+-independent constitutive dephosphorylation activity and an increased preference for the E1 conformation
K164L
-
site-directed mutagenesis, the mutant shows an alternative charge transport pathway H3O+-Gln161-Glu345, the mutant shows unaltered cell surface expression compared to the wild-type enzyme
K791S
-
the mutation greatly reduces enzyme activity as well as increases the Ki for SCH28080
L139A
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
L139F
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
L139I
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
L141I
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
N138A
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
N138F
the mutant shows strongly increased sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
N138L
the mutant shows strongly increased sensitivity against imidazo[1,2-a]pyridine inhibitors (BYK99 and BYK73)
Q161L
-
site-directed mutagenesis, the mutant shows no charge transport pathway, the mutant shows unaltered cell surface expression compared to the wild-type enzyme
Y140A
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
Y140F
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
Y140I
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
Y140L
the mutant shows wild type-like sensitivity against imidazo[1,2-a]pyridine inhibitors (SCH28080, SCH-Me-, SCH-CN-, BYK99 and BYK73)
additional information
K791S
-
the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
K791S
-
the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
D824A
complete loss of NH4+-stimulated H,K-ATPase activity, the Ki value for SCH28080 is decreased to about 78% of the wild-type value, NH4+-independent H,K-ATPase activity is 3.2fold higher than the wild-type value
D824A
NH4+-independent H,K-ATPase activity is 97% of the wild-type value
K791S
the apparent Km-value for NH4+ is increased about 2fold. the Ki value for SCH28080 is increased 20.7fold, NH4+-independent H,K-ATPase activity is 51% of the wild-type value
K791S
-
the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
E820Q
K+-insensitive activity and an E1 preference, E2 form-specific salt bridge between Glu820 and Lys791 is no longer possible
E820Q
site-directed mutagenesis, shows altered pH dependence compared to the wild-type enzyme
K791A
K+ affinity is markedly reduced without altering the E2 preference of the enzyme
K791A
site-directed mutagenesis, charge-neutralizing amino acid replacement, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type
K791R
site-directed mutagenesis, charge-inverting mutation, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type
K791S
-
the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
K791S
site-directed mutagenesis, charge-neutralizing amino acid replacement, insertion of the Lys791 mutations into the backbone of H,KATPase mutant S806C, which carries a reporter cysteine for site-specific fluorescence labeling. The mutation causes a conformational shift toward the E1P-state and a shift to more positive potentials compared with the wild-type
S806C
-
alpha-subunit mutation, exchange in the extracellulae M5/M6 loop, the S806C mutation does not affect the transport properties of H,K-ATPase
S806C
a single cysteine replacement in the TM5/TM6 extracellular loop of the alpha-subunit. The S806C mutation enables site-specific labeling of H,K-ATPase with the environmentally sensitive fluorophore TMRM, the S806C mutation does not affect the transport properties of gastric H,K-ATPase
additional information
-
mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity
additional information
-
a LacZ fusion enzyme fused to motor proteins reveals endogenous polarity in the cytoplasmic transport machinery, overview
additional information
point mutations of chimeras, single point mutation between the third and 4th transmembrane spanning domain redirects the enzyme to the basolateral membrane
additional information
-
point mutations of chimeras, single point mutation between the third and 4th transmembrane spanning domain redirects the enzyme to the basolateral membrane
additional information
-
mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity
additional information
-
targeted deletion of the nongastric H-K-ATPase alpha-subunit, mutant transcript present in amounts comparable to those of wild-type
additional information
-
construction of HKalpha1-deficient and HKalpha2-deficient mice, phenotypes with deprived H+,K+-ATPase activities, overview
additional information
-
mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity
additional information
-
mutation of 84 amino acids in the carboxy-terminus, incapable of sustaining functionality
additional information
-
the absence of the huge N-linked oligosaccharide moiety on the beta-subunit in the glycosylation-deficient Asn-to-Gln beta-mutants does not affect alpha/beta co-assembly, plasma membrane delivery or functional activity of the holoenzyme, differences in neither the voltage-dependent E1P/E2P ratio nor the kinetics of the E1P/E2P transition between holoenzymes comprising glycosylated and glycosylation-deficient beta-subunits, overview
additional information
-
mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity
additional information
inversion of the salt bridge polarity does not rescue function does not necessarily exclude that Lys791 and Glu820 in the wild-type proton pump interact in an E2P-stabilizing manner
additional information
-
chimera of the NH2-terminal half of the rat gastric H,K-ATPase and the COOH-terminal half of the rat Na,K-ATPase behaves as a functional ion pump and indicates that the protein domains involved in cardiac glycoside binding are not confined to the amino-terminal half of the Na,K-ATPase
additional information
-
mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity
additional information
-
the fluorescence probe FITC preferentially forms a covalent bond with the epsilon-amino group of the Lys-518 residue, which is embedded in the conserved Lys-518 in the ATP binding site of the N domain. This chemical modification of the Lys residue impairs H+,K+-ATPase activity (1.7% of activity compared with that of mock-treated enzyme) due to a loss of ATP-binding ability
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
solubilization at pH 4.0 causes rapid loss of ATPase activity, probably due to an increased protease activity
-
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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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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
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expression of alpha-subunit of wild-type and mutant enzymes in Spodopera frugiperda Sf9 cell membranes using the baculovirus transfection system
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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
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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
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expression of wild-type and mutant enzymes in HEK-293 cells, expression analysis, overview
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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
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gene HKalpha2, the -144/-135 element is important for HKalpha2 promoter activity, regulation of gene expression and interaction with Sp1 protein, expression analysis, overview
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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
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into pcDNA3.1(+)-Neo, expression in HEK-293 cells, mutant cloned into pEGFP-2C vector
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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
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
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
chronic acidosis and G protein-coupled receptor GPR4 increase HKalpha2 protein by increasing protein kinase A activity without altering HKalpha2 mRNA abundance. Heterologous expression of GPR4 is sufficient to increase both basal and acid-stimulated HKalpha2 expression. Upregulation of HKalpha2 by chronic acidosis is reversible
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exposure to light for 12 h does not affect the H+/NH+4-activated enzyme activity from the inner mantle
-
exposure to light for 12 h leads to a significant decrease in H+/NH+4-activated enzyme activity from the outer mantle
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exposure to light for 12 h leads to a significant increase in H+/NH+4-activated-HKA activity from ctenidia
-
PEG and mannitol treatments induce marked increases in H+-K+-ATPase in barley cultivars XZ5 and Tadmor
-
trimethyltin chloride does not change the expression of H+/K+-ATPase protein and mRNA
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
nongastric H-K-ATPase is required for acidification of luminal prostate fluids, operates as a proton pump, beta1 is an authentic subunit of nongastric H-K-ATPase in vivo, apical localization of beta1 in the prostate is completely dependent on its association with the enzyme alpha-subunit
pharmacology
-
lower concentration of [(dihydroindenyl)oxy]acetic acid should be used for evaluation of the activity of K+-Cl- cotranporter without affecting the activities of coexisting Na+,K+-ATPase and H+,K+-ATPase in cells
additional information
additional information
-
beta1 subunit is the predominant isoform in nongastric H-K-ATPase
additional information
-
binding and release steps of K+ and H+ in both principal conformations of the ion pump, E1 and P-E2, are electrogenic, whereas the conformation transitions do not contribute significantly to a charge movement wihtin the membrane dielectric
additional information
-
carboxy-terminus of the H+,K+-ATPase alpha subunit facilitates the proper folding of the H+,K+-ATPase alpha/beta1 subunit complex allowing translocation to the plasma membrane where K+ uptake occurs, otherwise the complex is destined for degradation
additional information
-
CD63 functions as a negative regulator of the colonic H+-K+-ATPase, specifically interacts with carboxy terminus of the enzyme, supression of CD63 protein synthesis in HEK-293 cells increases Rb+ uptake by the HKalpha2/NKbeta1 complex
additional information
-
CD63 functions as a negative regulator of the colonic H+-K+-ATPase, specifically interacts with carboxy terminus of the enzyme, supression of CD63 protein synthesis in HEK-293 cells increases Rb+ uptake by the HKalpha2/NKbeta1 complex
additional information
enzyme expression increases during freshwater acclimation but not exposure to hypercapnia
additional information
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enzyme expression increases during freshwater acclimation but not exposure to hypercapnia
additional information
-
infrared spectra on multilayer stacks of native gastric tubulovesicle membranes, membrane tilt does not significantly contribute to the infrared dichroism, even for the largest thicknesses tested
additional information
-
Na+,K+-ATPase is likely to represent the most physiologic and efficient subunit for H+,K+-ATPase alpha subunit assembly in distal colon
additional information
-
presence of fucosyl residues in N-linked oligosaccharidic chains in glyocoproteins of beta-H,K-ATPase subunits
additional information
-
role of the beta subunit in stabilizing conformations of the enzyme with occluded K+ ions, alpha/beta subunit interactions may be required to compensate for the tendency of occluded K+ ions to destabalize the trans-membrane segments and are effective only in the context of correct phospholipid-protein interactions
additional information
-
strong evidence that the catalytic unit of C12E8-solubilized gastric H/K-ATPase is a tetraprotomer
additional information
the non-gastric H,K-ATPase contains similar sorting motifs in close proximity to the 4th transmembrane spanning domain than the gastric H,K-ATPase, short extracellular loop between the third and the 4th transmembrane spanning domain is critical for the pump´s apical delivery
additional information
-
the non-gastric H,K-ATPase contains similar sorting motifs in close proximity to the 4th transmembrane spanning domain than the gastric H,K-ATPase, short extracellular loop between the third and the 4th transmembrane spanning domain is critical for the pump´s apical delivery
additional information
the salt bridge between Glu820 and Lys791 is essential for high-affinity K+ binding and the E2 preference of the enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lacapere, J.J.; Robert, J.C.; Thomas-Soumarmon, A.
Efficient solubilization and purification of the gastric H+,K+-ATPase for functional and structural studies
Biochem. J.
345
239-245
2000
Sus scrofa
brenda
Xian, Y.; Hebert, H.
Three-dimensional structure of the porcine gastric H,K-ATPase from negatively stained crystals
J. Struct. Biol.
118
169-177
1997
Sus scrofa
brenda
Hebert, H.; Xian, Y.; Hacksell, I.; Mardh, S.
Two-dimensional crystals of membrane-bound gastric H,K-ATPase
FEBS Lett.
299
159-162
1992
Sus scrofa
brenda
Chatterjee, P.K.; Das, P.K.
Characterization of Syrian hamster gastric mucosal H+,K+-ATPase
Mol. Cell. Biochem.
148
95-103
1995
Mesocricetus auratus
brenda
Gluck, S.L.; Nelson, M.D.; Lee, B.S.
Properties and regulation of the renal vacuolar H+-ATPase and H+-K+-ATPase
Curr. Opin. Nephrol. Hypertens.
2
715-724
1993
Turtle
brenda
Hango, T.; Nojima, S.; Setaka, M.
Purification and characterization of (H+ + K+)-ATPase from hog gastric mucosa
Jpn. J. Pharmacol.
52
295-305
1990
Sus scrofa
brenda
Okamoto, C.T.; Karpilow, J.M.; Smolka, A.; Forte, J.G.
Isolation and characterization of gastric microsomal glycoproteins. Evidence for a glycosylated beta-subunit of the H+/K+-ATPase
Biochim. Biophys. Acta
1037
360-372
1990
Sus scrofa
brenda
Silver, R.B.; Frindt, G.; Mennitt, P.; Satlin, L.M.
Characterization and regulation of H-K ATPase in intercalated cells of rabbit cortical collecting duct
J. Exp. Zool.
279
443-455
1997
Oryctolagus cuniculus
brenda
Grishin, A.V.; Reinhard, J.; Dunbar, L.A.; Courtois-Coutry, N.; Wang, T.; Giebisch, G.; Caplan, M.J.
Nongastric H+,K+-ATPase: Cell biologic and functional properties
Semin. Nephrol.
19
421-430
1999
Rhinella marina, Homo sapiens, Rattus norvegicus
brenda
Chow, D.C.; Forte, J.G.
Characterization of the beta-subunit of the H+-K+-ATPase using an inhibitory monoclonal antibody
Am. J. Physiol.
265
1562-1570
1993
Oryctolagus cuniculus
brenda
Planelles, G.; Anagnostopoulos, T.; Cheval, L.; Doucet, A.
Biochemical and functional characterization of H+-K+-ATPase in distal amphibian nephron
Am. J. Physiol.
260
F806-812
1991
Necturus maculosus, Pelophylax ridibundus
brenda
Hersey, S.J.; Perez, A.; Matheravidathu, S.; Sachs, G.
Gastric H+-K+-ATPase in situ: evidence for compartmentalization
Am. J. Physiol.
257
G539-547
1989
Oryctolagus cuniculus
brenda
Reuben, M.A.; Lasater, L.S.; Sachs, G.
Characterization of a beta-subunit of the gastric H+/K+-transporting ATPase
Proc. Natl. Acad. Sci. USA
87
6767-6771
1990
Oryctolagus cuniculus
brenda
Callaghan, J.M.; Toh, B.H.; Simpson, R.J.; Baldwin, G.S.
Rapid purification of the gastric H+/K+-ATPase complex by tomato-lectin affinty chromatography
Biochem. J.
283
63-68
1992
Sus scrofa
brenda
Codina, J.; Kone, B.C.; Delmas-Mata, J.T.; DuBose, T.D.
Functional expression of the colonic H+,K+-ATPase alpha-subunit. Pharmacologic properties and assembly with H+,K+-ATPase beta-subunit
J. Biol. Chem.
271
29759-29763
1993
Rattus norvegicus
brenda
Blostein, R.; Zhang, R.; Gottardi, C.J.; Caplan, M.J.
Functional properties of an H,K-ATPase/Na,K-ATPase chimera
J. Biol. Chem.
268
10654-10558
1993
Sus scrofa
brenda
De Pont, J.J.H.H.M.; Bonting, S.L.
Anion-sensitive ATPase and (K++H+)-ATPase
New Compr. Biochem.
2
209-234
1981
Oryctolagus cuniculus, Frog, Sus scrofa
-
brenda
Skrabanja, A.T.P.; van der Hijden, H.T.W.M.; de Pont, J.J.H.H.M.
Transport ratios of reconstituted (H++K+)-ATPase
Biochim. Biophys. Acta
903
434-440
1987
Sus scrofa
brenda
Lorentzon, P.; Jackson, R.; Wallmark, B.; Sachs, G.
Inhibition of (H++K+)-ATPase by omeprazole in isolated gastric vesicles requires proton transport
Biochim. Biophys. Acta
897
41-51
1987
Sus scrofa
brenda
Soumarmon, A.; Rangachari, P.K.; Lewin, M.J.M.
Passive transport of Rb+ by hog gastric (H+,K+)-ATPase
J. Biol. Chem.
259
11861-11867
1984
Sus scrofa
brenda
Faller, L.D.; Rabon, E.; Sachs, G.
Vanadate binding to the gastric H,K-ATPase and inhibition of the enzyme's catalytic and transport activities
Biochemistry
22
4676-4685
1983
Sus scrofa
brenda
Shull, G.E.
cDNA cloning of the beta-subunit of the rat gastric H,K-ATPase
J. Biol. Chem.
265
12123-12126
1990
Rattus norvegicus
brenda
Shull, G.E.; Linrel, J.B.
Molecular cloning of the rat stomach (H+ / K+)-ATPase
J. Biol. Chem.
261
16788-16791
1986
Rattus norvegicus
brenda
Beisvag, V.; Falck, G.; Loennechen, J.P.; Qvigstad, G.; Jynge, P.; Skomedal, T.; Osnes, J.B.; Sandvik, A.K.; Ellingsen, O.
Identification and regulation of the gastric H+/K+-ATPase in the rat heart
Acta Physiol. Scand.
179
251-262
2003
Rattus norvegicus
brenda
Crambert, G.; Horisberger, J.D.; Modyanov, N.N.; Geering, K.
Human nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different beta-subunits
Am. J. Physiol.
283
C305-314
2002
Homo sapiens
brenda
Kraut, J.A.; Helander, K.G.; Helander, H.F.; Iroezi, N.D.; Marcus, E.A.; Sachs, G.
Detection and localization of H+-K+-ATPase isoforms in human kidney
Am. J. Physiol. Renal. Physiol.
281
F763-768
2001
Homo sapiens
brenda
Modyanov, N.; Pestov, N.; Adams, G.; Crambert, G.; Tillekeratne, M.; Zhao, H.; Korneenko, T.; Shakhparonov, M.; Geering, K.
Nongastric H,K-ATPase: structure and functional properties
Ann. N. Y. Acad. Sci.
986
183-187
2003
Homo sapiens
brenda
Rulli, S.J.; Louneva, N.M.; Skripnikova, E.V.; Rabon, E.C.
Site-directed mutagenesis of cation coordinating residues in the gastric H,K-ATPase
Arch. Biochem. Biophys.
387
27-34
2001
Oryctolagus cuniculus (P18597), Oryctolagus cuniculus (P27112)
brenda
Shin, J.M.; Sachs, G.
Differences in binding properties of two proton pump inhibitors on the gastric H(+),K(+)-ATPase in vivo
Biochem. Pharmacol.
68
2117-2127
2004
Rattus norvegicus
brenda
Adams, G.; Tillekeratne, M.; Yu, C.; Pestov, N.B.; Modyanov, N.N.
Catalytic function of nongastric H,K-ATPase expressed in Sf-21 insect cells
Biochemistry
40
5765-5776
2001
Oryctolagus cuniculus
brenda
Vagin, O.; Munson, K.; Lambrecht, N.; Karlish, S.J.; Sachs, G.
Mutational analysis of the K+-competitive inhibitor site of gastric H,K-ATPase
Biochemistry
40
7480-7490
2001
Oryctolagus cuniculus (P18597), Oryctolagus cuniculus (P27112)
brenda
Vagin, O.; Denevich, S.; Munson, K.; Sachs, G.
SCH28080, a K+-competitive inhibitor of the gastric H,K-ATPase, binds near the M5-6 luminal loop, preventing K+ access to the ion binding domain
Biochemistry
41
12755-12762
2002
Oryctolagus cuniculus (P18597), Oryctolagus cuniculus (P27112)
brenda
Kimura, T.; Tabuchi, Y.; Takeguchi, N.; Asano, S.
Mutational study on the roles of disulfide bonds in the beta-subunit of gastric H+,K+-ATPase
J. Biol. Chem.
277
20671-20677
2002
Oryctolagus cuniculus
brenda
Liquori, G.E.; Zizza, S.; Mastrodonato, M.; Scillitani, G.; Calamita, G.; Ferri, D.
Pepsinogen and H,K-ATPase mediate acid secretion in gastric glands of Triturus carnifex (Amphibia, Caudata)
Acta Histochem.
107
133-141
2005
Triturus carnifex
brenda
Pestov, N.B.; Korneenko, T.V.; Radkov, R.; Zhao, H.; Shakhparonov, M.I.; Modyanov, N.N.
Identification of the b-subunit for nongastric H-K-ATPase in rat anterior prostate
Am. J. Physiol.
286
C1229-C1237
2004
Rattus norvegicus
brenda
Choe, K.P.; Verlander, J.W.; Wingo, C.S.; Evans, D.H.
A putative H+-K+-ATPase in the Atlantic stingray, Dasyatis sabina: primary sequence and expression in gills
Am. J. Physiol.
287
R981-R991
2004
Hypanus sabinus (Q7SZD4), Hypanus sabinus
brenda
Codina, J.; Li, J.; DuBose, T.D., Jr.
CD63 interacts with the carboxy terminus of the colonic H+-K+-ATPase to increase plasma membrane localization and 86Rb+ uptake
Am. J. Physiol.
288
C1279-C1286
2005
Mus musculus, Rattus norvegicus
brenda
Pestov, N.B.; Korneenko, T.V.; Shakhparonov, M.I.; Shull, G.E.; Modyanov, N.N.
Loss of acidification of anterior prostate fluids in Atp12a-null mutant mice indicates that nongastric H-K-ATPase functions as proton pump in vivo
Am. J. Physiol.
291
C366-C374
2006
Mus musculus
brenda
Chourasia, M.; Sastry, G.M.; Sastry, G.N.
Proton binding sites and conformational analysis of H+K+-ATPase
Biochem. Biophys. Res. Commun.
336
961-966
2005
Homo sapiens (P20648)
brenda
Ivanov, D.; Dubreuil, N.; Raussens, V.; Ruysschaert, J.M.; Goormaghtigh, E.
Evaluation of the ordering of membranes in multilayer stacks built on an ATR-FTIR germanium crystal with atomic force microscopy: The case of the H+,K+-ATPase-containing gastric tubulovesicle membranes
Biophys. J.
87
1307-1315
2004
Sus scrofa
brenda
Diller, A.; Vagin, O.; Sachs, G.; Apell, H.J.
Electrogenic partial reactions of the gastric H,K-ATPase
Biophys. J.
88
3348-3359
2005
Sus scrofa
brenda
Lerner, M.; Lemke, D.; Bertram, H.; Schillers, H.; Oberleithner, H.; Caplan, M.J.; Reinhardt, J.
An extracellular loop of the human non-gastric H,K-ATPase a-subunit is involved in apical plasma membrane polarization
Cell. Physiol. Biochem.
18
75-84
2006
Homo sapiens (P54707), Homo sapiens
brenda
Abe, K.; Kaya, S.; Taniguchi, K.; Hayashi, Y.; Imagawa, T.; Kikumoto, M.; Oiwa, K.; Sakaguchi, K.
Evidence for a relationship between activity and the tetraprotomeric assembly of solubilized pig gastric H/K-ATPase
J. Biochem.
138
293-301
2005
Sus scrofa
brenda
Koenderink, J.B.; Swarts, H.G.P.; Willems, P.H.G.M.; Krieger, E.; De Pont, J.J.H.H.M.
A conformation-specific interhelical salt bridge in the K+ binding site of gastric H,K-ATPase
J. Biol. Chem.
279
16417-16424
2004
Rattus norvegicus (P09626)
brenda
Cohen, E.; Goldshleger, R.; Shainskaya, A.; Tal, D.M.; Ebel, C.; le Maire, M.; Karlish, S.J.D.
Purification of Na+,K+-ATPase expressed in Pichia pastoris reveals an essential role of phospholipid-protein interactions
J. Biol. Chem.
280
16610-16618
2005
Komagataella pastoris
brenda
Qiu Li, Y.; Swarts Herman, G.P.; Tonk Elisa, C.M.; Willems Peter, H.G.M.; Koenderink Jan, B.; De Pont Jan Joep, H.H.M.
Conversion of the low affinity ouabain-binding site of non-gastric H,K-ATPase into a high affinity binding site by substitution of only five amino acids
J. Biol. Chem.
281
13533-13539
2006
Rattus norvegicus
brenda
Sawaguchi, A.; McDonald, K.L.; Forte, J.G.
High-pressure freezing of isolated gastric glands provides new insight into the fine structure and subcellular localization of H+/K+-ATPase in gastric parietal cells
J. Histochem. Cytochem.
52
77-86
2004
Oryctolagus cuniculus
brenda
Li, J.; Codina, J.; Petroske, E.; Werle, M.J.; DuBose, T.D.
The carboxy terminus of the colonic H+,K+-ATPase alpha-subunit is required for stable beta subunit assembly and function
Kidney Int.
65
1301-1310
2004
Rattus norvegicus
brenda
Li, J.; Codina, J.; Petroske, E.; Werle, M.J.; Willingham, M.C.; DuBose, T.D.
The effect of beta-subunit assembly on function and localization of the colonic H+,K+-ATPase alpha-subunit
Kidney Int.
66
1068-1075
2004
Rattus norvegicus
brenda
Johansson, M.; Jansson, T.; Pestov, N.B.; Powell, T.L.
Non-Gastric H+/K+ATPase is present in the microvillous membrane of the human placental syncytiotrophoblast
Placenta
25
505-511
2004
Homo sapiens
brenda
Reenstra, W.W.; Crothers, J.; Forte, J.G.
The conformation of H,K-ATPase determines the nucleoside triphosphate (NTP) selectivity for active proton transport
Biochemistry
46
10145-10152
2007
Sus scrofa
brenda
Duerr, K.L.; Tavraz, N.N.; Zimmermann, D.; Bamberg, E.; Friedrich, T.
Characterization of Na,K-ATPase and H,K-ATPase enzymes with glycosylation-deficient beta-subunit variants by voltage-clamp fluorometry in Xenopus oocytes
Biochemistry
47
4288-4297
2008
Rattus norvegicus
brenda
Swarts, H.G.; Koenderink, J.B.; Willems, P.H.; De Pont, J.J.
The human non-gastric H,K-ATPase has a different cation specificity than the rat enzyme
Biochim. Biophys. Acta
1768
580-589
2007
Homo sapiens
brenda
Zimmermann, P.J.; Brehm, C.; Buhr, W.; Palmer, A.M.; Volz, J.; Simon, W.A.
Novel imidazo[1,2-a]pyrazine derivatives as potent reversible inhibitors of the gastric H+/K+-ATPase
Bioorg. Med. Chem.
16
536-541
2008
Sus scrofa
brenda
Zimmermann, P.J.; Buhr, W.; Brehm, C.; Palmer, A.M.; Feth, M.P.; Senn-Bilfinger, J.; Simon, W.A.
Novel indanyl-substituted imidazo[1,2-a]pyridines as potent reversible inhibitors of the gastric H+/K+-ATPase
Bioorg. Med. Chem. Lett.
17
5374-5378
2007
Sus scrofa
brenda
Fujii, T.; Ohira, Y.; Itomi, Y.; Takahashi, Y.; Asano, S.; Morii, M.; Takeguchi, N.; Sakai, H.
Inhibition of P-type ATPases by [(dihydroindenyl)oxy]acetic acid (DIOA), a K+ -Cl- cotransporter inhibitor
Eur. J. Pharmacol.
560
123-126
2007
Sus scrofa
brenda
Morii, M.; Yamauchi, M.; Ichikawa, T.; Fujii, T.; Takahashi, Y.; Asano, S.; Takeguchi, N.; Sakai, H.
Involvement of the H3O+-Lys-164-Gln-161-Glu-345 charge transfer pathway in proton transport of gastric H+,K+-ATPase
J. Biol. Chem.
283
16876-16884
2008
Sus scrofa
brenda
Reyes-Chilpa, R.; Baggio, C.H.; Alavez-Solano, D.; Estrada-Muniz, E.; Kauffman, F.C.; Sanchez, R.I.; Mesia-Vela, S.
Inhibition of gastric H+,K+-ATPase activity by flavonoids, coumarins and xanthones isolated from Mexican medicinal plants
J. Ethnopharmacol.
105
167-172
2006
Canis lupus familiaris
brenda
Nishizawa, T.; Abe, K.; Tani, K.; Fujiyoshi, Y.
Structural analysis of 2D crystals of gastric H+,K+-ATPase in different states of the transport cycle
J. Struct. Biol.
162
219-228
2008
Sus scrofa
brenda
Aw, S.; Adams, D.S.; Qiu, D.; Levin, M.
H,K-ATPase protein localization and Kir4.1 function reveal concordance of three axes during early determination of left-right asymmetry
Mech. Dev.
125
353-372
2008
Gallus gallus, Xenopus laevis
brenda
Siddaraju, M.N.; Dharmesh, S.M.
Inhibition of gastric H+,K+-ATPase and Helicobacter pylori growth by phenolic antioxidants of Zingiber officinale
Mol. Nutr. Food Res.
51
324-332
2007
Ovis aries
brenda
Codina, J.; DuBose, T.D.
Molecular regulation and physiology of the H+,K+-ATPases in kidney
Semin. Nephrol.
26
345-351
2006
Mus musculus, Rattus norvegicus
brenda
Zavros, Y.; Orr, M.A.; Xiao, C.; Malinowska, D.H.
Sonic hedgehog is associated with H+-K+-ATPase-containing membranes in gastric parietal cells and secreted with histamine stimulation
Am. J. Physiol. Gastrointest. Liver Physiol.
295
G99-G111
2008
Oryctolagus cuniculus
brenda
Yu, Z.; Li, M.; Zhang, D.; Xu, W.; Kone, B.C.
Sp1 trans-activates the murine H+-K+-ATPase {alpha}2 subunit gene
Am. J. Physiol. Renal Physiol.
297
63-70
2009
Mus musculus
brenda
Law, R.J.; Munson, K.; Sachs, G.; Lightstone, F.C.
An ion gating mechanism of gastric H,K-ATPase based on molecular dynamics simulations
Biophys. J.
95
2739-2749
2008
Oryctolagus cuniculus
brenda
Morokuma, J.; Blackiston, D.; Levin, M.
KCNQ1 and KCNE1 K+ channel components are involved in early left-right patterning in Xenopus laevis embryos
Cell. Physiol. Biochem.
21
357-372
2008
Xenopus laevis
brenda
Nandi, J.; Das, P.K.; Zinkievich, J.M.; Baltodano, J.D.; Levine, R.A.
Cyclo-oxygenase-1 inhibition increases acid secretion by modulating H+,K+-ATPase expression and activation in rabbit parietal cells
Clin. Exp. Pharmacol. Physiol.
36
127-134
2009
Oryctolagus cuniculus
brenda
Vesper, B.J.; Jawdi, A.; Altman, K.W.; Haines, G.K.; Tao, L.; Radosevich, J.A.
The effect of proton pump inhibitors on the human microbiota
Curr. Drug Metab.
10
84-89
2009
Homo sapiens
brenda
Duerr, K.L.; Tavraz, N.N.; Dempski, R.E.; Bamberg, E.; Friedrich, T.
Functional significance of E2 state stabilization by specific alpha/beta-subunit interactions of Na,K- and H,K-ATPase
J. Biol. Chem.
284
3842-3854
2009
Rattus norvegicus
brenda
Fujii, T.; Takahashi, Y.; Ikari, A.; Morii, M.; Tabuchi, Y.; Tsukada, K.; Takeguchi, N.; Sakai, H.
Functional association between K+-Cl- cotransporter-4 and H+,K+-ATPase in the apical canalicular membrane of gastric parietal cells
J. Biol. Chem.
284
619-629
2009
Homo sapiens
brenda
Freitas, C.S.; Baggio, C.H.; Finau, J.; Anginoni, M.; Pizzolatti, M.G.; Santos, A.R.; Marques, M.C.
Inhibition of H+/K+ ATPase in the gastroprotective effect of Baccharis illinita DC
J. Pharm. Pharmacol.
60
1105-1110
2008
Oryctolagus cuniculus, Rattus norvegicus
brenda
Shin, J.M.; Munson, K.; Vagin, O.; Sachs, G.
The gastric HK-ATPase: structure, function, and inhibition
Pflugers Arch.
457
609-622
2009
Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
De Pont, J.J.; Swarts, H.G.; Karawajczyk, A.; Schaftenaar, G.; Willems, P.H.; Koenderink, J.B.
The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase
Pflugers Arch.
457
623-634
2009
Rattus norvegicus
brenda
Belisario, D.C.; Rocafull, M.A.; del Castillo, J.R.
Purification and characterization of the ouabain-sensitive H+/K+-ATPase from guinea-pig distal colon
Arch. Biochem. Biophys.
496
21-32
2010
Cavia porcellus
brenda
Witzke, A.; Lindner, K.; Munson, K.; Apell, H.J.
Inhibition of the gastric H,K-ATPase by clotrimazole
Biochemistry
49
4524-4532
2010
Sus scrofa
brenda
Garton, N.; Bailey, N.; Bamford, M.; Demont, E.; Farre-Gutierrez, I.; Hutley, G.; Bravi, G.; Pickering, P.
Discovery of biaryl inhibitors of H+/K+ ATPase
Bioorg. Med. Chem. Lett.
20
1049-1054
2010
Sus scrofa
brenda
Abe, K.; Tani, K.; Fujiyoshi, Y.
Structural and functional characterization of H+, K+-ATPase with bound fluorinated phosphate analogs
J. Struct. Biol.
170
60-68
2010
Sus scrofa (P19156)
brenda
Tang, X.; Yang, X.; Lai, G.; Guo, J.; Xia, L.; Wu, B.; Xie, Y.; Huang, M.; Chen, J.; Ruan, X.; Sui, G.; Ge, Y.; Zuo, W.; Zhao, N.; Zhu, G.; Zhang, J.; Li, L.; Zhou, W.
Mechanism underlying hypokalemia induced by trimethyltin chloride: Inhibition of H+/K+-ATPase in renal intercalated cells
Toxicology
271
45-50
2010
Rattus norvegicus
brenda
Codina, J.; Opyd, T.S.; Powell, Z.B.; Furdui, C.M.; Petrovic, S.; Penn, R.B.; DuBose, T.D.
pH-dependent regulation of the alpha-subunit of H+-K+-ATPase (HKalpha2)
Am. J. Physiol. Renal Physiol.
301
F536-F543
2011
Rattus norvegicus
brenda
Streif, D.; Iglseder, E.; Hauser-Kronberger, C.; Fink, K.G.; Jakab, M.; Ritter, M.
Expression of the non-gastric H+/K+ ATPase ATP12A in normal and pathological human prostate tissue
Cell. Physiol. Biochem.
28
1287-1294
2011
Homo sapiens
brenda
Duerr, K.L.; Seuffert, I.; Friedrich, T.
Deceleration of the E1P-E2P transition and ion transport by mutation of potentially salt bridge-forming residues Lys-791 and Glu-820 in gastric H+/K+-ATPase
J. Biol. Chem.
285
39366-39379
2010
Rattus norvegicus (P09626)
brenda
Fang, H.; Jin, L.; Zai, W.; Song, Y.; Wang, J.; Huang, N.
Synthesis and H+/K+-ATPase inhibitory activity of 2-phenyl-6,7-dihydrobenzofuran-4(5H)-one oxime ether derivatives
AIDS Res. Hum. Retroviruses
634-638
1192-1195
2013
Homo sapiens
-
brenda
Schatzberg, D.; Lawton, M.; Hadyniak, S.; Ross, E.; Carney, T.; Beane, W.; Levin, M.; Bradham, C.
H+/K+ ATPase activity is required for biomineralization in sea urchin embryos
Dev. Biol.
406
259-270
2015
Lytechinus variegatus
brenda
Ip, Y.; Ching, B.; Hiong, K.; Choo, C.; Boo, M.; Wong, W.; Chew, S.
Light induces changes in activities of Na+/K+-ATPase, H+/K+-ATPase and glutamine synthetase in tissues involved directly or indirectly in light-enhanced calcification in the giant clam, Tridacna squamosa
Front. Physiol.
6
68
2015
Tridacna squamosa
brenda
Dach, I.; Olesen, C.; Signor, L.; Nissen, P.; le Maire, M.; M?ller, J.V.; Ebel, C.
Active detergent-solubilized H+,K+-ATPase is a monomer
J. Biol. Chem.
287
41963-41978
2012
Sus scrofa
brenda
Abe, K.; Tani, K.; Fujiyoshi, Y.
Systematic comparison of molecular conformations of H+,K+-ATPase reveals an important contribution of the A-M2 linker for the luminal gating
J. Biol. Chem.
289
30590-30601
2014
Sus scrofa
brenda
Yu, H.; Zhou, J.; Takahashi, H.; Yao, W.; Suzuki, Y.; Yuan, X.; Yoshimura, S.H.; Zhang, Y.; Liu, Y.; Emmett, N.; Bond, V.; Wang, D.; Ding, X.; Takeyasu, K.; Yao, X.
Spatial control of proton pump H,K-ATPase docking at the apical membrane by phosphorylation-coupled ezrin-syntaxin 3 interaction
J. Biol. Chem.
289
33333-33342
2014
Oryctolagus cuniculus
brenda
Liu, J.; Huang, N.; Li, N.; Liu, S.; Li, M.; Li, H.; Luo, X.; Wang, Y.; Li, L.; Zou, Q.; Liu, Y.; Yang, T.
2-(1H-benzimidazol-2-yl)-4,5,6,7-tetrahydro-2H-indazol-3-ol, a benzimidazole derivative, inhibits T cell proliferation involving H+/K+-ATPase inhibition
Molecules
19
17173-17186
2014
Homo sapiens
brenda
Wang, J.; Barbuskaite, D.; Tozzi, M.; Giannuzzo, A.; Sorensen, C.E.; Novak, I.
Proton pump inhibitors inhibit pancreatic secretion: role of gastric and non-gastric H+/K+-ATPases
PLoS ONE
10
e0126432
2015
Homo sapiens
brenda
Duerr, K.L.; Tavraz, N.N.; Friedrich, T.
Control of gastric H,K-ATPase activity by cations, voltage and intracellular pH analyzed by voltage clamp fluorometry in Xenopus oocytes
PLoS ONE
7
e33645
2012
Rattus norvegicus
brenda
Abe, K.; Tani, K.; Friedrich, T.; Fujiyoshi, Y.
Cryo-EM structure of gastric H+,K+-ATPase with a single occupied cation-binding site
Proc. Natl. Acad. Sci. USA
109
18401-18406
2012
Sus scrofa
brenda
Rakesh, K.P.; Shantharam, C.S.; Manukumar, H.M.
Synthesis and SAR studies of potent H+/K+-ATPase inhibitors of quinazolinone-Schiff's base analogues
Bioorg. Chem.
68
1-8
2016
Ovis aries
brenda
Miyazaki, H.; Wangemann, P.; Marcus, D.C.
The gastric H,K-ATPase in stria vascularis contributes to pH regulation of cochlear endolymph but not to K secretion
BMC Physiol.
17
1-1
2016
Mus musculus
brenda
Feng, X.; Liu, W.; Zeng, F.; Chen, Z.; Zhang, G.; Wu, F.
K+ Uptake, H+-ATPase pumping activity and Ca2+ efflux mechanism are involved in drought tolerance of barley
Environ. Exp. Bot.
129
57-66
2015
Hordeum vulgare
-
brenda
Xian, Y.; Zhao, X.; Wang, C.; Kang, C.; Ding, L.; Zhu, W.; Hang, S.
Phenylalanine and tryptophan stimulate gastrin and somatostatin secretion and H+-K+-ATPase activity in pigs through calcium-sensing receptor
Gen. Comp. Endocrinol.
267
1-8
2018
Sus scrofa
brenda
Badanavalu Chandrashekar, K.; Dharmesh, S.M.
Gastro protective and H+, K+-ATPase/H. pylori inhibitory properties of pectic polysaccharides from potato
Int. J. Biol. Macromol.
84
385-393
2016
Ovis aries
brenda
Jana, K.; Bandyopadhyay, T.; Ganguly, B.
Designed inhibitors with hetero linkers for gastric proton pump H+,K+-ATPase Steered molecular dynamics and metadynamics studies
J. Mol. Graph. Model.
78
129-138
2017
Sus scrofa (P19156 and P18434)
brenda
Paresi, C.J.; Liu, Q.; Li, Y.M.
Benzimidazole covalent probes and the gastric H+/K+-ATPase as a model system for protein labeling in a copper-free setting
Mol. Biosyst.
12
1772-1780
2016
Sus scrofa (P19156)
brenda
Abe, K.; Shimokawa, J.; Naito, M.; Munson, K.; Vagin, O.; Sachs, G.; Suzuki, H.; Tani, K.; Fujiyoshi, Y.
The cryo-EM structure of gastric H+,K+-ATPase with bound BYK99, a high-affinity member of K+-competitive, imidazo[1,2-a]pyridine inhibitors
Sci. Rep.
7
6632
2017
Sus scrofa (P19156 and P18434)
brenda
Dubey, V.; Han, M.; Kopec, W.; Solovyov, I.A.; Abe, K.; Khandelia, H.
K+ binding and proton redistribution in the E2P state of the H+, K+-ATPase
Sci. Rep.
8
12732
2018
Sus scrofa
brenda
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