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2'-deoxyATP + H2O + H+/in + K+/out
2'-deoxyADP + phosphate + H+/out + K+/in
ADP + H2O + H+/in + K+/out
AMP + phosphate + H+/out + K+/in
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
ATP + H2O + H+/in + Rb+/out
ADP + phosphate + H+/out + Rb+/in
-
-
-
-
?
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
GTP + H2O + H+/in + K+/out
GDP + phosphate + H+/out + K+/in
ITP + H2O + H+/in + K+/out
IDP + phosphate + H+/out + K+/in
UTP + H2O + H+/in + K+/out
UDP + phosphate + H+/out + K+/in
additional information
?
-
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
-
-
-
-
?
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
Frog
-
-
-
?
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 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
-
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
ir
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
-
-
-
?
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
-
-
-
?
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
-
-
672633, 672636, 685080, 685549, 685586, 687724, 688697, 700593, 711245, 734202, 734279, 735163 -
-
?
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
-
-
-
-
?
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
Turtle
-
-
-
?
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
-
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + H+/in + K+/out
ADP + phosphate + H+/out + K+/in
ATP + H2O + H+[side 1] + K+[side 2]
ADP + phosphate + H+[side 2] + K+[side 1]
additional information
?
-
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
-
-
-
-
?
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
-
-
-
-
ir
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
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
-
-
-
-
?
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
-
-
-
-
?
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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(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-(2',6'-dimethylbiphenyl-3-yl)-4-methylpiperazine
-
-
1-(2',6'-dimethylbiphenyl-3-yl)-N-methylmethanamine
-
-
1-hydroxy-3,5,6-tri-O-acetyl-2(3,3-dimethyl-allyl)-xanthone
-
a xanthone isolated from Calophyllum brasiliense leaves
2-(2',6'-diethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-2-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1,4,5-trimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1-methyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1-propyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-4,5-diethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)-5-phenyl-1H-imidazole
-
-
2-(2',6'-dimethylbiphenyl-3-yl)pyridin-4-amine
-
-
2-(2-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(4-ethoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(4-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1-propyl-1H-imidazole
-
-
2-(4-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(6-methoxy-2',6'-dimethylbiphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(biphenyl-3-yl)-4,5-dimethyl-1H-imidazole
-
-
2-(biphenyl-4-yl)-4,5-dimethyl-1H-imidazole
-
-
2-Methoxy-2,4-diphenyl-3-dihydrofuranone
2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
2-phenyl-6,7-dihydrobenzofuran-4(5H)-one oxime
-
-
2-[(4-[4-[4-(azidomethyl)phenoxy]butoxy]-3-methylpyridin-2-yl)methanesulfinyl]-1H-benzimidazole
inhibits ATPase activity by approximately 50% at 0.01 mM
2-[4-(2,6-dimethylphenyl)furan-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[4-(2,6-dimethylphenyl)thiophen-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[4-(benzyloxy)-2',6'-dimethylbiphenyl-3-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[4-(difluoromethoxy)-2',6'-dimethylbiphenyl-3-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)-1-benzofuran-7-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)-2,3-dihydro-1-benzofuran-7-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)furan-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-[5-(2,6-dimethylphenyl)thiophen-2-yl]-4,5-dimethyl-1H-imidazole
-
-
2-{[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}acetamide
-
-
3'-(4,5-dimethyl-1H-imidazol-2-yl)-3-methylbiphenyl-4-thiol
-
-
3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-ol
-
-
3-(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-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
3-({[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}methyl)pyridine
-
-
4,5-dimethyl-2-(2',4,5,6'-tetramethylbiphenyl-3-yl)-1H-imidazole
-
-
-
4,5-dimethyl-2-(2',6,6'-trimethylbiphenyl-3-yl)-1H-imidazole
-
-
4,5-dimethyl-2-(2'-methylbiphenyl-3-yl)-1H-imidazole
-
-
4,5-dimethyl-2-[3-(2-phenylethenyl)phenyl]-1H-imidazole
-
-
4,5-dimethyl-2-[3-(2-phenylethyl)phenyl]-1H-imidazole
-
-
4-(2',6'-dimethylbiphenyl-3-yl)-1,2-dimethyl-1H-imidazole
-
-
4-(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-(4-oxo-3,4-dihydroquinazolin-2-yl)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
5,5'-dithiobis(2-nitrobenzoic acid)
5-(2',6'-dimethylbiphenyl-3-yl)-1-methyl-1H-imidazole
-
-
6-desoxyjacareubin
-
a xanthone isolated from Calophyllum brasiliense leaves
8-(benzyloxy)-2-methylimidazo[1,2-a]pyridine
-
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
BMT-1
-
i.e. 2-(1H-benzimidazol-2-yl)-4,5,6,7-tetrahydro-2H-indazol-3-ol
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
ethyl 2-ethoxyquinoline-1(2H)-carboxylate
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
-
jacareubin
-
a xanthone isolated from Calophyllum brasiliense leaves
K+
-
activates, required. But in the presence of 200m M KCl, ion binding sites are more than 99% saturated with K+. The enzyme activity under this condition is near zero
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+
mammea A/BA
-
a coumarin isolated from Calophyllum brasiliense leaves
mammea C/OA
-
a coumarin isolated from Calophyllum brasiliense leaves
methyl {[3-(4,5-dimethyl-1H-imidazol-2-yl)-2',6'-dimethylbiphenyl-4-yl]oxy}acetate
-
-
minimiflorin
-
a flavonoid isolated from Lonchocarpus oaxacensis roots
Mn2+
-
in presence of Mg2+
mundulin
-
a flavonoid isolated from Lonchocarpus oaxacensis roots
N'-(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-chlorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
N'-(4-chlorobenzylidene)-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-hydroxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-(4-methoxybenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
N'-(4-methoxybenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-(4-nitrobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
N'-(4-nitrobenzylidene)-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N'-benzylidene-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanehydrazide
-
-
N'-benzylidene-4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
-
-
N,N'-dicyclohexylcarbodiimide
N-(2,6-dimethylbenzyl)-3-(4,5-dimethyl-1H-imidazol-2-yl)aniline
-
-
N-(2-ethyl-6-methylbenzyl)-2,3-dimethyl-6-(pyrrolidin-1-ylcarbonyl)imidazo[1,2-a]pyrazin-8-amine
-
-
N-(2-ethyl-6-methylbenzyl)-6-(methoxymethyl)-2,3-dimethylimidazo[1,2-a]pyrazin-8-amine
-
-
N-(4-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)butane hydrazide
-
-
N-(4-fluorobenzylidene)-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propane hydrazide
-
-
N-[3-(4,5-dimethyl-1H-imidazol-2-yl)phenyl]-2,6-dimethylaniline
-
-
N-[3-(4,5-dimethyl-1H-imidazol-2-yl)phenyl]benzamide
-
-
ouabagenin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
p-chloromercuribenzene sulfonate
potato galactan polysaccharide
-
potent inhibitory activity with an IC50 value of 0.42 mg/ml in vitro
-
SCH-CN-
i.e. 8-(benzyloxy)-2-methylimidazo[1,2-a]pyridine
SCH-Me-
i.e. [8-(benzyloxy)imidazo[1,2-a]pyridin-3-yl]acetonitrile
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
[(dihydroindenyl)oxy]acetic acid
-
DIOA
[8-(benzyloxy)-2-methylimidazo[1,2-a]pyridin-3-yl]acetonitrile
-
[8-(benzyloxy)imidazo[1,2-a]pyridin-3-yl]acetonitrile
-
2-Methoxy-2,4-diphenyl-3-dihydrofuranone
-
-
2-Methoxy-2,4-diphenyl-3-dihydrofuranone
-
-
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
-
-
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
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
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
Butanedione
-
-
BYK36399
-
-
Ca2+
-
2 mM, complete inhibition
diethyldicarbonate
-
-
digoxin
-
-
digoxin
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
Dipicrylamine
-
-
esomeprazole
-
-
ethyl 2-ethoxyquinoline-1(2H)-carboxylate
-
-
ethyl 2-ethoxyquinoline-1(2H)-carboxylate
-
-
F-
-
-
lansoprazole
-
-
lansoprazole
-
IC50 value of 0.0193 mg/ml
luteolin
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
-
N-methyl-BYK36399
-
-
Na+
-
above 100 mM, 60-70% inhibition
NEM
-
-
oligomycin
-
increases the phosphorylation of the enzyme and the sensitivity of the phosphorylated intermediate to AD inhibiting the conversion of E1P to E2P
Omeprazole
-
-
Omeprazole
-
inhibits HKalpha1
Omeprazole
-
acid-activated, irreversible
Omeprazole
-
binding at Cys813 and Cys892 is reversible both in vivo and in vitro
Omeprazole
-
inhibits HKalpha1
Omeprazole
-
pH-dependent inhibition
Omeprazole
-
no effect in the presence of K+ alone or NH4+. Inhibitory action can be fully reversed by addition of beta-mercaptoethanol
Ouabain
-
-
Ouabain
-
inhibits HKalpha2, but not HKalpha1
Ouabain
-
K+ exhibits strong antagonism with the inhibitor
Ouabain
-
blocks Rb+ uptake
Ouabain
-
inhibits Rb+ uptake in a dose-dependent manner
Ouabain
-
inhibits HKalpha2, but not HKalpha1
Ouabain
-
inhibition of mutant D312E/S319G/A778P/I795L/F802C, not of the wild-type enzyme
oubain
-
-
oubain
-
binding affinity of wild-type is 2000fold lower than that of mutated enzyme in NH4+-stimulated Sf9 cells
p-chloromercuribenzene sulfonate
-
-
p-chloromercuribenzene sulfonate
-
-
pantoprazole
-
-
pantoprazole
-
binding at Cys822 is irreversible
rabeprazole
-
-
rabeprazole
complete inhibition at 0.1 mM
SCH 28080
-
inhibits the NH4+-stimulated activity
SCH 28080
-
inhibits HKalpha1, but not HKalpha2
SCH 28080
-
inhibits HKalpha1, but not HKalpha2
SCH28080
-
-
SCH28080
-
potent competitive inhibitor
SCH28080
-
i.e., 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
SCH28080
IC50: 0.00041 for wild-type enzyme
SCH28080
-
K+ exhibits strong antagonism with the inhibitor
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
-
H+/K+-ATPase inhibitor
SCH28080
a K+-competitive inhibitor, SCH28080 is specific for both E2 and E2P conformations
SCH28080
-
completely blocks enzyme activity
SCH28080
specific H+,K+-ATPase inhibitor
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
SCH28080
-
i.e., 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile
timoprazole
-
-
Trypsin
-
-
-
Trypsin
-
limited proteolysis, determination of peptide fragment sequences, overview
-
vanadate
-
-
vanadate
interacts specifically with the E2 conformational state
vanadate
-
potent inhibition of catalytic and transport activities
Zn2+
-
-
additional information
-
inhibitor binding and inhibition kinetics
-
additional information
-
no inhibition by SCH-28080 and bafilomycin-A
-
additional information
-
H+/K+-ATPase inhibition does not affect Cx43 expression in chicken
-
additional information
-
almost resistant to digoxigenin and ouabagenin
-
additional information
-
inhibitor binding and inhibition kinetics
-
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
-
inhibitor binding and inhibition kinetics
-
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
-
inhibitor binding and inhibition kinetics
-
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
-
inhibitor binding and inhibition kinetics
-
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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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
0.248
3-(4-oxo-3,4-dihydroquinazolin-2-yl)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
0.241
4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanehydrazide
Ovis aries
-
at pH 7.5 and 37°C
0.04
4-coumaric acid
Ovis aries
-
pH 6.5, 37°C
1.581
6-desoxyjacareubin
Canis lupus familiaris
-
pH 7.4, 37°C
0.11
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
0.0062
AR-HO47108
Sus scrofa
-
pH 7.4, 22°C
0.0027
caffeic acid
Ovis aries
-
pH 6.5, 37°C
0.015
Cinnamic acid
Ovis aries
-
pH 6.5, 37°C
0.00075
digoxigenin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.00076
digoxin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.027
dihydro-ouabain
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.034
ferulic acid
Ovis aries
-
pH 6.5, 37°C
0.132
gallic acid
Ovis aries
-
pH 6.5, 37°C
0.059
gentisic acid
Ovis aries
-
pH 6.5, 37°C
0.0015
ginger hydrolysed phenolic fraction
Ovis aries
-
pH 6.5, 37°C
-
0.0029
ginger-free phenolic fraction
Ovis aries
-
pH 6.5, 37°C
-
0.0467
jacareubin
Canis lupus familiaris
-
pH 7.4, 37°C
0.0193
lansoprazole
Ovis aries
-
pH 6.5, 37°C
0.1095
mammea A/BA
Canis lupus familiaris
-
pH 7.4, 37°C
0.638
mammea C/OA
Canis lupus familiaris
-
pH 7.4, 37°C
0.0096
minimiflorin
Canis lupus familiaris
-
pH 7.4, 37°C
0.07
mundulin
Canis lupus familiaris
-
pH 7.4, 37°C
0.151
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+
0.41
Omeprazole
Canis lupus familiaris
-
pH 7.4, 37°C
0.0028
ouabagenin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.047
protocatechuic acid
Ovis aries
-
pH 6.5, 37°C
0.0059
SCH 32651
Sus scrofa
-
pH 7.4, 22°C
0.00041 - 0.0011
SCH28080
0.00017
strophanthidin
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.037
syringic acid
Ovis aries
-
pH 6.5, 37°C
0.097
[(dihydroindenyl)oxy]acetic acid
Sus scrofa
-
endogenous Na+,K+-ATPase
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
0.03
luteolin
Rattus norvegicus
-
-
0.03
luteolin
Oryctolagus cuniculus
-
-
0.00031
Ouabain
Rattus norvegicus
-
pH 7.0, 37°C, mutant D312E/S319G/A778P/I795L/F802C
0.0017
Ouabain
Cavia porcellus
-
pH 7.4, temperature not specified in the publication
0.06
oubain
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 100 mM Na+
0.4
oubain
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM NH4+
8
oubain
Homo sapiens
-
above, pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM K+
0.02
SCH 28080
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 100 mM Na+
0.03
SCH 28080
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM NH4+
4
SCH 28080
Homo sapiens
-
above, pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM K+
0.00041
SCH28080
Oryctolagus cuniculus
IC50: 0.00041 mM for wild-type enzyme
0.0011
SCH28080
Sus scrofa
at pH 7.6 and 37°C
0.0008
vanadate
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 100 mM Na+
0.0013
vanadate
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM NH4+
0.0016
vanadate
Homo sapiens
-
pH 7.0, 37°C, recombinant enzyme, in presence of 10 mM K+
0.0016
vanadate
Cavia porcellus
-
pH 7.4, temperature not specified in the publication
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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
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
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
-
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
E343D
low spontaneous dephosphorylation rate
E343D/E820Q
low spontaneous dephosphorylation rate
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
I795L/I798V/F802C
-
expression level rather similar to that of the recombinant enzyme, ability of binding 3(H)ouabain with high affinity
K791A/E343D
no K+-independent ATPase activity
K791A/E343D/E820Q
completely K+-insensitive
K791A/E820Q
no K+-independent ATPase activity
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/E343D
no K+-independent ATPase activity, no K+-stimulated dephosphorylation activity
K791R/E343D/E820Q
no K+-stimulated dephosphorylation activity
K791R/E820Q
some K+-independent ATPase activity, no K+-stimulated dephosphorylation activity
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
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
-
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
-
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)
E343A
-
the mutant has no activity
E343L
-
the mutant has no activity
E343Q
-
the mutation demonstrates reduced activity
E343V
-
the mutant has no activity
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
E820D
-
the mutant remains active
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)
L141A
the mutant has low ATPase activity
L141F
the mutant has low ATPase activity
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)
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
K+-stimulated ATPase acitvity hardly significant
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
rather similar properties than the K791A mutant
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
S806C
-
the mutation does not affect ion transport activity
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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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
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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
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Sus scrofa
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Rattus norvegicus
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Homo sapiens
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Sus scrofa
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Homo sapiens
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Sus scrofa
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Homo sapiens
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Homo sapiens
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Sus scrofa
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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