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7.2.2.19: H+/K+-exchanging ATPase

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

Word Map on EC 7.2.2.19

Reaction

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

Synonyms

(H++K+)-ATPase, Atp12a, ATP1al1, ATP4A, ATP4B, EC 3.6.1.36, EC 3.6.3.10, electroneutral H+/K+-ATPase, gastric (H+, K+)-ATPase, gastric H+,K+-ATPase, gastric H+/K+-ATPase, gastric H+K+-ATPase, gastric H,K-ATPase, gastric H/K-ATPase, gastric HK-ATPase, gastric proton pump, H(+),K(+)-ATPase, H+, K+-ATPase, H+,K+ ATPase, H+,K+-adenosine triphosphatase, H+,K+-ATPase, H+-K+-adenosinetriphosphatase, H+-K+-ATPase, H+-K+-ATPase alpha2, H+/K+ ATPase, H+/K+ pump, H+/K+-ATPase, H+K+-ATPase, H,K-ATPase, H-K-ATPase, HKA, HKalpha1, HKalpha2, HKbeta, More, non-gastric H+/K+ ATPase, non-gastric H+/K+ATPase, non-gastric H,K-ATPase, nongastric H+-K+-ATPase, nongastric H,K-ATPase, nongastric H-K-ATPase, ouabain-sensitive H+/K+-ATPase, Proton pump

ECTree

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

Engineering

Engineering on EC 7.2.2.19 - H+/K+-exchanging ATPase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K791S
C10S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S/C152S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S/C152S/C162S/C178S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C131S/C152S/C162S/C178S/C201s/C263S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C152S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C162S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C162S/C178S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C178S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C201S/C263S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C210S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C21S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C263S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C58S
-
beta-subunit mutant, loss of H+,K+-ATPase activity, mutation does not permit delivery of the alpha-subunit to the cell surface
C813A
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
C813S
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
C813T
mutant enzyme shows 9fold loss of SCH28080 affinity
D824A
D824E
NH4+-independent H,K-ATPase activity is 2.8fold higher than the wild-type value
D824N
NH4+-independent H,K-ATPase activity is 46% of the wild-type value
E343A
complete loss of NH4+-stimulated H,K-ATPase activity, NH4+-independent H,K-ATPase activity is 80% of the wild-type value
E343D
complete loss of NH4+-stimulated H,K-ATPase activity, NH4+-independent H,K-ATPase activity is 39% of the wild-type value
E343Q
the apparent Km-value for NH4+ is increased about 4fold, the Ki value for SCH28080 is increased about 2fold, NH4+-independent H,K-ATPase activity is 83% of the wild-type value
E774A
IC50 for SCH28080 is 2.2fold higher than that of the wild-type enzyme
E774Q
IC50 for SCH28080 is nearly identical to that of the wild-type enzyme
E795D
the apparent Km-value for NH4+ is increased about 3fold, the Ki value for SCH28080 is increased about 11fold, NH4+-independent H,K-ATPase activity is 29% of the wild-type value
E795Q
the Ki value for SCH28080 is increased 1.3fold, NH4+-independent H,K-ATPase activity is 2.3fold higher than the wild-type value
E797Q
IC50 for SCH28080 is 4.3fold higher than that of the wild-type enzyme
E820A
complete loss of NH4+-stimulated H,K-ATPase activity
E820D
the Ki value for SCH28080 is increased 2.7fold, NH4+-independent H,K-ATPase activity is 1.5fold higher than the wild-type value
E914Q
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
E936D
the apparent Km-value for NH4+ is increased about 2fold. the Ki value for SCH28080 is increased 2.5fold, NH4+-independent H,K-ATPase activity is 1.7fold higher than the wild-type value
E936Q
NH4+-independent H,K-ATPase activity is 2.95fold higher than the wild-type value
E936V
complete loss of NH4+-stimulated H,K-ATPase activity
E938A
IC50 for SCH28080 is 8.2fold lower than that of the wild-type enzyme
E938Q
IC50 for SCH28080 is 1.6fold higher than that of the wild-type enzyme
F818C
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
F917Y
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
F932L
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
G918E
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
I803L
mutation has no effect on inhibitor kinetics of SCH28080
I814F
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
I814V
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
I816L
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
I819L
mutant enzyme shows mixed inhibition with SCH28080, no change in inhibitor affinity
I940A
mutation reduces affinity to the inhibitor SCH28080 by about 10fold and results in mixed inhibition
K791A
complete loss of NH4+-stimulated H,K-ATPase activity, NH4+-independent H,K-ATPase activity is 17% of the wild-type value
K791S
L809F
mutation results in a about 100fold decrease in affinity towards SCH28080
L809V
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
L811F
mutation reduces affinity to the inhibitor SCH28080 by about 10fold and results in mixed inhibition
L811V
mutation has no effect on inhibitor kinetics of SCH28080
M937V
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
P798C
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
P810A
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
P810G
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
Q905N
mutation has no effect on inhibitor kinetics of SCH28080
Q923V
mutant enzyme shows mixed inhibition with SCH28080, no change in inhibitor affinity
S806N
mutation has no effect on inhibitor kinetics of SCH28080
T823V
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
T825A
IC50 for SCH28080 is nearly identical to that of the wild-type enzyme
T825L
IC50 for SCH28080 is 4.5fold lower than that of the wild-type enzyme
T929L
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
V807I
mutation has no effect on inhibitor kinetics of SCH28080
Y799F
mutation has no effect on inhibitor kinetics of SCH28080
Y802F
mutation has no effect on inhibitor kinetics of SCH28080
Y802L
mutation reduces the affinity for SCH28080 up to 10fold without affecting the nature of the kinetics
Y922I
mutation reduces affinity to the inhibitor SCH28080 by about 10fold and results in mixed inhibition
Y925A
mutant enzyme shows mixed inhibition with SCH28080, no change in inhibitor affinity
Y925F
mutation reduces affinity towards the inhibitor SCH28080 by about 10fold, resulting in noncompetitive kinetics
Y928H
mutation has no effect on inhibitor kinetics of SCH28080
A778P/C781T
-
expression level rather similar to that of the recombinant enzyme, ability of binding 3(H)ouabain with high affinity
A778P/C781T/Y786F/V788I/G790N/L791I/I795L/I798V/F802C
-
expression level and 3(H)ouabain binding level rather similar to that of the recombinant enzyme
D312E/S319G/A778P/I795L/F802C
-
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
E820Q
I795L/I798V/F802C
-
expression level rather similar to that of the recombinant enzyme, ability of binding 3(H)ouabain with high affinity
K791A
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
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
K791S
N103Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N130Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N146Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N161Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N193Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N225Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
N99Q
-
site-directed mutagenesis, the mutation of the glycosylation site does not alter the enzyme's properties compared to the wild-type enzyme
S806C
Y309T/V310W/D312E/I314V/S319G
-
expression level rather similar to that of the recombinant enzyme, ability of binding 3(H)ouabain with high affinity
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
-
expression level rather similar, but 3(H)ouabain binding level significantly higher than that of the recombinant enzyme
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/C802F
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/E312D
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/G319S
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/L795I
-
3(H)ouabain binding level significantly lower than that of mutant Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C
Y309T/V310W/D312E/I314V/S319G/A778P/C781T/I795L/I798V/F802C/P778A
-
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)
additional information