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7.2.2.13: Na+/K+-exchanging ATPase

This is an abbreviated version!
For detailed information about Na+/K+-exchanging ATPase, go to the full flat file.

Word Map on EC 7.2.2.13

Reaction

ATP
+
H2O
 +
Na+[side 1]
 +
K+[side 2]
=
ADP
 +
phosphate
 +
Na+[side 2]
 +
K+[side 1]

Synonyms

(Na+ + K+)-activated ATPase, (Na+ + K+)-ATPase, (Na+, K+)-ATPase, (Na+, K+)-dependent ATPase, (Na+,K+)-activated ATPase, (Na+-K+)-ATPase, alpha2Na+/K+-ATPase, ATP1a1, atp1a1a, ATPalpha, EC 3.6.1.3, EC 3.6.1.37, EC 3.6.3.9, Na pump, Na(+)-K(+)-exchanging ATPase, Na+ pump, Na+, K+ -ATPase, Na+, K+-ATPase, Na+,K+ pump, Na+,K+-adenosine triphosphatase, Na+,K+-ATPase, Na+,K+-pump, Na+-K+ ATPase, Na+-K+ pump, Na+-K+ pump alpha1-isoform, Na+-K+ pump alpha2-isoform, Na+-K+-ATPase, Na+-K+-ATPase alpha2-isoform, Na+-K+-pump, Na+/K+ -ATPase, Na+/K+ ATPase, Na+/K+ pump, Na+/K+-ATPase, Na+K+-ATPase, Na+K+ATPase, Na, K-ATPase, Na,K pump, Na,K-activated ATPase, Na,K-adenosine triphosphatase, Na,K-ATPase, Na,K-Pump, Na-K-ATPase, Na/K pump, Na/K-ATPase, NKA, Nkaalpha protein, nkaalpha1, nkaalpha3a, nkaalpha3b, renal sodium-potassium pump, SNaK1, sodium potassium adenosinetriphosphatase, sodium pump, sodium-potassium pump, sodium/potassium ATPase

ECTree

     7 Translocases
         7.2 Catalysing the translocation of inorganic cations
             7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
                7.2.2.13 Na+/K+-exchanging ATPase

Engineering

Engineering on EC 7.2.2.13 - Na+/K+-exchanging ATPase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D409E
-
phosphorylation site of alpha-subunit, inactive pump
R669Q
-
ATP binding site of alpha-subunit, inactive pump
F785L
-
mutation associated with familial rapid-onset dystonia parkinsonism, leads to functionally altered, but active, Na+K+-pumps with reduced apparent affinity for cytoplasmic Na+. Defect in the interaction of the E1 form of enzyme with Na+, and the E1-E2 equilibrium is not displaced. K+ interaction at the external activating sites of E2P phosphoenzyme is normal. The affinity for ouabain is significantly reduced
F785L/L786F
-
aromatic function of F785 is critical for Na+ and ouabain binding
F785Y
-
aromatic function of F785 is critical for Na+ and ouabain binding
T618M
-
mutation associated with familial rapid-onset dystonia parkinsonism, leads to functionally altered, but active, Na+K+-pumps with reduced apparent affinity for cytoplasmic Na+. The Na+-affinity is reduced because of displacement of the conformational equilibrium in favor of the K+-occluded E2 form. K+ interaction at the external activating sites of E2P phosphoenzyme is normal
C911S/C964A/Q111R/N122D
-
alpha-subunit: mutant without extracellularly exposed cysteine residues (911, 964) and with reduced ouabain sensitivity (111, 122)
C911S/C964S/Q111R/N122D
-
alpha1-subunit mutant without extracellularly exposed cysteine residues (911, 964), and with reduced ouabain sensitivity (111, 122)
D714A
-
insensitive to palytoxin
D714E
-
the IC50 of the palytoxin-induced K+ efflux is 4fold higher than in cells expressing the wild-type enzyme
D714R
-
insensitive to palytoxin
E779A
-
15fold increase in K+ concentration that half-maximally activates Na,K-pump current at 0 mV in extracellular Na+-free solutions
G848F
-
alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
G848W
-
alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
K691A
-
insensitive to palytoxin
K691D
-
insensitive to palytoxin
K691R
-
the EC50 of the palytoxin-induced K+ efflux is 7fold higher than in cells expressing the wild-type enzyme
N122D
-
membrane potential and K+ dependence similar to wild-type Na,K-ATPase
Q111R
-
membrane potential and K+ dependence similar to wild-type Na,K-ATPase
Q849G
-
alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
Q849H
-
alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
Q849W
-
alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
S62C/N158Q/N193Q/N265Q
-
beta-subunit: mutation for site-directed fluorescence labeling without impairing enzyme function (62) and mutations in all N-glycosylation sites of the beta1-ectodomain (158, 193, 265)
S62C/Y39F/Y43F
-
beta1-subunit mutant with Cys for site-directed fluorescence labeling (62), and with a shift of the conformational equilibrium (39,43)
S62C/Y39S/Y43S
-
beta1-subunit mutant with Cys for site-directed fluorescence labeling (62), and with a shift of the conformational equilibrium (39,43)
S62C/Y39W/Y43W
-
beta1-subunit mutant with Cys for site-directed fluorescence labeling (62), and with changed apparent rate constant for reverse binding of extracellular Na+ (39, 43)
S775A
-
155fold increase in K+ concentration that half-maximally activates Na,K-pump current at 0 mV in extracellular Na+-free solutions
Y847W
-
alpha1-subunit, located in transmembrane domain 7 (alpha/beta interface)
D928A
-
the mutant exhibits a modest reduction of the apparent Na+ affinity to 5fold relative to the wild type enzyme
D928E
-
the mutant exhibits a modest reduction of the apparent Na+ affinity to 4fold relative to the wild type enzyme
D928H
-
the mutant exhibits a modest reduction of the apparent Na+ affinity to 7fold relative to the wild type enzyme
D928L
-
the mutant exhibits a modest reduction of the apparent Na+ affinity to 10fold relative to the wild type enzyme
D928N
-
the mutant exhibits a dramatic reduction of the apparent Na+ affinity to 78fold and slight 1.5fold increase of apparent K+ affinity relative to the wild type enzyme
E314D
-
the mutant exhibits an 3.2fold increase of the apparent Na+ affinity and 1.7fold increase of apparent K+ affinity relative to the wild type enzyme
E314D/D928A
-
the mutant exhibits an 1.2fold increase of the apparent Na+ affinity and slight 1.7fold decrease of apparent K+ affinity relative to the wild type enzyme
E314D/D928N
-
the mutant exhibits a modest 8.1fold decrease of the apparent Na+ affinity and slight 1.5fold increase of apparent K+ affinity relative to the wild type enzyme
A330C
A338C
C111S
E334C
F323C
G326C
G335C
G803C
-
the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
I322C
I325C
I327C
I328C
L324C
L336C
L337C
-
K+ induced current, I_K in nA, lower (negative) than control - ouabain-sensitive current, I_ouab in nA, lower (negative) than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
L344C
L802C
-
the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
N331C
P333C
P801C
-
the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
T339C
-
K+ induced current, I_K in nA, lower than control - ouabain-sensitive current, I_ouab in nA, lower than control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower control
T341C
-
K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, similar to control - membrane conductance induced by palytoxin, G_PTX in mikroS, lower than control
T804C
-
the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
V321C
V329C
V332C
V340C
V342C
-
K+ induced current, I_K in nA, higher than control - ouabain-sensitive current, I_ouab in nA, higher than control - membrane conductance induced by palytoxin, G_PTX in mikroS, higher than control
V805C
-
the effect of cysteine mutations on the K+ activated and ouabain-sensitive currents, the effect of acid pH and omeprazole, the effect of MTSET on Na+, K+-ATPase cysteine mutants and the effect of MTSET on the voltage-dependent kinetics of activation by extracellular K+ is measured.
D813C
-
decrease in cation/anion selectivity, which is grossly impaired after treatment with 2-trimethylammonium-ethyl-methanethiosulphonate
D817C
-
highly cation-selective pump-channel, no response to modification by 2-trimethylammonium-ethyl-methanethiosulphonate
E321C
-
reaction with 2-trimethylammonium-ethyl-methanethiosulphonate does not decrease cation current
E336C
-
decrease in cation/anion selectivity, which is transformed from cation-selective to anoin-selective after treatment with 2-trimethylammonium-ethyl-methanethiosulphonate
E788C
-
highly cation-selective pump-channel, no response to modification by 2-trimethylammonium-ethyl-methanethiosulphonate
G805C
-
reaction with 2-trimethylammonium-ethyl-methanethiosulphonate or with 2-aminocarbonyl-ethyl-methanethiosulphonate does not decrease cation current
N785C
-
highly cation-selective pump-channel, no response to modification by 2-trimethylammonium-ethyl-methanethiosulphonate
T806C
-
cation current is diminished after reaction with 2-trimethylammonium-ethyl-methanethiosulphonat and 7fold decreased after reaction with 2-aminocarbonyl-ethyl-methanethiosulphonate
additional information