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Enzyme Nomenclature
Information on EC 3.6.3.9 - Na+/K+-exchanging ATPase
for references in articles please use BRENDA:EC3.6.3.9
Word Map on EC 3.6.3.9
- 3.6.3.9
- ouabain
- cardiac
-
ouabain-sensitive
- tubule
-
basolateral
- hypertension
- erythrocyte
-
influx
-
cotransporter
- epithelium
-
depolarization
-
alpha-subunits
- cl
-
electrogenic
-
hyperpolarization
-
reabsorption
-
perfuse
-
contractile
- atpases
-
sarcolemmal
- gill
- digoxin
-
voltage
- nephron
- amiloride
- aldosterone
-
transepithelial
- myocytes
- digitalis
-
ca-atpase
- mg2+-atpase
-
cardiotonic
-
normotensive
-
microelectrodes
- rb+
-
short-circuit
- na+,k+-atpase
-
inotropic
- sarcoplasmic
- vanadate
- furosemide
-
natriuresis
-
k+-dependent
-
amiloride-sensitive
-
phosphoenzyme
- bumetanide
- nai
-
voltage-clamped
- tetrodotoxin
- henle
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.6.3.9
-
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RECOMMENDED NAME
GeneOntology No.
Na+/K+-exchanging ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Na+/in + K+/out = ADP + phosphate + Na+/out + K+/in
-
-
-
-
ATP + H2O + Na+/in + K+/out = ADP + phosphate + Na+/out + K+/in
formation of a phosphorylated intermediate
-
ATP + H2O + Na+/in + K+/out = ADP + phosphate + Na+/out + K+/in
reaction sequence and transport mechanism
-
ATP + H2O + Na+/in + K+/out = ADP + phosphate + Na+/out + K+/in
the enzyme gamma subunit is located adjacent to the M2-M6-M9 pocket of the alpha subunit at the transmembrane-extracellular interface. During the E1 to E2 transition, there is no relative change in distance between the alpha and gamma subunits but there is a relative change in distance between the beta and gamma subunits
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphate bond
-
-
-
-
hydrolysis of phosphoric ester
transmembrane transport
hydrolysis of phosphoric ester
-
-
transmembrane transport
-
-
-
-
transmembrane transport
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Na+/K+-exchanging)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na+ and influx of two K+ per ATP hydrolysed. It is involved in generating the plasma membrane electrical potential.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
acclimation from fresh water to seawater is accompanied by 8fold increase in enzyme activity and 3fold increase in enzyme protein number. Enzyme activity in seawater fish is negatively correlated with basolateral membrane cholesterol content and positively correlated with phosphatidylethanolamine and linoleic acid content. Activity in freshwater fish is not correlated to any membrane lipid parameter
-
-
-
246952, 246962, 246966, 246968, 246973, 673611, 674599, 684332, 687630, 695476, 697098, 699784, 701433, 711156, 711712, 711774, 712134, 712805, 713004, 713011, 734675
-
-
-
246950, 246954, 246958, 246959, 246962, 246964, 246966, 246969, 246972, 655745, 655822, 656021, 671274, 672635, 675717, 684330, 684331, 685509, 685863, 685974, 687507, 688626, 688762, 688905, 695469, 695495, 695856, 696017, 699696, 700430, 701003, 710811, 711636, 711638, 711941, 712817, 720204, 720411, 733517, 734325, 734529, 734530, 734538, 734859, 735119, 735146, 735302
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
knockdown causes a significant depolarization of the resting membrane potential in slow-twitch fibers of skeletal muscles. Abrupt mechanosensory responses are observed in alpha2Na+/K+-ATPase-deficient embryos, possibly linked to a postsynaptic defect. The enzyme deficiency reduces the heart rate and causes a loss of left-right asymmetry in the heart tube
malfunction
-
depletion of subunit ATP1a1 reduces the level of active Rab27a in melanocytes and ist targeting to melanosomes
malfunction
-
knocking down of catalytic subunit ATPalpha, but not alpha-like, in the entire Johnston's organ results in complete deafness. Knocking down beta subunit nrv2 in scolopale cells reduces ATPalpha expression in scolopale cells and causes almost complete deafness
metabolism
-
in vivo administration of isovaleric acid inhibits the citric acid cycle probably through the enzyme citrate synthase, as well as Na+,K+-ATPase, a crucial enzyme responsible for maintaining the basal potential membrane necessary for a normal neurotransmission, inhibition of these activities may be involved in the pathophysiology of the neurological dysfunction of isovaleric academic patients. Isovaleric acidemia is an autosomal recessive inherited metabolic disorder of leucine metabolism caused by a deficiency of isovaleryl-CoA dehydrogenase
metabolism
-
the enzyme is tightly coupled to glycolysis with undetectable flux of ATP between mitochondria and the enzyme
physiological function
-
Na+, K+-ATPase plays an important role in pulmonary inflammation
physiological function
-
Na+, K+-ATPase plays a role in regulating electrolyte concentration in the lens, contributing to lens transparency, and is involved in cataract formation caused by prolonged use of glucocorticoids, that suppress the Na+,K+-ATPase in the lens, overview
physiological function
-
inactivation of Na+, K+-ATPase leads to partial membrane depolarization allowing excessive Ca2+ entry inside neurons with resultant toxic events such as excitotoxicity
physiological function
-
Na/K-ATPase is a plasma membrane protein complex transferring the stored energy of ATP to the active transport of Na+ and K+ ions across the cell membrane. The generated electrochemical gradient is essential for a number of other cellular functions
physiological function
-
Na/K-ATPase is a plasma membrane protein complex transferring the stored energy of ATP to the active transport of Na+ and K+ ions across the cell membrane. Na/K-ATPase alpha1 isoform modulates signaling mechanisms leading to apoptosis, cell migration, and cell proliferation
physiological function
Na+,K+-ATPase is responsible for establishing Na+ and K+ concentration gradients across the plasma membrane and therefore plays an essential role in, for instance, generating action potentials
physiological function
-
Klotho is a transmembrane protein with particularly strong expression in kidney, parathyroid glands and choroid plexus. Klotho-hypomorphic mice suffer from renal salt wasting and hypovolemia despite hyperaldosteronism. Na+/K+ ATPase protein abundance in isolated collecting ducts is lower in Klothohm mice than in their wild type littermates
physiological function
-
Klotho is a transmembrane protein with particularly strong expression in kidney, parathyroid glands and choroid plexus. Expression of Klotho in Xenopus oocytes increases the Na+/K+ ATPase pump current. Treatment of Xenopus oocytes with Klotho protein similarly increases the pump current
physiological function
-
the degree of activation of Na+/K+-ATPase at physiological Na+-concentrations differs between oxidative and glycolytic muscles and between subcellular membrane domains with different isoform compositions
physiological function
-
the beta subunits of the enzyme play a role in tissues during development and osmoregulation with beta1 subunits involved in the adaptation to hyperosmotic conditions and beta3 subunits to hypoosmotic environments
physiological function
function of Na+,K+ ATPase Atp1a1 in the elongation of the zebrafish heart tube. Embryos lacking Atp1a1 function exhibit abnormal migration behavior of cardiac precursors, defects in the elongation of the heart tube, and a severe reduction in extracellular matrix/fibronectin deposition around the myocardium. Atp1a1 is expressed in an extraembryonic tissue, the yolk syncytial layer, at earlier stages. Knockdown of Atp1a1 activity specifically in the yolk syncytial layer produces heart tube elongation defects like those found in atp1a1 mutants
physiological function
-
nuclear Na+/K+-ATPase plays an active role in nucleoplasmic Ca2+ homeostasis
physiological function
-
alpha2Na+/K+-ATPase is important for skeletal and heart muscle function
physiological function
-
the neuronal glycine transporter GlyT2 function is strictly coupled to the sodium electrochemical gradient actively generated by the Na/K-ATPase
physiological function
-
the Na+/K+-ATPase-alpha1 isoform is specifically involved in detection of extracellular Na+ concentration
physiological function
-
Na+,K+-ATPase functionally interacts with the plasma membrane Na+,Ca2+ exchanger to prevent Ca2+ overload and neuronal apoptosis in excitotoxic stress
physiological function
the enzyme maintains intracellular Na+ and K+ homeostasis and clears extracellular K+ after electric organe discharge
physiological function
-
subunit ATP1a1 plays an essential role in Rab27a-dependent melanosome transport. The subunit is essential for targeting and activation of Rab27a to melanosomes
physiological function
-
the Na+K+-ATPase vascular functional activity is greater in male than femals rats
physiological function
-
the catalytic subunit ATPalpha is required for hearing
physiological function
-
in addition to its role as a sodium pump regulating sperm motility, Na+/K+-ATPase is also involved as a signalling molecule during sperm capacitation
additional information
-
odoroside A and ouabain potently reduce NF-kappaB-inducible de novo protein synthesis, largely due to its ability to block Na+-dependent transport of amino acids across the plasma membrane, but not to interfering with the translation machinery
additional information
-
Na+,K+-ATPase alpha1 subunit is one of the targets for reactive oxygen species and is directly involved in oxidative stress. alpha1 Subunit level decrease after fluid percussion injury inducing traumatic brain injury in rats, overview. Physical training is effective against Na+,K+-ATPase enzyme activity inhibition, while fluid percussion injury induces a decrease in Na+,K+-ATPase activity in the ipsilateral cerebral cortex of sedentary animals
additional information
-
Na+, K+-ATPase inhibition by cardiotonic steroids increases COX-2 expression in A-549 cells, overview
additional information
-
ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum. The inhibitory effect is abolished by chelator of intracellular-free calcium BAPTA-AM, Ca2+ channel blocker nicardipine, inositol 1,4,5-trisphosphate receptor blocker 2-aminoethyl diphenyl borate, and PI3 kinase inhibitor wortmannin, overview
additional information
-
ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum. The inhibitory effect is abolished by chelator of intracellular-free calcium BAPTA-AM, Ca2+ channel blocker nicardipine, inositol 1,4,5-trisphosphate receptor blocker 2-aminoethyl diphenyl borate, and PI3 kinase inhibitor wortmannin, overview
additional information
-
the Na/K-ATPase-derived, membrane-bound peptide inhibits the activity of Src kinase targeting the Na/K-ATPase/Src receptor complex and antagonizing ouabain-induced protein kinase cascades in rat cardiomyocytes, molecular mechanism of Na/KATPase-mediated Src regulation, overview. NaKtide does not directly affect the ERK and protein kinase C family of kinases. It inhibits Lyn with a much lower potency with IC50 of 0.0025 mM
additional information
-
Na+,K+-ATPase inhibitor ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. KN93 prevents ouabain-induced apoptosis without affecting inotropy
additional information
-
Na+,K+-ATPase inhibitor ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. KN93 prevents ouabain-induced apoptosis without affecting inotropy
additional information
-
Na+,K+-ATPase inhibitor ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. KN93 prevents ouabain-induced apoptosis without affecting inotropy
additional information
-
crucial role for Na+/K+-ATPase activity in determining neuronal vulnerability to domoic acid-mediated excitotoxicity. The enzyme inhibitor palytoxin enhances vulnerability of cultured cerebellar neurons to domoic acid via sodium-dependent mechanisms, overview
additional information
-
inhibition of proliferation of Panc-1 cells by oleandrin is significantly reduced when the relative expression of subunit alpha3 is decreased or when the expression of the alpha1 isoform is increased
additional information
-
ethanol-induced Na+,K+-ATPase inhibition leads to cerebellar dysfunction causing motor coordination impairments and cognitive deficits, and may also contribute to neuronal function alterations in other brain regions, overview. Ethanol increases firing frequency and regularity of spontaneous firing in presence of neurotransmitter receptor antagonists, ethanol increases spontaneous firing frequency and depolarizes the membrane potential, overview
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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
ADP + phosphate + 3 Na+/out
ATP + 3 Na+/in
-
in the absence of K+ and in the presence of ATP and ADP without net ATP hydrolysis
transphosphorylation of ATP/ADP
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
r
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
-
reaction obeys Michaelis-Menten kinetics
-
-
?
ATP + 3 Na+/in
ADP + phosphate + 3 Na+/out
-
enzyme has a high- and a low-affinity ATP hydrolizing site
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
formation of a phosphorylated intermediate
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
a continous Na+ influx exists across the plasma membrane in the presence of external Na+. When Na+ is removed from both external and internal solutions, a transient outward pump current is observed by adding K+ to the external solution, thus indicating that the transient pump current is activated by the residual intracellular Na+
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
enzyme does not show a distinct voltage dependency either with or without extracellular Na+. In presence of extracellular Na+ a steady Na+-K+ pump current exists even in absence of internal Na+. A steady Na+-K+ pump current is observed with 10 mM intracellular Na+
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
enzyme plays a crucial role in cellular ion homeostasis
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
may not play a significant role in adaption in freshwater crustaceans
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
for each ATP molecule hydrolyzed three Na+ ions are transported out of and two K+ ions into the cell
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
creation of a electrochemical gradient of Na+ ions into and K+ ions out of the cell
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
246950, 246954, 246958, 246959, 246962, 246964, 246966, 246969, 246972, 695469, 695495, 712134, 712794, 713007, 713111, 713119, 733517, 734325, 734529, 734530, 734538, 735119, 735146, 735302
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
modelling of enzyme function in neurons in absence or presence of ethanol, overview
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
shark
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + Rb+/out
ADP + phosphate + Na+/out + Rb+/in
-
measurement of enzyme activity by ouabain-sensitive 86Rb+ uptake
-
-
?
ATP + H2O + Na+/in + Rb+/out
ADP + phosphate + Na+/out + Rb+/in
-
measurement of enzyme activity by ouabain-sensitive Rb+ uptake
-
-
?
ATP + Na+/in
ADP + phosphate + Na+/out
-
under saturating Mg2+, Na+, and K+ conditions, enzyme exhibits two well-defined ATP hydrolyzing sites. At the high-affinity sites, K0.5 value is 63.8 nmol per l, at the low-affinity sites, hydrolysis follows Michaelis-Menten kinetics
-
-
?
additional information
?
-
-
Na+K+-ATPase actively participates in the regulation of endosomal pH value and endocytosed membrane traffic
-
-
-
additional information
?
-
-
the enzyme also catalyzes: 1. uncoupled Na+ efflux in presence of Na+/in, Mg2+ and ATP, 2. Na+-dependent ADP/ATP exchange, 3. K+-dependent enzyme phosphorylation by phosphate
-
-
-
additional information
?
-
-
assay using solid-supported membrane, overview
-
-
-
additional information
?
-
-
electrogenic Na+K+-ATPase partially contributes to the ustained hyperpolarization of endothelial cells in response to acetylcholine
-
-
-
additional information
?
-
-
subunit isoform alpha2 abundance is higher in the t-tubules than in the surface sarcolemma. The isoform is functinally coupled to the Na+/Ca2+-exchanger and can regulate Ca2+ handling without changing global concentration of Na+
-
-
-
additional information
?
-
-
K+-dependent ATPase activity in absence of Na+ at acid pH, protons can be transported by the sodium pump in place of Na+
-
-
-
additional information
?
-
-
the Na/K-ATPase-derived, membrane-bound peptide inhibits the activity of Src kinase targeting the Na/K-ATPase/Src receptor. ND1 as a Src-interacting domain from the Na/K-ATPase alpha1 subunit, overview
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
r
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
-
-
-
?
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
-
each cycle extrudes 3 Na+ from the cell and moves 2 K+ into the cell with utilization of 1 ATP
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
Q98SL3
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
enzyme plays a crucial role in cellular ion homeostasis
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
may not play a significant role in adaption in freshwater crustaceans
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
creation of a electrochemical gradient of Na+ ions into and K+ ions out of the cell
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
T2B3R7
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
modelling of enzyme function in neurons in absence or presence of ethanol, overview
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
Q4H132
-
-
-
?
ATP + H2O + Na+/in + K+/out
ADP + phosphate + Na+/out + K+/in
-
-
-
-
?
additional information
?
-
-
Na+K+-ATPase actively participates in the regulation of endosomal pH value and endocytosed membrane traffic
-
-
-
additional information
?
-
-
electrogenic Na+K+-ATPase partially contributes to the ustained hyperpolarization of endothelial cells in response to acetylcholine
-
-
-
additional information
?
-
-
subunit isoform alpha2 abundance is higher in the t-tubules than in the surface sarcolemma. The isoform is functinally coupled to the Na+/Ca2+-exchanger and can regulate Ca2+ handling without changing global concentration of Na+
-
-
-
additional information
?
-
-
the Na/K-ATPase-derived, membrane-bound peptide inhibits the activity of Src kinase targeting the Na/K-ATPase/Src receptor. ND1 as a Src-interacting domain from the Na/K-ATPase alpha1 subunit, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cr3+
-
causes oxidative stress in fish and leads to reduced enzyme activity in the brain, mechanism, overview. The level of ATP production in brain mitochondria may be an important criteria in the CrIII induced inhibition of Na+K+ATPase activity of fish brain, reduction of Na+K+ATPase activity is partially mediated by lipid peroxidation and deficient mitochondrial electron transport chain activity. Also direct interaction of CrIII ion with the -SH group of Na+K+ATPase enzyme might play a role
Cs+
-
the Na,K pump is activated by the combined effect of Na+ on the cytoplasmic side and of K+ on the extracellular side of the membrane. K+ can be replaced by the following monovalent cations in the order of decreasing activation: K+, Rb+, NH4+, Cs+, Li, Na+
K+
Li+
-
the Na,K pump is activated by the combined effect of Na+ on the cytoplasmic side and of K+ on the extracellular side of the membrane. K+ can be replaced by the following monovalent cations in the order of decreasing activation: K+, Rb+, NH4+, Cs+, Li, Na+
Mg2+
Na+
NH4+
Rb+
-
the Na,K pump is activated by the combined effect of Na+ on the cytoplasmic side and of K+ on the extracellular side of the membrane. K+ can be replaced by the following monovalent cations in the order of decreasing activation: K+, Rb+, NH4+, Cs+, Li, Na+
additional information
K+
-
the KCl concentration giving the half-maximal activity i 1.2 mM. The Na+:K+ ratios giving the maximal activity are 1:3 to 3:1
K+
-
stimulation, following a single saturation curve. Synergistic effects of K+ and NH4+
K+
-
stimulation, following a single saturation curve. Synergistic effects of K+ and NH4+. Km value 1.5 mM
K+
-
completely abolishes oubain binding to alpha1-beta1 isoenzymes. Residual oubain binding is still observed at high K+ concentrations for alpha2-beta1 and alpha3-beta1 complexes
K+
-
stimulation, synergistic effect of NH4+ and K+. Enzyme exhibits a single K+ binding site, NH4+ binding to a second, exlcusive site
K+
-
K+ and NH4+ (1-20 mM each) synergistically stimulate enzyme activity (about 25%)
K+
-
the Na,K pump is activated by the combined effect of Na+ on the cytoplasmic side and of K+ on the extracellular side of the membrane. K+ can be replaced by the following monovalent cations in the order of decreasing activation: Rb+, NH4+, Cs+, Li, Na+
Mg2+
-
the optimal concentration of MgCl2 is 3 mM in presence of 10 mM NaCl and 30 mM KCl
Mg2+
-
stimulation, following a single saturation curve. K0.5 value 0.36 mM
Na+
-
the NaCl concentration giving the halfmaximal activity is 6.0 mM. The Na+:K+ ratios giving the maximal activity are 1:3 to 3:1
Na+
-
the Na,K pump is activated by the combined effect of Na+ on the cytoplasmic side and of K+ on the extracellular side of the membrane. Na+ cannot be replaced by any other monovalent cation. K+ can be replaced by the following monovalent cations in the order of decreasing activation: K+, Rb+, NH4+, Cs+, Li, Na+
NH4+
-
K+ and NH4+ (1-20 mM each) synergistically stimulate enzyme activity (about 25%)
NH4+
-
the Na,K pump is activated by the combined effect of Na+ on the cytoplasmic side and of K+ on the extracellular side of the membrane. K+ can be replaced by the following monovalent cations in the order of decreasing activation: K+, Rb+, NH4+, Cs+, Li, Na+
additional information
-
CaCl2 up to 300 microM does not affect Na+/K+-ATPase activity, but CaCl2 above 1 mM inhibits the activity
additional information
-
K+ plus NH4+ do not synergistically stimulate (Na+, K+)-ATPase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-2,3a,11,11a-tetrahydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
(1R,2R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)-2-(2-oxopropanoyl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-13a-formyl-3a,11a-dihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-11-yl beta-D-glucopyranoside
-
-
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
-
-
1,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
i.e. wedelolactone, inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
1-chloro-2,4-dinitrobenzene
-
inhibition of the transport activity of the Na-K pump
19-hydroxy-2''-oxovoruscharin
-
i.e. UNBS1450, a trans-trans-cis cardiotonic steroid
1H-[1,2,4]oxadiazole[4,3-a]quinoxalin-1-one
-
ODQ, inhibition of SNP-induced pump stimulation
2,3-dihydroxy-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
2,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
2,9-dihydroxy-3,8-dimethoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
2-aminoethyl-methanethiosulfonate
-
inhibition of mutants F323C, P333C, E334C, G335C, I322C, G326C and A330C
3,8,9-trihydroxy-2-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
-
inhibitor of kidney Na+K+-ATPase and ligand for the central benzodiazepine receptor
3-[(2-O-D-glucopyranosyl-D-glucopyranosyl)oxy]-12-hydroxydammar-24-en-20-yl D-glucopyranoside
-
-
4-[(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-13a-(hydroxymethyl)-9,15a-dimethylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
-
-
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
-
-
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
-
-
5-hydroxydecanoate
-
presence of 5 mM ATP, inhibitory above 1 mM. Presence of 0.05 mM ATP, inhibitory above 0.25 mM. No effect on ouabain-sensitiviy of the enzyme
8-methoxycoumestrol
-
inhibits the isozyme alpha1beta1 Na,K-ATPase, mechanism, overview
A-769662
-
inhibits the Na+-K+-ATPase transport activity and cell surface abundance in L6 cells, which is independent of AMP kinase activation, overview
astragaloside III
-
from dried roots of Astragalus membraneceus or var. mongholicus
benzyltriethylammonium chloride
-
inhibition of pump current is dependent on membrane potential
epicatechin-3-gallate
-
solubilization of the Na+,K+-ATPase with a nonionic detergent reduces sensitivity to epigallocatechin-3-gallate
epigallocatechin-3-gallate
-
noncompetitive with respect to ATP, reduces the affinity for vanadate, shifts the equilibrium of E1P and E2P toward E1P, and reduces the rate of the E1P to E2P transition
ethanol
-
inhibits the enzyme in Golgi membranes of cerebellar neurons leading to potentiation of GABAergic transmission at Golgi cell-to-granule cell synapses throughan increase in Golgi cell excitability
ethylester of glutathione
-
inhibition of the transport activity of the Na-K pump
fenoldopam
-
induces inhibition of Na+ ?K+-ATPase activity in HK-2 cells. Ouabain protects against the cyclic adenosine monophosphate accumulation and Na+ ?K+-ATPase inhibition induced by the D1 receptor agonist fenoldopam in HK-2 cells. Chronic ouabain treatment decreases the protein and mRNA expression levels of the D1 receptor and increases the basal phosphorylation of the D1 receptor in HK-2 cells
genistein
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
glyburide
-
presence of 5 mM ATP, slightly stimulating up to 1 mM, inhibitory above. Presence of 0.05 mM ATP, stimulating at least up to 3 mM
glycyrrhizin
-
from roots of Glycyrrhiza uralensis , Glycyrrhiza inflata, or Glycyrrhiza glabra
herbimycin A
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
isovaleric acid
-
isovaleric acid injection significantly inhibits Na+,K+-ATPase activity by 25% in cerebral cortex of rats 2 or 24 h after administration, while pre-treatment of rats with creatine completely prevents the inhibitory effects of isovaleric acid on Na+,K+-ATPase
lauric acid
-
presence of 5 mM ATP, inhibitory above 0.25 mM. Presence of 0.05 mM ATP, stimulating up to 0.3 mM, inhibitory above
lavendustin A
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
Lyn kinase
-
Lyn kinase directly binds to the Na+,K+-ATPase alpha3 subunit for regulation of activity
-
m-trifluoromethyl-diphenyl diselenide
-
i.e. (m-CF3C6H4Se)2, activity is restored by DTT
MTSET
-
[2-(trimethylammonium)ethyl]methanethiosulphonate bromide, inhibits mutants G803C, V805C
odoroside A
-
i.e. 3beta-O-(beta-D-diginosyl)-14-hydroxy-5beta,14beta-card-20(22)-enolide, isolated from the stems and twigs of Nerum oleander, inhibits the enzyme's ATPase activity
p-chloro-diphenyl diselenide
-
i.e. (p-ClC6H4Se)2, activity is restored by DTT
p-methoxyl-diphenyl diselenide
-
i.e. (p-CH3OC6H4Se)2, activity is restored by DTT
Pb2+
-
inhibitory effect of Pb2+ on the transport cycle of the Na+,K+-ATPase, overview. Pb2+ inhibits cycling of the enzyme, but it does not affect cytoplasmic Na+ binding and release of Na+ ions at the extracellular side at concentrations below 0.010 mM
reduced glutathione
-
extracellular and, or intracellular, inhibition of the transport activity of the Na-K pump
saikosaponin A
-
from dried roots of Bupleurum chinense or Bupleurum scorzonerifolium
tetraethylammonium chloride
-
inhibition of pump current is independent on membrane potential
Tumor necrosis factor alpha
-
TNF-alpha, TNF-alpha affects the Na+-K+ pump via PGE2-dependent pathways
-
[PdCl(dien)]+
-
noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition
[PdCl(Me4dien)]+
-
noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition
-
[PdCl4]2-
-
noncompetitive, affinity for binding in decreasing order: [PdCl4]2-, [PdCl(dien)]+, [PdCl(Me4dien)]+. Addition of L-cysteine or glutathoione before exposure to Pd(II) complexes prevents inhibition
BAY-K8644
-
a calcium channel agonist, the effect is blocked by a phosphatidylinositol-3 kinase inhibitor wortmannin
BAY-K8644
-
a calcium channel agonist, the effect is blocked by a phosphatidylinositol-3 kinase inhibitor wortmannin
bufalin
-
inhibition of the enzyme, enhancement of the acidification of the late endosome, alteration in membrane traffic
Ca2+
-
CaCl2 up to 300 microM does not affect Na+/K+-ATPase activity, but CaCl2 above 1 mM inhibits the activity
Ca2+
-
enzyme from anterior intestine is 5-fold more sensitive than enzymes from pyloric caeca and posterior intestine
Na/K ATPase-alpha1-specific siRNA A1
-
0% decreases in expression of human alpha subunit in 293T cells
-
Na/K ATPase-alpha1-specific siRNA A2
-
20% decreases in expression of human alpha subunit in 293T cells
-
Na/K ATPase-alpha1-specific siRNA A3
-
20% decreases in expression of human alpha subunit in 293T cells
-
Na/K ATPase-alpha1-specific siRNA A4
-
40% decreases in expression of human alpha subunit in 293T cells
-
oleandrin
-
oleandrin treatment results in selective inhibition of human cancer cell growth but not rodent cell proliferation, which corresponds to the relative level of Na,K-ATPase alpha3 subunit protein expression. A correlation is observed between the ratio of alpha3 to alpha1 isoforms and the level of oleandrin uptake during inhibition of cell growth and initiation of cell death, the higher the alpha3 expression relative to alpha1 expression, the more sensitive the cell is to treatment with oleandrin
oleandrin
-
oleandrin treatment results in selective inhibition of human cancer cell growth but not rodent cell proliferation, which corresponds to the relative level of Na,K-ATPase alpha3 subunit protein expression. A correlation is observed between the ratio of alpha3 to alpha1 isoforms and the level of oleandrin uptake during inhibition of cell growth and initiation of cell death, the higher the alpha3 expression relative to alpha1 expression, the more sensitive the cell is to treatment with oleandrin
oligomycin
-
inhibits (Na+,K+)-ATPase reaction and Na+-ATPase reaction, has little effect on the K+-phosphatase reaction and can stimulate the ADP/ATP exchange reaction
oligomycin
-
not completely inhibits but decreases the rate of turnover of transport and of the hydrolysis reaction. Oligomycin affects the extracellular side of the system, Na+ on the cytoplasmic side of the system is necessary for the effect, oligomycin decreases the rate of transition from the Na+ form to the K+ form of the enzyme, but has no effect on the rate of the reverse reaction
Ouabain
-
ouabain up to 1 mM decreases silkworm ATPase activity to 42% of the maximal ATPase activity in presence of 10 mM NaCl and 30 mM KCl
Ouabain
-
ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. The NCX inhibitor KB-R7943 and by the CaMKII inhibitors, KN93 and AIP prevent ouabain-induced apoptosis without affecting inotropy. Ouabain produces in the cat at 25 nM a 43% decrease in cell viability due to apoptosis and necrosis
Ouabain
-
inhibition of enzyme, enhancement of the acidification of the late endosome
Ouabain
-
ouabain does not affect TNF-alpha-induced mRNA expression but inhibits TNF-alpha-induced protein expression
Ouabain
-
interaction is dependent on the conformation and phosphorylation state of the protein
Ouabain
-
ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis.The NCX inhibitor KB-R7943 and by the CaMKII inhibitors, KN93 and AIP prevent ouabain-induced apoptosis without affecting inotropy
Ouabain
-
ouabain triggers an apoptotic cascade that involves NCX and CaMKII as a downstream effector. Ouabain simultaneously activates an antiapoptotic cascade involving PI3K/AKT which is however, insufficient to completely repress apoptosis. The NCX inhibitor KB-R7943 and by the CaMKII inhibitors, KN93 and AIP prevent ouabain-induced apoptosis without affecting inotropy. Ouabain produces in the rat at 0.002 mM a 43% decrease in cell viability due to apoptosis and necrosis
Ouabain
-
-
671274, 673231, 675717, 675725, 695469, 695856, 696017, 699696, 700430, 701003, 710811, 713119, 734325, 734538, 735119
Ouabain
-
enzyme from anterior intestine is ten-fold more sensitive than enzymes from pyloric caeca and posterior intestine
Ouabain
a cardiac glycoside derived from Strophanthus gratus, ouabain is deeply inserted into the transmembrane domain with the lactone ring very close to the bound K+. Low-affinity ouabain-bound state due to antagonism between ouabain and K+. The closure of the binding cavity confers a high affinity, homology model for the high affinity state, structures, overview. Binding of sugar moiety and steroid core, overveiw
Ouabain
-
about 50% inhibition at 3 mM, ouabain inhibition increases about 80% in the presence of NH4+ with a 3fold lower KI value
oubain
-
K+ completely abolishes oubain binding to alpha1-beta1 isoenzymes. Residual oubain binding is still observed at high K+ concentrations for alpha2-beta1 and alpha3-beta1 complexes
oubain
-
quantitative aspects of the interaction between oubain and the enzyme in vitro
palytoxin
-
mild, non-toxic, exposures to the Na+/K+-ATPase inhibitor palytoxin synergistically sensitizes the vulnerability of neurons to normally non-toxic concentrations of domoic acid, leaving NMDA receptor-mediated excitotoxic response unaltered. Palytoxin causes a voltage-sensitive Na+ channel-independent increase in intracellular Na+. Enhancement of the excitotoxic response to domoic acid by palytoxin is time-dependent and is not affected by gene expression inhibitors
perillyl alcohol
-
a monoterpene, inhibits Na/K-ATPase, non-competitive inhibition for Na+ and K+ and an uncompetitive inhibition for ATP in brain and kidney
perillyl alcohol
-
a monoterpene, inhibits Na/K-ATPase showing a noncompetitive inhibition profile to Na+ and K+ and an uncompetitive inhibition towards ATP. The generated electrochemical gradient is essential for a number of other cellular functions
strophanthidin
-
tyrosine kinase inhibitor, block phosphorylation of alpha-subunit of the Na+,K+-ATPase
vanadate
-
20fold less sensitive to vanadate than alpha1 and 3; 20 times more sensitive to vanadate than alpha2
vanadate
-
epigallocatechin-3-gallate reduces the affinity for vanadate, shifts the equilibrium of E1P and E2P toward E1P, and reduces the rate of the E1P to E2P transition
additional information
-
not inhibitory: NH4+. At elevated concentrations of NH4+, enzyme is fully active and K+ cannot displace NH4+ from its exclusive binding sites
-
additional information
-
odoroside A and ouabain potently reduce NF-kappaB-inducible de novo protein synthesis, largely due to its ability to block Na+-dependent transport of amino acids across the plasma membrane, but not to interfering with the translation machinery
-
additional information
-
ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum
-
additional information
-
inhibitory potencies of cardenolide glycosides, isolated from the roots of Pergularia tomentosa, on Na+,K+-ATPase activity
-
additional information
-
enzyme activity is inhibited by excess ATP
-
additional information
-
decrease in extracellular pH inhibits Na+-K+ pump activity
-
additional information
-
physical training is effective against Na+,K+-ATPase enzyme activity inhibition, while fluid percussion injury induces a decrease in Na+,K+-ATPase activity in the ipsilateral cerebral cortex of sedentary animals
-
additional information
-
ETB receptor inhibits Na+-K+ ATPase activity by facilitating extracellular Ca2+ entry and Ca2+ release from endoplasmic reticulum
-
additional information
cardiac glycosides are efficient inhibitors of the Na+,K+-ATPase
-
additional information
-
molecular docking and modelling, and inhibitory potencies of steroid-like compounds from Chinese medicinal products, used for promoting the blood circulation, with Na+,K+-ATPase, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-chloro-2,4-dinitrobenzene
-
increase of the hydrolytic activity of the Na/K ATPase
4-aminobutyric acid
-
hypothesis: stimulate Na+/K+ transport via specific receptor inputs
8-pCPT-CGMP
-
induces a concentration-dependent increase in pump current, activator of PKG
Baclofen
-
hypothesis: stimulate Na+/K+ transport via specific receptor inputs
beta-catenin
-
expression of beta-catenin significantly enhances the ouabain-sensitive current of the endogeneous Na+/K+-ATPase. beta-Catenin does not significantly modify the retrieval of the Na+/K+ ATPase from the cell membrane. The stimulating effect of beta-catenin on both Na+/K+ ATPase and Na+-coupled glucose transporter SGLT1 activity is observed even in the presence of actinomycin D
-
desipramine
-
inhibitor of adrenalin uptake and antidepressive action. Treatment differentially enhances the activity of Na+K+-ATPase alpha isoforms
dexamethasone
-
postnatal treatment of lamb with 0.5 mg per kg results in 21.4% increase in Na+K+-ATPase activity and a 30.4% increase in catalytic subunit alpha1 expression in the cerebral cortex. Treatment is not associated with significant changes in subunit beta1 expression. In the kidney, dexamethasone treatment is not associated with significant changes in enzyme activity, or alpha-1- or beta-1-isoform expression
epinephrine
-
hypothesis: stimulate Na+/K+ transport via specific receptor inputs
glyburide
-
presence of 5 mM ATP, slightly stimulating up to 1 mM, inhibitory above. Presence of 0.05 mM ATP, stimulating at least up to 3 mM
interleukin-2
-
increases transport activity of the Na/K pump and the content of Na,K-ATPase alpha1 protein
-
lauric acid
-
presence of 5 mM ATP, inhibitory above 0.25 mM. Presence of 0.05 mM ATP, stimulating up to 0.3 mM, inhibitory above
Lyn kinase
-
Lyn kinase directly binds to the Na+,K+-ATPase alpha3 subunit for regulation of activity
-
norepinephrine
-
hypothesis: stimulate Na+/K+ transport via specific receptor inputs
sodium nitroprusside
-
SNP, NO donor, not a simple concentration-dependent effect on pump current
NH4+
-
stimulation, following a single saturation curve. Synergistic effects of K+ and NH4+. At elevated concentrations of NH4+, enzyme is fully active and K+ cannot displace NH4+ from its exclusive binding sites
NH4+
-
stimulation, following a single saturation curve. Synergistic effects of K+ and NH4+. Km value 4.5 mM
NH4+
-
stimulation, synergistic effect of NH4+ and K+. Enzyme exhibits a single K+ binding site, NH4+ binding to a second, exlcusive site
Ouabain
-
pretreatment of HK-2 cells with ouabain increases the Na+K+ATPase activity and inhibits the inhibitory effect of the D1 receptor on enzyme levels and activity, overview
additional information
-
the distal tube and collecting duct cells show more intense Na+/K+-ATPase immunoreaction in freshwater eel than in seawater-acclimated eel
-
additional information
the alpha-subunit is 2-fold more abundant in seawater-acclimated salt glands than in freshwater-acclimated glands. There is no increase in the specific activity of NKA in seawtaer-acclimated animals and the in vitro rate of oxygen consumption by salt gland slices from seawater-acclimated animals is not significantly different from that of Ffreshwater-acclimated animals
-
additional information
-
the alpha-subunit is 2-fold more abundant in seawater-acclimated salt glands than in freshwater-acclimated glands. There is no increase in the specific activity of NKA in seawtaer-acclimated animals and the in vitro rate of oxygen consumption by salt gland slices from seawater-acclimated animals is not significantly different from that of Ffreshwater-acclimated animals
-
additional information
-
half activated by a membrane potential of about -65 mV
-
additional information
-
increase in extracellular pH potentiates Na+-K+ pump activity
-
additional information
-
The Na+-affinity is higher in oxidative muscle compared with glycolytic muscle and in purified membranes from oxidative muscle compared with glycolytic muscle
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.92
K+
-
apparent dissociation constant in the presence of 2 mM spermidine
0.46
K+/out
enzyme from main electric organ, at pH 7.2 and 25°C
1.2
K+/out
enzyme from Sach's electric organ, at pH 7.2 and 25°C
1.47
K+/out
enzyme from Hunter's electric organ, at pH 7.2 and 25°C
5.35
Na+
-
apparent dissociation constant in the presence of 2 mM spermidine
6.3
Na+
-
white vastus lateralis, total membranes, after exercise (running)
8.3
Na+
-
extensor digitorum longus, total membranes, after exercise (running)
11.6
Na+
-
glycolytic fiber, sarcolemmal membrane, after exercise (running)
7.47
Na+/in
enzyme from main electric organ, at pH 7.2 and 25°C
8.6
Na+/in
-
posterior gill, juvenile crab acclimated to dilute seawater of 150 mOsm, pH 7.4
18.14
Na+/in
enzyme from Hunter's electric organ, at pH 7.2 and 25°C
21.3
Na+/in
-
anterior gill, sub-adult crab acclimated to dilute seawater of 150 mOsm, pH 7.4
24.2
Na+/in
enzyme from Sach's electric organ, at pH 7.2 and 25°C
additional information
additional information
-
1.72 mmol/l with p-nitrophenyl phosphate as substrate, 0.165 mmol/l with ATP as substrate
-
additional information
additional information
-
changes in alphabetagamma stoichiometry of Na+K+-ATPase do not alter Km1 value for ATP, and slightly increase km², but Vmax decreases at both catalytic and regulatory sites
-
additional information
additional information
-
presence of phospholemman raises the K0.5 value for Na+ ions. Different functional effects depend on the degree of phosphorylation of phospholemman at residue S68
-
additional information
additional information
-
presence of phospholemman lowers the K0.5 value for Na+ ions by about 30%, but does not affect the turnover rate or Km value of ATP. Different functional effects depend on the degree of phosphorylation of phospholemman at residue S68
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20.1
Na+/in
maximum turnover rate per pump, pH not specified in the publication, 22°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4
benzyltriethylammonium chloride
-
half maximum inhibition of Na,K-pump current
26.6
tetraethylammonium chloride
-
half maximum inhibition of Na,K-pump current
additional information
additional information
-
0.05 mmol/l with ATP as inhibitor, 0.762 mmol/l with ouabain as inhibitor, 0.00025 mmol/l with o-vanadate as inhibitor
-
additional information
additional information
-
inhibition kinetics, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
(1R,2R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-2,3a,11,11a-tetrahydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.0012
(1R,2R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)-2-(2-oxopropanoyl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.0005
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-13a-formyl-3a,11a-dihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-11-yl beta-D-glucopyranoside
Homo sapiens
-
pH 7.8, 37°C
0.0004
(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,15a-dimethyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.0005
(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9-(hydroxymethyl)-15a-methyl-1-(5-oxo-2,5-dihydrofuran-3-yl)icosahydro-7aH,13aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxine-13a-carbaldehyde
Homo sapiens
-
pH 7.8, 37°C
0.0007
1,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.003
2,3-dihydroxy-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.0007
2,8,9-trihydroxy-3-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.006
2,9-dihydroxy-3,8-dimethoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.003
3,8,9-trihydroxy-2-methoxy-6H-[1]benzofuro[3,2-c]chromen-6-one
Rattus norvegicus
-
37°C, pH 7.4
0.171
4,7-diacetoxy-14-hydroxydolast-1(15),8-diene
Cavia porcellus
-
enzym preparation from kidney
0.0007
4-[(1R,3aS,5aS,6aR,7aS,9R,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-13a-(hydroxymethyl)-9,15a-dimethylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
Homo sapiens
-
pH 7.8, 37°C
0.0004
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15aR)-3a,11,11a-trihydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
Homo sapiens
-
pH 7.8, 37°C
0.0003
4-[(1R,3aS,5aS,6aR,7aS,9S,11R,11aS,12aR,13aR,15R,15aS)-3a,11,11a,15-tetrahydroxy-9,13a-bis(hydroxymethyl)-15a-methylicosahydro-1H,7aH-cyclopenta[7,8]phenanthro[2,3-b]pyrano[3,2-e][1,4]dioxin-1-yl]furan-2(5H)-one
Homo sapiens
-
pH 7.8, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.133
-
enzyme activity in HK-2 cells in presence of fenoldopam, pH not specified in the publication, temperature not specified in the publication
0.183
-
enzyme activity in HK-2 cells, pH not specified in the publication, temperature not specified in the publication
0.25
-
enzyme activity in ouabain-pretreated HK-2 cells in presence of fenoldopam, pH not specified in the publication, temperature not specified in the publication
0.267
-
enzyme activity in ouabain-pretreated HK-2 cells, pH not specified in the publication, temperature not specified in the publication
32
65
additional information
-
decrease in specific activity by 78.5% in neonatal hypothyroidism
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7.5
7.8
7.4
-
myocytes in the experimental chamber for measurement of Na+-K+ pump current
7.4
-
myocytes in the experimental chamber for measurement of Na+-K+ pump current
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 7.8
-
variation of extracelluar pH for measurements of Na+-K+ pump activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
32
-
cells in temperature-controlled Lucite bath for patch-clamp experiments
35
37
additional information
37
-
myocytes in the experimental chamber for measurement of Na+-K+ pump current
37
-
myocytes in the experimental chamber for measurement of Na+-K+ pump current
additional information
comparison of temperature sensitivity of the endogenous pump current of Na+/K+-ATPase in Antarctic Pareledone sp. and temperate Octopus bimaculatus. The voltage dependence of the pumps is equivalent. At room temperature the maximum turnover rate of the Antarctic pump is 25% higher than that of the temperate pump. In addition, the Antarctic pump exhibits a lower temperature sensitivity, leading to significantly higher relative activity at lower temperatures
additional information
Pareledone sp.
comparison of temperature sensitivity of the endogenous pump current of Na+/K+-ATPase in Antarctic Pareledone sp. and temperate Octopus bimaculatus. The voltage dependence of the pumps is equivalent. At room temperature the maximum turnover rate of the Antarctic pump is 25% higher than that of the temperate pump. In addition, the Antarctic pump exhibits a lower temperature sensitivity, leading to significantly higher relative activity at lower temperatures
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
glioblastoma cells, A172 cells overexpress Na/K-ATPase alpha1 isoform in the caveolar structure
-
muscle cell line, A-769662 inhibits the Na+-K+-ATPase cell surface abundance in L6 cells by decreasing the phosphorylation of the alpha-subunit
-
enzyme activity is well-maintained in the dissociated neostriatal neurons
-
differential distribution of enzyme alpha subunit isoforms in subicular interneurones and pyramidal cells. While ATP1A3-isoforms regulate sodium and potassium homeostasis in subicular interneurones, ATPA1-isoforms assume this function in pyramidal cells
additional information
-
electrogenic Na+K+-ATPase partially contributes to the ustained hyperpolarization of endothelial cells in response to acetylcholine
-
little changes in enzyme alpha subunit isoform composition between summer and winter. Exposure to anoxia does not affect the activity of Na+K+-ATPase, but there is a 150fold extension in brain anoxia tolerance by seasonal changes in energy supply-demand ratio. Enzyme shows 10times lower catalytic activity in winter than in summer
-
-
-
rodent cancer cells lack discernable expression of the alpha3 subunit Na,K-ATPase isoform
-
acclimation to dilute seawater induces increased expression of Na+K+-ATPase and enzyme activity, with the increase being less in juveniles than in larger crabs. Juveniles maintain osmotic and ionic homeostasis by the expression and utilization of extremely high levels of gill Na+K+ATPase, in posterior, as well in anterior, gills
-
following acclimation in dilute seawater, specific activity of Na+K+-ATPase is progressively increased up to 3.9fold. Increased enzyme activity may be modulated by the changed proportion of fatty acids in the purified membranes of posterior gills. Long-term acclimation to dilute seawater results in increase in metallothionein content in posterior gill
-
neither osmotic pressure, Na+K+-ATPase activity, nor free amino acids are affected by diets rich/low in highly unsaturated fatty acids. Higher water content in gills of shrimp exposed to low salinty is counteracted by increased content in highly unsaturated fatty acids