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ATP phosphohydrolase
-
-
-
-
auto-inhibited H+-ATPase isoform 2
-
EC 3.6.3.6
-
-
formerly
-
HA5
-
isoform of non-penultimate threonine-containing H+-ATPase
HA6
isoform of non-penultimate threonine-containing H+-ATPase
HA7
isoform of non-penultimate threonine-containing H+-ATPase
non-penultimate threonine-containing H+-ATPase
non-pT H+-ATPase
penultimate threonine-containing H+-ATPase
pT H+-ATPase
plasma membrane H*-ATPase pump
plasma membrane H+-ATPase
plasma membrane H+-ATPase isoform 2
-
-
plasma membrane H+-ATPase LHA1
-
plasma membrane H+-ATPase LHA2
-
plasma membrane H+-ATPase LHA3
-
plasma membrane P-type H+-ATPase
plasma membrane proton pump
-
plasma membrane V-ATPase
-
-
plasma membrane vacuolar H+-ATPase
-
-
proton-translocating ATPase
-
-
-
-
tonoplast P-ATPase transporter
vacuolar proton-translocating ATPase
vacuolar-type H+-ATPase
-
vacuolar-type H+-translocating ATPase
yeast plasma membrane ATPase
-
-
-
-
yeast plasma membrane H+-ATPase
-
-
-
-
AHA1
-
isoform
AHA2
-
-
EC 3.6.1.35
-
-
formerly
-
H+ ATPase 2
-
-
H+-ATPase
-
-
-
-
HA1
-
HA1
-
isoform of penultimate threonine-containing H+-ATPase
HA2
-
HA2
isoform of penultimate threonine-containing H+-ATPase
HA3
-
HA3
isoform of penultimate threonine-containing H+-ATPase
HA4
-
isoform
HA4
isoform of penultimate threonine-containing H+-ATPase
HA8
-
isoform
HA8
isoform of non-penultimate threonine-containing H+-ATPase
P-type ATPase
-
-
PH5
-
-
plasma membrane ATPase
-
-
plasma membrane ATPase
-
-
plasma membrane ATPase
-
-
plasma membrane H*-ATPase pump
-
-
plasma membrane H*-ATPase pump
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
plasma membrane H+-ATPase
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
plasma membrane H+-ATPase
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane P-type H+-ATPase
-
plasma membrane P-type H+-ATPase
-
-
plasma membrane P-type H+-ATPase
-
-
plasma membrane P-type H+-ATPase
-
-
-
PM H+-ATPase
-
-
PMA1
-
Pma1p
-
-
PMA2
-
-
tonoplast P-ATPase transporter
-
-
tonoplast P-ATPase transporter
-
-
V-ATPase
-
vacuolar ATPase
-
-
vacuolar H+-ATPase
-
-
vacuolar proton pump
-
-
vacuolar proton-translocating ATPase
-
-
vacuolar proton-translocating ATPase
-
-
-
vacuolar proton-translocating ATPase
-
-
-
vacuolar-type ATPase
-
vacuolar-type H+-translocating ATPase
-
-
vacuolar-type H+-translocating ATPase
-
-
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ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
ATP + H2O + H+/in
ADP + phosphate + H+/out
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
dATP + H2O + H+/in
dADP + phosphate + H+/out
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
-
6.5% of the activity with ATP
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
-
9.5% of the activity with ATP
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
-
9.5% of the activity with ATP
-
-
?
additional information
?
-
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
ATP in form of MgATP2-
-
-
?
ATP + H2O + 4 H+[side 1]
ADP + phosphate + 4 H+[side 2]
-
ATP in form of MgATP2-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
high substrate specificity for ATP
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
reaction is slightly cooperative, Hill number 1.5, S0.5 value 0.8 mM ATP. Kd value of ATP 0.7 mM
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
mechanism involves a covalent phosphoryl-enzyme intermediate
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
high substrate specificity for ATP
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
the PMA1 gene encoding plasma membrane ATPase is essential because a null mutation is lethal in haploid cells. The proton gradient generated by the enzyme drives the active transport of nutrients by H+-symport. In addition, the external acidification in plants and the internal alkalinization in fungi both resulting from activation of the H+ pump, have been proposed to mediate growth responses
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
high substrate specificity for ATP
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
specific for ATP
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
activity is independent of growth phase
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
additional information
?
-
-
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
?
additional information
?
-
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
?
additional information
?
-
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
?
additional information
?
-
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
?
additional information
?
-
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
?
additional information
?
-
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
?
additional information
?
-
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
?
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2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
-
an ebselen analogue
2-methylbenzisoselenazol-3(2H)-one
-
-
2-n-propylbenzisoselenazol-3(2H)-one
-
-
2-phenyl-1,2-benzisoselenazol-3(2H)-one
2-phenyl-1,2-benzisoselenazol-3(2H)-one 1-oxide
-
an ebselen analogue
2-phenyl-7-azabenzisoselenazol-3(2H)-one
-
-
2-phenylbenzisothiazol-3(2H)-one
-
-
adenosine 5'-(beta,gamma-imido)-triphosphate
-
5 mM, 60% inhibition
adenosine 5'-monophosphate
decreases the interaction between the phosphorylated Vha2 and the 14-3-3 protein, followed by a reduction of the H+-ATPase activity and citrate exudation under Al stress conditions
ADP
-
5 mM, 60% inhibition, Kd value 0.8 mM
aluminium
-
the activity of plasma membrane H+-ATPase is affected by aluminium at the transcription, translation, and post-translation levels
ATP
-
competitive inhibitor, the enzyme activity decreases in the presence of Mg2+-free ATP. ATP inhibition also occurs at pH 7.5. Upon increasing Mg2+ concentration from 5 mM to 15 mM, the decrease in ATPase activity at high ATP concentration is prevented
benzisoselenazol-3(2H)-one
-
-
Cd2+
-
complete loss of ATP hydrolysis and proton transport. Exposure does not enhance the lipid peroxidation in plasma membrane, but causes an increase in the saturation of plasma membrane fatty acids and a decrease of the fatty acid chain length
destruxin B
-
specific and reversible inhibition, complete inhibition at concentrations above 0.02 mM
ebselen
-
i.e. 2-phenylbenzisoselenazol-3(2H)-one
fluoroaluminates
-
Mg2+ is an essential cofactor for inhibition, biphasic inhibitory process at pH 7.5 with a preference for AlF4- species
-
Hemileia vastatrix
-
treatment with soluble fraction of urediospores induces specific inhibition of of the resistant variety's Colombia H+-ATPase and proton pump activities, while the inhibition of the Caturra variety's proton-pump acitivy is only 16.5%
-
iejimalide A
-
a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
iejimalide B
-
a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
K+
-
K+ is an intrinsic uncoupler of the proton pump. Binding of K+ to the cytoplasmic phosphorylation domain can induce dephosphorylation of the phosphorylated E1P reaction cycle intermediate by a mechanism involving residue E184 in the conserved TGEs motif
K2SO4
-
in plants grown with 10 mM K2SO4 plus 100 mM NaCl supply, activity decreases competitively with Na+, after 21 d of salinity, with different effects on Km and Vmax
N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline
-
no protection by MgADP-, protection by MgATP2- or Mg-vanadate
NEM
-
pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
Phenylglyoxal
-
pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
SidK
-
a protein of Legionella pneumophila, an intracellular pathogen, specifically targets host v-ATPase. SidK interacts via an N-terminal portion with VatA, a key component of the proton pump leading to the inhibition of ATP hydrolysis and proton translocation. SidK inhibits vacuole acidification and impairs the ability of the cells to digest non-pathogenic Escherichia coli
-
Trypsin
-
85% inhibition of the enzyme in plasma membrane vesicles in absence of MgATP2-, no inhibition in presence of MgATP2-
-
Zn2+
-
short-term (10 min) exposure to zinc (0.25 mM) completely inhibits the activity of the enzyme
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
i.e. ebselen, inhibition of enzyme results in inhibition of medium acidification. Fungicidal effect is at least in part due to interference with both the proton-translocating function and the ATPase activity of plasma membrane H+-ATPase
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
i.e. ebselen, a synthetic selenium-containing compound with antimicrobial activity. It acts fungicidally against Candida albicans at 0.030 mM, effect of ebselen on the growth of the strain, overview
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
i.e. ebselen, inhibition of enzyme results in inhibition of medium acidification. Fungicidal effect is at least in part due to interference with both the proton-translocating function and the ATPase activity of plasma membrane H+-ATPase
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
i.e. ebselen, inhibition of enzyme results in inhibition of medium acidification. Fungicidal effect is at least in part due to interference with both the proton-translocating function and the ATPase activity of plasma membrane H+-ATPase
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
i.e. ebselen
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
i.e. ebselen, a synthetic selenium-containing compound with antimicrobial activity, effect of ebselen on the growth of the strain, overview; i.e. ebselen, a synthetic selenium-containing compound with antimicrobial activity, effect of ebselen on the growth of the strain, overview. The antifungal action of ebselen is related, at least in part, to its ability to interact with L-cysteine, high affinity of selenium for sulfhydryl groups
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
i.e. ebselen, inhibition of enzyme results in inhibition of medium acidification. Fungicidal effect is at least in part due to interference with both the proton-translocating function and the ATPase activity of plasma membrane H+-ATPase
Al3+
-
the proton transport activity of the enzyme is inhibited by 50% in the presence of 100 mM Al3+ at pH 6.5 and 10% at pH 7.5
Al3+
-
inhibition of H+-ATPase activity, Mg2+ partly prevents
bafilomycin A1
-
-
Ca2+
-
extracellular, inhibits the enzym ein osteoclast membranes, Ca2+ behaves as a negative feedback signal for osteoclast function
Ca2+
-
completely inactive when Mg2+ is substituted by Ca2+, strongly inhibited by Ca2+ in presence of Mg2+
Cu2+
-
short-term (10 min) exposure to copper (0.05 mM) completely inhibits the activity of the enzyme
Cu2+
-
complete loss of ATP hydrolysis and proton transport. Exposure does not enhance the lipid peroxidation in plasma membrane, but causes an increase in the saturation of plasma membrane fatty acids and a decrease of the fatty acid chain length
Cu2+
-
short-term (10 min) exposure to copper (0.05 mM) completely inhibits the activity of the enzyme
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
no protection by MgATP2-
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
-
Dio-9
-
-
-
distilbestrol
-
-
K-252a
-
a potent inhibitor of protein kinase
K-252a
-
a potent inhibitor of protein kinase
miconazole
-
-
molybdate
-
86% residual activity at 1 mM
molybdate
-
87% residual activity at 1 mM
N-ethylmaleimide
-
2 mM, 26% inhibition
NaF
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
sodium orthovanadate
-
-
sodium orthovanadate
-
specific inhibitor
Triton X-100
-
strong inhibition
Triton X-100
-
strong inhibition
vanadate
-
-
vanadate
-
Na3VO4, non-competitive
vanadate
-
about 7% residual activity at 0.3 mM
vanadate
-
8% residual activity at 0.1 mM
vanadate
-
inhibition of enzyme, treatment additionally leads to severe suppression of phosphorus uptake by roots in low-phosphorus nutrient solution
vanadate
significant inhibition at 0.1 mM; significant inhibition at 0.1 mM; significant inhibition at 0.1 mM
vanadate
-
8% residual activity at 0.1 mM
vanadate
-
for enzymes isolated from root, kinetic models of vanadate inhibition indicate simultaneous binding of Mg-ATP and vanadate to the same enzyme state. For shoot enzymes, application of the competitive inhibitor Mg-free ATP attenuates vanadate inhibition, consistent with a model in which either Mg-free ATP or Mg-ATP is bound to the enzyme when vanadate binds
additional information
-
proton pump interactor (PPI1) is unable to suppress the auto-inhibitory action of the enzyme C-terminus, but further enhances the activity of the enzyme whose C-terminus has been displaced by low pH or by fusicoccin-induced binding of 14-3-3 proteins
-
additional information
-
not inhibited by nitrate, azide, and molybdate
-
additional information
-
not inhibited by azide and nitrate
-
additional information
-
ebselen is at least 10fold more potent as antifungal compound compared the azoles fluconazole, itraconazole, and ketoconatzole, and as amphotericin B
-
additional information
-
not inhibitory: Ni2+
-
additional information
-
both inhibitors, iejimalides A and B, sequentially neutralize the pH of lysosomes, induce S-phase cell-cycle arrest, and trigger apoptosis in MCF-7 cells, overview
-
additional information
-
not inhibitory: SCH28080
-
additional information
-
inhibitor screening, overview
-
additional information
phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity
-
additional information
phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity
-
additional information
phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity
-
additional information
-
not inhibited by azide and nitrate
-
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14-3-3 protein
-
the activated enzyme consists of 6 phosphorylated molecules, assembled in a hexameric structure, together with six 14-3-3 molecules
-
AlK(SO4)2
-
treatment of cells results in increase in vandate-sensitive H+-transport and in enzymatic activity, whereas yeast-hypha transition is inhibited
ATP
-
exogenously applied ATP induces increased enzyme activity in tea roots at both pH 4.0 and 5.0
auxin
-
auxin regulates enzyme activity by phosphorylation
coumarin
-
when coumarin and NO3- are concurrently added to the nutrient solution, a significant increase in the PM H+-ATPase activity is observed. However, coumarin does not affect enzyme activity by direct contact
Cu2+
-
at longer exposure times (8 days) of Cu2+, the enzyme exhibits 2.3fold increased activity
D-glucose
-
activates, brings about a global conformational change in H+-ATPase
dithiothreitol
-
2 mM, 26% stimulation
iodoacetic acid
-
in roots in low-phosphorus nutrient solution, iodoacetic acid stimulates the activity of plasma membrane H+-ATPase and phosphorus uptake. The effect is blocked by naphthylphthalamic acid
lysophosphatidylcholine
-
stimulates
NO3-
-
exposure to 0.2 mM NO3- brings about an increase in ATP hydrolytic activity after 8 h (31%) and 24 h (33%) compared to the control
proton pump interactor
-
proton pump interactor, isoform 1 (PPI1) is unable to suppress the auto-inhibitory action of the enzyme C-terminus, but further enhances the activity of the enzyme whose C-terminus has been displaced by low pH or by fusicoccin-induced binding of 14-3-3 proteins
-
fusicoccin
-
activation of enzyme, treatment additionally leads to 35% increase in phosphorus uptake by roots in low-phosphorus nutrient solution
fusicoccin
increases the interaction between the phosphorylated Vha2 and the 14-3-3 protein, followed by an enhancement of the H+-ATPase activity and citrate exudation under Al stress conditions
indole-3-acetic acid
-
-
Mg-ATP
-
activation of H+-ATPase occurs by the addition of 5 mM Mg-ATP
Mg-ATP
-
activation of H+-ATPase occurs by the addition of 5 mM Mg-ATP
NaCl
-
50 mm, 132% of initial activity, 150 mM, 156% of initial activity
NaCl
-
treatment with 200 mM NaCl increases shoot V-ATPase hydrolysis activity by 1.65fold while 1.39fold in roots
NH4+
-
small activation
NH4+
-
markedly increases activity
Phospholipid
-
activated by exogenous phospholipids
Phospholipid
-
requires added phospholid for maximal activity
Phospholipid
-
requires added phospholid for maximal activity
Phospholipid
-
activated 3fold to 6fold by soybean phospholipids
Phospholipid
-
requires added phospholid for maximal activity
spermine
-
a concentration of 1 mM is the most effective
spermine
-
about 2fold stimulation due to an increase in regulatory protein 14-3-3 levels associated with the enzyme. Stimulation has an S50 value of 0.07 mM, and spermine induces 14-3-3 protein association with the unphosphorylated C-terminal domain of the enzyme. The effect is stronger and additive to that of Mg2+
additional information
-
the plasma membrane H + -ATPase is activated via phosphorylation of the penultimate threonine in the C-terminus leading to subsequent binding of a 14-3-3 protein
-
additional information
-
activity and translation of the plasma membrane H+-ATPase, as well as 14-3-3 proteins, increases after 3 days of cold stress. The increase in H+-ATPase activity during recovery for 2 h at 25°C is less pronounced, followed by decay to background levels within 24 h. H+-pumping increases after 15 min recovery. An increase in phosphorylation levels parallels the increase in H+-transport rate
-
additional information
-
activity and translation of the plasma membrane H+-ATPase, as well as 14-3-3 proteins, increases after 3 days of cold stress. The increase in H+-ATPase activity is most dramatic in Camelina roots after recovery for 2 h at 25°C, followed by decay to background levels within 24 h. H+-pumping increases after 15 min recovery. An increase in phosphorylation levels parallels the increase in H+-transport rate
-
additional information
-
neither octyl glucoside, 7-cyclohexyl-1-heptyl-beta-D-maltoside nor n-dodecyl-N,N-dimethylamine-N-oxide activate isoform Pma1p
-
additional information
-
the plasma membrane H + -ATPase is activated via phosphorylation of the penultimate threonine in the C-terminus leading to subsequent binding of a 14-3-3 protein
-
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Acidosis
Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing.
Acidosis, Renal Tubular
Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing.
Adenocarcinoma
Genomic organization of the gene coding for TIRC7, a novel membrane protein essential for T cell activation.
Alkalosis
Recovery from blood alkalosis in the Pacific hagfish (Eptatretus stoutii): involvement of gill V-H+-ATPase and Na+/K+-ATPase.
Bone Resorption
Osteoclastic bone resorption by a polarized vacuolar proton pump.
Bone Resorption
SB 242784, a selective inhibitor of the osteoclastic V-H+ATPase, inhibits arterial calcification in the rat.
Breast Neoplasms
Lactoferrin selectively triggers apoptosis in highly metastatic breast cancer cells through inhibition of plasmalemmal V-H+-ATPase.
Breast Neoplasms
VD3 mitigates breast cancer aggressiveness by targeting V-H+-ATPase.
Carcinoma, Hepatocellular
A high-affinity (Ca2+ + Mg2+)-ATPase in plasma membranes of rat ascites hepatoma AH109A cells.
Carcinoma, Hepatocellular
Isolation and characterization of the plasma membranes from rat ascites hepatomas and from normal rat livers, including newborn, regenerating, and adult livers.
Cardiomegaly
Identification of a receptor for extracellular renalase.
Congenital Abnormalities
Bone marrow-derived osteoclast-like cells from a patient with craniometaphyseal dysplasia lack expression of osteoclast-reactive vacuolar proton pump.
Cystic Fibrosis
Calcium and sodium transport processes in patients with cystic fibrosis. I. A specific decrease in Mg2+-dependent, Ca2+-adenosine triphosphatase activity in erythrocyte membranes from cystic fibrosis patients.
Cystic Fibrosis
Calcium-ATPase activity in cystic fibrosis erythrocyte membranes: decreased activity in patients with pancreatic insufficiency.
Dehydration
Comparative effects of allelochemical and water stress in roots of Lycopersicon esculentum Mill. (Solanaceae).
Exocrine Pancreatic Insufficiency
Calcium-ATPase activity in cystic fibrosis erythrocyte membranes: decreased activity in patients with pancreatic insufficiency.
Hepatitis C
Crystal structure of the TLDc domain of human NCOA7-AS.
Hyperostosis
Bone marrow-derived osteoclast-like cells from a patient with craniometaphyseal dysplasia lack expression of osteoclast-reactive vacuolar proton pump.
Hypocalcemia
Impaired gastric acidification negatively affects calcium homeostasis and bone mass.
Infections
Crystal structure of the TLDc domain of human NCOA7-AS.
Infections
Differential regulation of gene expression in the obligate biotrophic interaction of Uromyces fabae with its host Vicia faba.
Infections
Mitochondrial ATP-ASE as a measure of uncoupling of rat muscle mitochondria in experimental infection with Trichinella spiralis and Trichinella pseudospiralis.
Influenza, Human
Crystal structure of the TLDc domain of human NCOA7-AS.
Lung Neoplasms
[Ca2+, Mg2+-ATPase activity of the erythrocyte membrane in patients with lung cancer]
Malnutrition
Effect of exercise during rehabilitation on swimming performance, metabolism and function of muscle in rats.
Mastocytoma
Synthesis and activation of mitotic Ca2+-adenosinetriphosphatase during the cell cycle of mouse mastocytoma cells.
Neoplasm Metastasis
VD3 mitigates breast cancer aggressiveness by targeting V-H+-ATPase.
Neoplasms
Antiproliferative activity of mammalian lignan derivatives against the human breast carcinoma cell line, ZR-75-1.
Neoplasms
Co-administration of probenecid, an inhibitor of a cMOAT/MRP-like plasma membrane ATPase, greatly enhanced the efficacy of a new 10-deazaaminopterin against human solid tumors in vivo.
Neoplasms
Evidence for high activity of xylem parenchyma and ray cells in the interface of host stem and Agrobacterium tumefaciens-induced tumours of Ricinus communis.
Neoplasms
Genomic organization of the gene coding for TIRC7, a novel membrane protein essential for T cell activation.
Neoplasms
Lactoferrin selectively triggers apoptosis in highly metastatic breast cancer cells through inhibition of plasmalemmal V-H+-ATPase.
Neoplasms
P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer.
Neoplasms
VD3 mitigates breast cancer aggressiveness by targeting V-H+-ATPase.
Osteopetrosis
A phenocopy of CAII deficiency: a novel genetic explanation for inherited infantile osteopetrosis with distal renal tubular acidosis.
Osteopetrosis
Association between a polymorphism affecting an AP1 binding site in the promoter of the TCIRG1 gene and bone mass in women.
Osteopetrosis
Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis.
Osteopetrosis
Human osteopetroses and the osteoclast V-H+-ATPase enzyme system.
Osteopetrosis
Human osteopetrosis and other sclerosing disorders: recent genetic developments.
Osteopetrosis
Novel mutations in the TCIRG1 gene encoding the a3 subunit of the vacuolar proton pump in patients affected by infantile malignant osteopetrosis.
Osteopetrosis
Osteopetrosis and Glanzmann's thrombasthenia in a child.
Osteopetrosis
Sibling pair linkage and association studies between peak bone mineral density and the gene locus for the osteoclast-specific subunit (OC116) of the vacuolar proton pump on chromosome 11p12-13.
Osteoporosis
Novel bone antiresorptive agents that selectively inhibit the osteoclast V-H+-ATPase.
Prostatic Neoplasms
Resveratrol derivatives increase cytosolic calcium by inhibiting plasma membrane ATPase and inducing calcium release from the endoplasmic reticulum in prostate cancer cells.
Sarcoma, Yoshida
Inactivation of (Na-++K-+)-stimulated ATPase by a cytotoxic protein from cobra venom in relation to its lytic effects on cells.
Starvation
In vivo activation of the yeast plasma membrane ATPase during nitrogen starvation. Identification of the regulatory domain that controls activation.
Starvation
In vivo activation of yeast plasma membrane H+-ATPase by ethanol: effect on the kinetic parameters and involvement of the carboxyl-terminus regulatory domain.
Starvation
Metabolic responses in cucumber (Cucumis sativus L.) roots under Fe-deficiency: a 31P-nuclear magnetic resonance in-vivo study.
Starvation
Root plasma membrane H+-ATPase is involved in the adaptation of soybean to phosphorus starvation.
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0.161
ATP
-
enzyme in vesicles from pH 7.0-grown cells, pH and temperature not specified in the publication
0.17
ATP
-
glucose-metabolizing cells
0.184
ATP
-
enzyme in vesicles from pH 5.0-grown cells, pH and temperature not specified in the publication
0.4
ATP
mutant M795A, pH 5.7, 30°C
0.434
ATP
-
wild-type, pH 6.5
0.5
ATP
-
mutant D720C, 30°C, pH 5.7
0.5
ATP
-
mutant S716A, 30°C, pH 5.7
0.6
ATP
-
mutant N715A, 30°C, pH 5.7
0.6
ATP
-
activated enzyme state from plasma membrane, at pH 5.9 and 30°C
0.636
ATP
-
wild-type lacking C-terminal 40 amino acids, pH 6.5
0.7
ATP
mutant E803A, pH 5.7, 30°C
0.7
ATP
mutant L797A, pH 5.7, 30°C
0.7
ATP
-
mutant enzyme E803A, at pH 5.7 and 30°C
0.7
ATP
-
mutant enzyme L797A, at pH 5.7 and 30°C
0.7
ATP
-
mutant D720A, 30°C, pH 5.7
0.7
ATP
-
mutant D720A, pH 5.7, 30°C
0.7
ATP
-
mutant D720E, 30°C, pH 5.7
0.7
ATP
-
mutant D720E, pH 5.7, 30°C
0.8
ATP
mutant F808A, pH 5.7, 30°C
0.8
ATP
mutant G793E, pH 5.7, 30°C
0.9
ATP
mutant R811A, pH 5.7, 30°C
0.9
ATP
mutant W805A, pH 5.7, 30°C
0.9
ATP
-
mutant D714N, 30°C, pH 5.7
0.9
ATP
-
mutant D714N, pH 5.7, 30°C
0.9
ATP
-
mutant D720N, 30°C, pH 5.7
0.9
ATP
-
mutant D720N, pH 5.7, 30°C
1
ATP
-
wild type enzyme and histidine-tagged enzyme
1
ATP
-
mutant D720V, pH 5.7, 30°C
1
ATP
-
mutant I719A, 30°C, pH 5.7
1
ATP
-
mutant S716C, 30°C, pH 5.7
1.1
ATP
mutant G793A, pH 5.7, 30°C
1.1
ATP
mutant N792A, pH 5.7, 30°C
1.1
ATP
mutant N792H, pH 5.7, 30°C
1.1
ATP
mutant Q798E, pH 5.7, 30°C
1.1
ATP
mutant T802A, pH 5.7, 30°C
1.1
ATP
mutant T810A, pH 5.7, 30°C
1.1
ATP
-
mutant D718A, 30°C, pH 5.7
1.2
ATP
mutant N792Q, pH 5.7, 30°C
1.2
ATP
-
mutant I719C, 30°C, pH 5.7
1.24
ATP
-
pH 6.5, 37°C, Colombia variety
1.26
ATP
-
pH 6.5, 37°C, Caturra variety
1.3
ATP
mutant M791A, pH 5.7, 30°C
1.3
ATP
mutant N792D, pH 5.7, 30°C
1.3
ATP
-
wild-type, pH 5.7, 30°C
1.3
ATP
-
wild-type, 30°C, pH 5.7
1.4
ATP
mutant S800A, pH 5.7, 30°C
1.4
ATP
wild-type, pH 5.7, 30°C
1.4
ATP
-
wild type enzyme, at pH 5.7 and 30°C
1.5
ATP
mutant I809A, pH 5.7, 30°C
1.6
ATP
mutant N804A, pH 5.7, 30°C
1.6
ATP
-
mutant N715C, 30°C, pH 5.7
1.8
ATP
mutant L806A, pH 5.7, 30°C
1.9
ATP
-
glucose-starved cells
2.4
ATP
-
basal enzyme state from plasma membrane, at pH 5.9 and 30°C
2.8
ATP
-
mutant D718C, 30°C, pH 5.7
0.05
vanadate
-
mutant D617A, pH 6.5, 30°C
0.052
vanadate
-
mutant D617A/D684N, pH 6.5, 30°C
0.056
vanadate
-
mutant D684N, pH 6.5, 30°C
0.064
vanadate
-
wild-type, pH 6.5, 30°C
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0.0067
2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
Saccharomyces cerevisiae
-
pH 6.5, 30°C
0.06615
2-methylbenzisoselenazol-3(2H)-one
Candida albicans
-
pH and temperature not specified in the publication
0.03345
2-n-propylbenzisoselenazol-3(2H)-one
Candida albicans
-
pH and temperature not specified in the publication
0.0025 - 0.006
2-phenyl-1,2-benzisoselenazol-3(2H)-one
0.004
2-phenyl-1,2-benzisoselenazol-3(2H)-one 1-oxide
Saccharomyces cerevisiae
-
pH 6.5, 30°C
0.01686
2-phenyl-7-azabenzisoselenazol-3(2H)-one
Candida albicans
-
pH and temperature not specified in the publication
0.01969
2-phenylbenzisothiazol-3(2H)-one
Candida albicans
-
pH and temperature not specified in the publication
100
Al3+
Lupinus albus
-
at pH 6.5, temperature not specified in the publication
0.00002
bafilomycin A1
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.1
benzisoselenazol-3(2H)-one
Candida albicans
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0054
destruxin B
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.01814
ebselen
Candida albicans
-
pH and temperature not specified in the publication
0.1
fluconazole
Candida albicans
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.000004
folimycin
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.0025
2-phenyl-1,2-benzisoselenazol-3(2H)-one
Saccharomyces cerevisiae
-
pH 6.5, 30°C
0.003
2-phenyl-1,2-benzisoselenazol-3(2H)-one
Saccharomyces cerevisiae
-
pH not specified in the publication, 30°C
0.006
2-phenyl-1,2-benzisoselenazol-3(2H)-one
Candida albicans
-
pH not specified in the publication, 30°C
0.0013
vanadate
Saccharomyces cerevisiae
mutant N792D, pH 5.7, 30°C
0.0015
vanadate
Saccharomyces cerevisiae
mutant M791A, pH 5.7, 30°C
0.0015
vanadate
Saccharomyces cerevisiae
mutant N792H, pH 5.7, 30°C
0.0015
vanadate
Saccharomyces cerevisiae
mutant N792Q, pH 5.7, 30°C
0.0015
vanadate
Saccharomyces cerevisiae
mutant Q798E, pH 5.7, 30°C
0.0015
vanadate
Saccharomyces cerevisiae
wild-type, pH 5.7, 30°C
0.0018
vanadate
Saccharomyces cerevisiae
mutant I809A, pH 5.7, 30°C
0.0018
vanadate
Saccharomyces cerevisiae
mutant L797A, pH 5.7, 30°C
0.0018
vanadate
Saccharomyces cerevisiae
mutant T802A, pH 5.7, 30°C
0.0019
vanadate
Saccharomyces cerevisiae
mutant M795A, pH 5.7, 30°C
0.002
vanadate
Saccharomyces cerevisiae
mutant G793E, pH 5.7, 30°C
0.002
vanadate
Saccharomyces cerevisiae
mutant L806A, pH 5.7, 30°C
0.0021
vanadate
Saccharomyces cerevisiae
mutant S800A, pH 5.7, 30°C
0.0021
vanadate
Saccharomyces cerevisiae
mutant T810A, pH 5.7, 30°C
0.0022
vanadate
Saccharomyces cerevisiae
mutant N792A, pH 5.7, 30°C
0.0022
vanadate
Saccharomyces cerevisiae
mutant R811A, pH 5.7, 30°C
0.0022
vanadate
Saccharomyces cerevisiae
mutant W805A, pH 5.7, 30°C
0.0026
vanadate
Saccharomyces cerevisiae
mutant F808A, pH 5.7, 30°C
0.0027
vanadate
Saccharomyces cerevisiae
mutant N804A, pH 5.7, 30°C
0.0029
vanadate
Saccharomyces cerevisiae
mutant G793A, pH 5.7, 30°C
0.0042
vanadate
Saccharomyces cerevisiae
mutant E803A, pH 5.7, 30°C
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malfunction
-
inactivation of the enzyme can affect the CO2 uptake in a plant cell
malfunction
-
isoform AHA2-deficient plants exhibit reduced primary root elongation and lower H+ efflux in the root elongation zone. Isoform AHA7-deficient plants exhibit reduced root hair density and lower H+ efflux in the root hair zone
physiological function
-
the high capacity proton pump Pma1p plays a critical role in the intracellular regulation of pH and in nutrient uptake of yeast
physiological function
-
the plasma membrane H + -ATPase drives the stomatal opening, which is mediated by blue light receptor phototropins, by activation of via phosphorylation of the penultimate threonine in the C-terminus and subsequent binding of a 14-3-3 protein
physiological function
-
the plasma membrane H + -ATPase drives the stomatal opening, which is mediated by blue light receptor phototropins, by activation of via phosphorylation of the penultimate threonine in the C-terminus and subsequent binding of a 14-3-3 protein
physiological function
-
the protons secreted by the enzyme in osteoclast membrane into the closed extracellular compartment are essential for demineralization of calcified bone
physiological function
-
v-ATPase is a multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells
physiological function
-
H+-ATPase is a key enzyme of cell metabolism generating electrochemical proton gradient across the plasma membrane, thus playing an important role in the maintenance of ion homeostasis in the cell
physiological function
-
plasma membrane H+-ATPases play a major role in the apoplastic acidification by H+ transport from cytosol to the apoplast
physiological function
the plasma membrane H+-ATPase generates an electrochemical gradient of H+ across the plasma membrane that provides the driving force for solute transport and regulates pH homeostasis and membrane potential
physiological function
-
vacuolar proton-translocating ATPase is responsible for organelle acidification
physiological function
a TNt1 insertion mutant is impaired in the development of arbuscules but not in root colonization by Rhizophagus irregularis hyphae. Artificial microRNA silencing of HA1 results in small and truncated arbuscules. Unlike the wild type, the mutant fails to show a positive growth response to mycorrhizal colonization under phosphate-limiting conditions. Mutants are unable to take up phosphate via the mycorrhizal pathway. In the apoplast of abnormal arbuscule-containing cells of the mutant pH is increased. HA1 may be crucial for building a proton gradient across the periarbuscular membrane and indispensible for the transfer of phosphate from the fungus to the plant
physiological function
-
plasma membrane activity largely increases in Ca2+-treated plants. Higher ATPase activity is related with apoplast acidification, cytosol alkalinization and low cytosolic [Na+], and may explain why extra calcium improves shoot and leaf growth
physiological function
plasma membrane H+-ATPase AHA1 activity in transgenic plants lacking cytoplasmic immune receptor RPM1 is significantly lower than that in plants lacking cytoplasmic immune receptor RPM1 but expressing Pseudomonas syringae effector protein AvrB. AHA1 promotes the interaction between the jasmonate receptor CORONATINE INSENSITIVE1 and JASMONATE ZIM-DOMAIN proteins and enhances jasmonate signaling, which is required for optimum stomatal infection in AHA1-active plants. Pseudomonas syringae effector protein AvrB also induces the CORONATINE INSENSITIVE1 and JASMONATE ZIM-DOMAIN interaction and the degradation of multiple JASMONATE ZIM-DOMAIN proteins
physiological function
primary root length is significantly shorter in the an Aha2 mutant line in both short (10 day) and long-term (6 week) experiments
physiological function
the H+ efflux and Ca2+ influx in guard cells is impaired by vanadate pre-treatment or plasma membrane H+-ATPase Aha1 mutation, suggesting that the rapid H+ efflux mediated by plasma membrane H+-ATPases can function upstream of the Ca2+ flux. Treatment with methyl jasmonate induces transmembrane H+ efflux. After the rapid H+ efflux, the guard cells have a longer oscillation period than before treatment, indicating reduced activity of the plasma membrane H+-ATPase
physiological function
-
isoform AHA1 plays a major role in stomatal opening in response to blue light
physiological function
-
the enzyme generates the electrochemical proton-motive force across the membrane that drives the energy-dependent uptake of amino acids, sugars, nucleosides, and inorganic ions. In addition, H+ transport mediated by this enzyme contributes to the regulation of intracellular pH and surface pH along the hyphae
physiological function
-
the enzyme is involved in the lower accumulation of nitrogen in tea roots cultivated in nitrate nutrient at pH 4.0 than at pH 5.0
physiological function
-
the enzyme is involved in this NH4+ efflux process of barley roots
physiological function
-
the enzyme plays important roles in organic acids exudation in plant response to aluminium toxicity and phosphorus deficiency stresses
physiological function
the higher H+-pumping activity generated by the enzyme improves the growth of transgenic plants via regulating ion and reactive oxygen species homeostasis in plant cells under salinity stress (100-200 mM NaCl for 7-10 days)
physiological function
-
the membrane potential and proton gradient created by the enzyme energize multiple ion channels and various H+-coupled transporters in the plasma membrane for diverse physiological responses including stomatal movement, phloem loading and unloading, xylem loading and unloading, seed germination, solute uptake in roots, leaf movement, tip growth, and cell expansion
physiological function
-
the plasma membrane H+-ATPase-mediated H+ influx is associated with the maintenance of cytosolic pH and the plasma membrane gradients as well as aluminium-induced citrate efflux mediated by a H+-ATPase-coupled MATE co-transport system. Activation of the enzyme improves plant resistance to aluminum stress
physiological function
-
the vacuolar proton pump consists of two interacting P-ATPases, PH1 and PH5, that hyper-acidify the vacuoles of petal cells. The combination of isoforms PH1 and PH5 is required for the reddish color of the petals necessary for the attraction of pollinators. Isoform PH5, but not PH1, is required for the accumulation of tannins in the seeds
physiological function
-
the vacuolar proton pump consists of two interacting P-ATPases, PH1 and PH5, that hyper-acidify the vacuoles of petal cells. The combination of isoforms PH1 and PH5 is required for the reddish color of the petals necessary for the attraction of pollinators. Isoform PH5, but not PH1, is required for the accumulation of tannins in the seeds
physiological function
-
under low-phosphorus conditions, isoform AHA2 acts mainly to modulate primary root elongation by mediating H+ efflux in the root elongation zone, whereas isoform AHA7 plays an important role in root hair formation by mediating H+ efflux in the root hair zone
physiological function
-
vacuolar H+-ATPase is responsible for the creation and maintenance of trans-membrane electrochemical gradients in the nuclear membranes
physiological function
-
the high capacity proton pump Pma1p plays a critical role in the intracellular regulation of pH and in nutrient uptake of yeast
-
physiological function
-
the enzyme generates the electrochemical proton-motive force across the membrane that drives the energy-dependent uptake of amino acids, sugars, nucleosides, and inorganic ions. In addition, H+ transport mediated by this enzyme contributes to the regulation of intracellular pH and surface pH along the hyphae
-
physiological function
-
vacuolar proton-translocating ATPase is responsible for organelle acidification
-
additional information
-
a protein kinase-phosphatase pair, K-252a-insensitive protein kinase and Mg2+ -dependent type 2C protein phosphatase, co-localizes at least in part with the H+-ATPase in the plasma membrane and regulates the phosphorylation status of the penultimate threonine of the H+-ATPase
additional information
-
a protein kinase-phosphatase pair, K-252a-insensitive protein kinase and Mg2+ -dependent type 2C protein phosphatase, co-localizes at least in part with the H+-ATPase in the plasma membrane and regulates the phosphorylation status of the penultimate threonine of the H+-ATPase
additional information
-
Ca2+ facilitates a dynamin- and V-ATPase-dependent endocytosis in association with with an inhibition of the plasma membrane V-ATPase, overview
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D617A
-
35% increase in catalytic activity
D617A/D684N
-
22% of wild-type activity, insensitive to vanadate
D684N
-
24% of wild-type activity, insensitve to vanadate
G602D
-
the mutant has impaired activity compared to the wild type enzyme
E14D
-
constitutively activated
E14D/S938A
-
constitutively activated /phosphorylation site
E14D/S938D
-
constitutively activated /phosphorylation site
E14D/T931A
-
constitutively activated /phosphorylation site
E14D/T931D
-
constitutively activated /phosphorylation site
E14D/T955A
-
constitutively activated /phosphorylation site
H930A
-
binding of regulatory protein 14-3-3 to the entire binding motif of the enzyme, i.e. residues 905-956 bearing the mutation, is significantly reduced
K943E
-
binding of regulatory protein 14-3-3 to the entire binding motif of the enzyme, i.e. residues 905-956 bearing the mutation, is significantly reduced
L932A
-
binding of regulatory protein 14-3-3 to the entire binding motif of the enzyme, i.e. residues 905-956 bearing the mutation, is significantly reduced
N510K
-
constitutively activated
N510K/S938A
-
constitutively activated /phosphorylation site
N510K/S938D
-
constitutively activated /phosphorylation site
P154R
-
constitutively activated
P154R/S938D
-
constitutively activated /phosphorylation site
S938D
-
phosphorylation site
S938E
-
binding of regulatory protein 14-3-3 to the entire binding motif of the enzyme, i.e. residues 905-956 bearing the mutation, is significantly reduced
T931A/S938A
-
phosphorylation sites
T931D
-
phosphorylation site
A135F
-
rate of acidification rapidly declines
A135G
-
wild-type rate of medium acidification
A135I
-
reduction in initial rate of acidification
A135L
-
wild-type rate of medium acidification
A135V
-
wild-type rate of medium acidification
C376L
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 65% of the activity of the wild type enzyme, 5fold increase in Ki for vanadate
D378N
-
5fold lower Ki for vanadate than in wild type
D378S
-
model substrate for endoplasmic reticulum-associated degradation. Expression of the misfolded mutant proein induces heat shock response in the absence of elevated temperatures. Role for Hsp70 cytoplasmic chaperones in recognition by the endoplasmic reticulum-associated ubiquitination pathway
D534N
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 10% of the activity of the wild type enzyme
D560N
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 5% of the activity of the wild type enzyme
D634N
-
slow turnover, increased level of phosphorylated enzyme-intermediate, 10fold increase in Ki for vanadate
D638N
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 5% of the activity of the wild type enzyme
D714C
-
mutation blocks trafficking, enzyme is not delivered to secretory vesicles. 4% of wild-type ATP hydrolysis
D714V
-
4% of wild-type expression, intracellular trafficking is disrupted
D718A
-
79% of wild-type expression, 104% of wild-type ATP hydrolysis
D718C
-
84% of wild-type expression, 108% of wild-type ATP hydrolysis
D720C
-
85% of wild-type expression, 80% of wild-type ATP hydrolysis
D720V
-
41% of wild-type expression
D730N
-
increased level of phosphorylated enzyme-intermediate
F808A
83% of wild-type activity
G793A
38% of wild-type activity
G793E
36% of wild-type activity
I719A
-
3fold reduction in coupling ratio between ATP hydrolysis and H+ transport
I719C
-
mutant is similar to wild-type
I809A
88% of wild-type activity
K474H
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 10% of the activity of the wild type enzyme
K474Q
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is less than 5% of the activity of the wild type enzyme
K474R
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 30% of the activity of the wild type enzyme
L327V
-
different from wild type by resistance to hygromycin
L717A
-
mutation blocks trafficking, enzyme is not delivered to secretory vesicles
L717C
-
mutation blocks trafficking, enzyme is not delivered to secretory vesicles
L806A
120% of wild-type activity
M791A
49% of wild-type activity
M795A
45% of wild-type activity
N715A
-
68% of wild-type expression, 71% of wild-type ATP hydrolysis
N715C
-
88% of wild-type expression, 58% of wild-type ATP hydrolysis
N792A
53% of wild-type activity
N792D
98% of wild-type activity
N792H
64% of wild-type activity
N792Q
118% of wild-type activity
N804A
46% of wild-type activity
P335A
-
30% decrease in ATPase activity, 60% decrease in H+ transport
Q798E
78% of wild-type activity
R811A
86% of wild-type activity
S234A
-
3.5fold increase in ATPase activity, 20% decrease in H+ transport
S660C
-
different from wild type by resistance to hygromycin
S660F/F611L
-
different from wild type by resistance to hygromycin
S716A
-
71% of wild-type expression, 60% of wild-type ATP hydrolysis
S716C
-
95% of wild-type expression, 101% of wild-type ATP hydrolysis
S800A
89% of wild-type activity, mutation in the middle of transmembrane helix M8, increase in apparent stoichiometry of H+ transport
T231G
-
greatly increased level of phosphorylated enzyme-intermediate, 30fold higher Ki for vanadate
T802A
52% of wild-type activity
T810A
84% of wild-type activity
W805A
65% of wild-type activity
D714C
-
mutation blocks trafficking, enzyme is not delivered to secretory vesicles. 4% of wild-type ATP hydrolysis
-
D720E
-
61% of wild-type expression
-
F796A
-
4% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation causes enzyme and cell sensitivity to heat shock when expressed in secretory vesicles
-
I794A
-
4% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation increases temperature sensitivity of cells when the enzyme is expressed either in secretory vesicles or, to a lesser extent, in plasma membrane
-
I799A
-
2% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation is lethal for cells regardless of expression of the enzyme in secretory vesicles or plasma membrane
-
L797A
-
20% ATPase and 17% H+ transport activity compared to the wild type enzyme
-
Q798A
-
1% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation is lethal for cells regardless of expression of the enzyme in secretory vesicles or plasma membrane
-
S938A
-
binding of regulatory protein 14-3-3 to the entire binding motif of the enzyme, i.e. residues 905-956 bearing the mutation, is increased
S938A
-
phosphorylation site
T931A
-
binding of regulatory protein 14-3-3 to the entire binding motif of the enzyme, i.e. residues 905-956 bearing the mutation, is significantly reduced
T931A
-
phosphorylation site
D226N
-
decreased turnover and level of phosphorylated enzyme-intermediate
D226N
-
5% decrease in ATPase activity, 35% decrease in H+ transport
D378E
-
5fold lower Ki for vanadate than in wild type
D378E
-
no decrease in ATPase activity, 65% decrease in H+ transport
D378T
-
about 3fold lower Ki for vanadate than in wild type
D378T
-
20% decrease in ATPase activity, 85% decrease in H+ transport
D714A
-
22% of wild-type expression, intracellular trafficking is disrupted
D714A
-
5fold decrease in expression, loss of catalytic activity
D714E
-
12% of wild-type expression, 7% of wild-type ATP hydrolysis
D714E
-
12% of wild-type expression, intracellular trafficking is disrupted
D714N
-
67% of wild-type expression
D714N
-
67% of wild-type expression, 97% of wild-type ATP hydrolysis
D720A
-
63% of wild-type expression
D720A
-
65% of wild-type expression, 47% of wild-type ATP hydrolysis
D720E
-
61% of wild-type expression
D720E
-
61% of wild-type expression, 87% of wild-type ATP hydrolysis
D720N
-
72% of wild-type expression
D720N
-
72% of wild-type expression, 88% of wild-type ATP hydrolysis
E233Q
-
no turnover, increased level of phosphorylated enzyme-intermediate
E233Q
-
70% decrease in ATPase activity, 85% decrease in H+ transport
E803A
74% of wild-type activity
E803A
-
15% ATPase and 13% H+ transport activity compared to the wild type enzyme. The mutation has no significant influence on the ATPase and cell sensitivity to heat shock. However, it causes a shift in the equilibrium between E1 and E2 conformations of the enzyme towards E1
F796A
no catalytic activity
F796A
-
4% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation causes enzyme and cell sensitivity to heat shock when expressed in secretory vesicles
I794A
no catalytic activity
I794A
-
4% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation increases temperature sensitivity of cells when the enzyme is expressed either in secretory vesicles or, to a lesser extent, in plasma membrane
I799A
no catalytic activity
I799A
-
2% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation is lethal for cells regardless of expression of the enzyme in secretory vesicles or plasma membrane
I807A
no catalytic activity
I807A
-
11% ATPase and no H+ transport activity compared to the wild type enzyme
K379Q
-
mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 70% of the activity of the wild type enzyme
K379Q
-
abour 3fold lower Ki for vanadate than in wild type
L797A
105% of wild-type activity
L797A
-
20% ATPase and 17% H+ transport activity compared to the wild type enzyme
L801A
no catalytic activity
L801A
-
7% ATPase and no H+ transport activity compared to the wild type enzyme
Q798A
no catalytic activity
Q798A
-
1% ATPase and no H+ transport activity compared to the wild type enzyme. The mutation is lethal for cells regardless of expression of the enzyme in secretory vesicles or plasma membrane
D714A
-
22% of wild-type expression, intracellular trafficking is disrupted
-
D714A
-
5fold decrease in expression, loss of catalytic activity
-
D714E
-
12% of wild-type expression, intracellular trafficking is disrupted
-
D714E
-
12% of wild-type expression, 7% of wild-type ATP hydrolysis
-
D714N
-
67% of wild-type expression
-
D714N
-
67% of wild-type expression, 97% of wild-type ATP hydrolysis
-
D720A
-
63% of wild-type expression
-
D720A
-
65% of wild-type expression, 47% of wild-type ATP hydrolysis
-
additional information
-
mutant cax3 defective in vacuolar transport displays a reduction in vacuolar H+/Ca2+-transport during salt stress and decreased plasma membrane ATPase ativity
additional information
-
transgenic Arabidopsis thaliana plants absorb more phosphorus under low-phosphorus conditions than wild-type. Increase in activity of enzyme by phosphorus starvation is caused by transcriptional and translational regulation
additional information
-
mutant 210 exhibits a single T-DNA insertion into the promoter region of PMA1 gene leading to twofold reduction in expression. Mutant displays a total loss of pathogenicity towards its host plant, it is unable to germinate on the host leaf surface
additional information
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expression of wild-type gene in Nicotiana tabacum at 4fold increased level does not result in modification of external acidification rates, or any unusual phenotype despite markedly increased activity of H+-ATPase activity. Plants expressing a gene lacking the C-terminal 103 residues corresponding to the autoinhibitory domain and therefore a constitutively activated enzyme display a lower apoplastic and external root pH value, abnormal leaf inclination, and twisted stems. They also exhibit increased salt tolerance during germination and seedling growth
additional information
enzyme is functional in Saccharomyces cerevisiae
additional information
-
enzyme contains an inhibitory C-terminal domain, removal of the final 40 amino acids significantly Vmax value and growth of cells at pH 6.5. Enzyme is functional in Saccharomyces cerevisiae
additional information
-
in plasma membrane fractions of mutants lacking vaculolar H+-ATPase activity, the activity of plasma membrane H+-ATPase is 65-75% lower than in wild-type. In the mutant, plasma membrane H+-ATPase protein is reduced in plasma membrane and increased at the vacuole and other compartments
additional information
generation of stepwise truncation mutants. Truncations upstream of Lys889, removing more than 30 amino acid residues, yield no viable mutants, and the stretch from Ala881 (at the end of TM10) to Gly888 is required for stable folding and plasma membrane targeting. The stretch between Lys889 and Lys916 is ubiquitinated in carbon-starved cells as part of cellular quality control and is essential for normal ATPase folding and stability, as well as for autoinhibition of ATPase activity during glucose starvation. Removal of even one or two residues (Glu917 and Thr918) from the extreme C-terminus leads to visibly reduced expression of the ATPase at the plasma membrane
additional information
enzyme depletion by RNAi causes growth inhibition, which is more accentuated in procyclic forms. Knock-down of TbHA1 results in cells with lower steady-state intracellular pH value and a slower rate of intracellular pH value recovery from acidification. Enzyme is functional in Saccharomyces cerevisiae
additional information
enzyme depletion by RNAi causes growth inhibition, which is more accentuated in procyclic forms. Knock-down of TbHA1 results in cells with lower steady-state intracellular pH value and a slower rate of intracellular pH value recovery from acidification. Enzyme is functional in Saccharomyces cerevisiae
additional information
enzyme depletion by RNAi causes growth inhibition, which is more accentuated in procyclic forms. Knock-down of TbHA1 results in cells with lower steady-state intracellular pH value and a slower rate of intracellular pH value recovery from acidification. Enzyme is functional in Saccharomyces cerevisiae
additional information
-
enzyme depletion by RNAi causes growth inhibition, which is more accentuated in procyclic forms. Knock-down of TbHA1 results in cells with lower steady-state intracellular pH value and a slower rate of intracellular pH value recovery from acidification. Enzyme is functional in Saccharomyces cerevisiae
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24 h after the larvae are infected with the Bombyx mori nucleopolyhedrovirus, the expression level of the V-ATPase B subunit in the midgut of the resistant strain NB is about 3times higher than in the susceptible strain 306 then the expression level of the V-ATPase B subunit decreases rapidly to a very low level
5 mM H2O2 induces expression of PM H+-ATPase isoform HA2
5 mM H2O2 induces expression of PM H+-ATPase isoform HA3
5 mM H2O2 induces expression of PM H+-ATPase isoforms HA4, HA8, HA9, and HA10
activation of the plasma membrane H+-ATPase occurs under phosphate deficiency and salt and heavy metal stresses
-
an increased Na+/K+ ratio decreases the enzyme activity. A significant decrease in hydrolytic activity is observed at 25 mM Na+ concentration at pH 7.0 (reduction in active H+ flux is 20%). The active H+ flux is decreased to 80% when 100 mM K+ are substituted by 100 mM Na+
-
at 25 mM Na+ concentration, hydrolytic activity is not affected (reduction in active H+ flux is 5%)
-
enzyme activity of barley roots under NH4+ nutrition (1 mM) is significantly higher than that under NO3- nutrition
-
exposure of tomato roots to 0.01 mM aluminium (Al), for 1 h increases the mRNA accumulation of isoform LHA1. The activity of the enzyme reaches a maximum in the roots exposed to 0.01 mM Al, and higher Al concentrations results in a decline of the activity, although it is still stimulated by 0.05 mM Al when compared with the control roots. The regulation of plasma membrane H+-ATPase in response to Al is subjected to transcriptional and posttranscriptional control. Exposure of tomato roots to 0.01 mM LaCl3 for 1 h also causes a significant increase in enzymatic activity
exposure of tomato roots to 0.01 mM aluminium (Al), for 1 h increases the mRNA accumulation of isoform LHA2. The activity of the enzyme reaches a maximum in the roots exposed to 0.01 mM Al, and higher Al concentrations results in a decline of the activity, although it is still stimulated by 0.05 mM Al when compared with the control roots. The regulation of plasma membrane H+-ATPase in response to Al is subjected to transcriptional and posttranscriptional control. Exposure of tomato roots to 0.01 mM LaCl3 for 1 h also causes a significant increase in enzymatic activity
exposure of tomato roots to 0.01 mM aluminium (Al), for 1 h increases the mRNA accumulation of isoform LHA4. The activity of the enzyme reaches a maximum in the roots exposed to 0.01 mM Al, and higher Al concentrations results in a decline of the activity, although it is still stimulated by 0.05 mM Al when compared with the control roots. The regulation of plasma membrane H+-ATPase in response to Al is subjected to transcriptional and posttranscriptional control. Exposure of tomato roots to 0.01 mM LaCl3 for 1 h also causes a significant increase in enzymatic activity
expression is decreased in the presence of 80 microM Fe
expression is induced by ethylene treatment
expression is repressed by ethylene treatment
expression is up to 2fold up-regulated under Fe deficiency in cucumber roots
expression of Aha2 is induced twofold to threefold by low nitrate in wild-type roots
high (7.0 mM) nitrate level represses primary and lateral root elongation and it is associated with reduced Aha2 expression in wild-type roots
in developing rose petals, isoform PH5 and RhPH1 mRNAs are expressed, simultaneously with the accumulation of pigments, and their expression decreases later in development
-
methyl-ammonium has no significant effect on enzyme activity
-
nitrate stress leads to higher enzyme activity
-
plasma membrane H+-ATPase hydrolytic and pumping activities are not affected by application of 150 mM NaCl
-
root-localized isoforms PMA1, PMA2 and PMA3 transcripts are upregulated under conditions of iron deficiency
-
the active H+ flux is decreased to 60% when 100 mM K+ are substituted by 100 mM Na+
-
the activity and mRNA level of PM-H+-ATPase isoform HA2 is decreased in plants treated for 3 days with a temperature of 10°C
the activity and mRNA level of PM-H+-ATPase isoform HA3, is decreased in plants treated for 3 days with a temperature of 10°C
the activity and mRNA level of PM-H+-ATPase isoforms HA4, HA8, HA9, and HA10 is decreased in plants treated for 3 days with a temperature of 10°C
the enzyme expression is up-regulated by aluminium stress and phosphorus deficiency
-
the expression of isoforms AHA2 and AHA7 in roots is enhanced under low-phosphorus stress conditions
-
there is 57% higher enzyme activity in vacuoles isolated after cell growth at extracellular pH of 7.0 than after growth at pH 5.0 in minimal medium
transcript levels of plasma membrane H+-ATPase are elevated in cucumber roots after 24-h treatment of plants with abscisic acid or H2O2. Heat shock elevates the endogenous level of abscisic acid both in plants treated for 2 h with heat shock and in post-stress plants
-
there is 57% higher enzyme activity in vacuoles isolated after cell growth at extracellular pH of 7.0 than after growth at pH 5.0 in minimal medium
-
there is 57% higher enzyme activity in vacuoles isolated after cell growth at extracellular pH of 7.0 than after growth at pH 5.0 in minimal medium
-
-
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