Information on EC 3.6.3.6 - H+-exporting ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.3.6
-
RECOMMENDED NAME
GeneOntology No.
H+-exporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphate bond
-
-
-
-
transmembrane transport
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Oxidative phosphorylation
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
B subunit; strains strain NB and 306
UniProt
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
var. marathon
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
a fluconazole-resistant strain, gene PMA1
-
-
Manually annotated by BRENDA team
Candida albicans ATCC 96901
a fluconazole-resistant strain, gene PMA1
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
cv. Amiga
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
gene PMA1b, protein sequence idetical to PMA1a; differenial expression during asexual development, with a more than 10fold increase in expression in germinated cysts
SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
gene PMA1
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-
Manually annotated by BRENDA team
gene PMA1
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-
Manually annotated by BRENDA team
strain NY13
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Zea mays Pioneer 3906
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
dATP + H2O + H+/in
dADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
-
6.5% of the activity with ATP
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
9.5% of the activity with ATP
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
-
9.5% of the activity with ATP
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-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
19% of the activity with Mg2+
CaSO4
-
in plants grown with 5 mM CaSO4 supply, Vmax of plasma membrane ATPase increases
Iron
-
the process of H+secretion, driven by PM-H+-ATPase, is enhanced in iron-deficient rice roots
NaCl
-
in plants grown with 100 mM NaCl supply, ATPase activity increases with salinity in a non-competitive way for 7 d and 21 d. 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
Zn2+
-
33% of the activity with Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Butanedione
-
-
2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
-
an ebselen analogue
2-phenyl-1,2-benzisoselenazol-3(2H)-one
2-phenyl-1,2-benzisoselenazol-3(2H)-one 1-oxide
-
an ebselen analogue
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
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5 mM, 60% inhibition, Kd value 0.8 mM
Al3+
-
inhibition of H+-ATPase activity, Mg2+ partly prevents
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
bafilomycin A1
-
-
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
Dicyclohexylcarbodiimide
diethylstilbestrol
-
-
distilbestrol
fluoroaluminates
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Mg2+ is an essential cofactor for inhibition, biphasic inhibitory process at pH 7.5 with a preference for AlF4- species
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Hemileia vastatrix
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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%
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iejimalide A
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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
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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+
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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
K-252a
K2SO4
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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
lansoprazole
-
-
miconazole
molybdate
N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline
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no protection by MgADP-, protection by MgATP2- or Mg-vanadate
N-ethylmaleimide
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2 mM, 26% inhibition
Na2MO4
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weak
Na3VO4
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0.1 mM
NEM
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pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
Omeprazole
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-
orthovanadate
-
-
oxidized glutathione
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-
p-hydroxymercuribenzoate
Phenylglyoxal
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pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
SidK
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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
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Triton X-100
Trypsin
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85% inhibition of the enzyme in plasma membrane vesicles in absence of MgATP2-, no inhibition in presence of MgATP2-
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vanadate
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14-3-3-protein
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AlK(SO4)2
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treatment of cells results in increase in vandate-sensitive H+-transport and in enzymatic activity, whereas yeast-hypha transition is inhibited
D-glucose
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activates, brings about a global conformational change in H+-ATPase
dithiothreitol
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2 mM, 26% stimulation
fusicoccin
iodoacetic acid
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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
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stimulates
Mg-ATP
Phospholipid
proton pump interactor
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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
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spermine
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.161 - 2.8
ATP
0.6 - 1.5
MgATP2-
0.05 - 0.064
vanadate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 56.7
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.01
vanadate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067
2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
Saccharomyces cerevisiae
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pH 6.5, 30C
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
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pH 6.5, 30C
0.0013 - 0.0042
vanadate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
mutants G793A, G793E
5.6
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mutant L797A
6.3
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wild type enzyme
6.4
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mutants D684N, D617A/D684N
6.6
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histidine-tagged enzyme
6.9 - 7
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assay at
7
5 hours after light start; 5 hours after light start; 5 hours after light start
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 7
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about 45% of maximal activity at pH 5.4 and at pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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enzyme from both variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
and flower, high abundance of transcripts; and flower, high abundance of transcripts
Manually annotated by BRENDA team
and bark, high abundance of transcripts; and bark, high abundance of transcripts
Manually annotated by BRENDA team
high abundance of transcripts; high abundance of transcripts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
recombinant N-terminal cytosolic tail of V-ATPase a2-subunit isoform a2N1-402, NuPAGE
48500
recombinant N-terminal cytosolic tail of V-ATPase a2-subunit isoform a2N1-402, calculated from amino acid sequence
600000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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phosphorylation of the dimer triggers the binding of 14-3-3 dimers, resulting in a heterododecamer (six ATPase and six 14-3-3 molecules)
homohexamer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
side-chain modification
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contains 80 mol of phospholipid per mol of 100000 Da ATPase, 60% phosphatidylcholine, 30% phosphatidylethanolamine, 5% lysophosphatidylcholine
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
functional unit is defined by ten transmembrane helices and three cytoplasmic domains. Transmembrane domains reveal a large cavity, located near the middle of the membrane plane and lined by conserved hydrophilic and charged residues
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purified recombinant AHA2 in detergent micelles, X-ray diffraction structure determination and anaylsis at 3.5 A resolution, molecular replacement and low-resolution MR, AHA2 trimming of the search model by the removal of non-conserved loop regions
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two-dimensional crystallization of the reconstituted enzyme
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dodecylmaltoside complex
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regulatory protein 14-3-3 in complex with the entire binding motif of the enzyme, i.e. residues 905-956 expressed in yeast, and in complex with the hexameric enzyme. Three 14-3-3 dimers are located on top of a PMA2 hexamer where they may coordinate six autoinhibitory domains of the active enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NDSB-256 is required not only during protein refolding but also afterward for stabilization of a2N1-402 protein in the solution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme fused to glutathione S-transferase, expressed in Escherichia coli
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large-scale purification
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Ni2+-affinity chromatography
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Talon bead chromatography, HisTrap column chromatography, and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AHA2, overexpression in Saccharomyces cerevisiae
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cloning of pma-1-A135V revertant alleles
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enzyme fused to glutathione S-transferase, expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae NY13 cells
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expression in Arabidopsis thaliana
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expression in Nicotiana tabacum, either wild-type gene or gene lacking the C-terminal 103 residues corresponding to the autoinhibitory domain
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expression in Saccharomyces cerevisiae
subunit a2N1-402 is expressed in Escherichia coli BL21(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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+
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at 25 mM Na+ concentration, hydrolytic activity is not affected (reduction in active H+ flux is 5%)
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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 decreased in the presence of 80 microM Fe
expression is induced by ethylene treatment; expression is induced by ethylene treatment; 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 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
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high (7.0 mM) nitrate level represses primary and lateral root elongation and it is associated with reduced Aha2 expression in wild-type roots
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plasma membrane H+-ATPase hydrolytic and pumping activities are not affected by application of 150 mM NaCl
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root-localized isoforms PMA1, PMA2 and PMA3 transcripts are upregulated under conditions of iron deficiency
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the active H+ flux is decreased to 60% when 100 mM K+ are substituted by 100 mM Na+
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the activity and mRNA level of PM-H+-ATPase isoform HA2 is decreased in plants treated for 3 days with a temperature of 10C; the activity and mRNA level of PM-H+-ATPase isoform HA3, is decreased in plants treated for 3 days with a temperature of 10C; 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 10C
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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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
D226N
-
5% decrease in ATPase activity, 35% decrease in H+ transport; decreased turnover and level of phosphorylated enzyme-intermediate
D378E
-
5fold lower Ki for vanadate than in wild type; no decrease in ATPase activity, 65% decrease in H+ transport
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
D378T
-
20% decrease in ATPase activity, 85% decrease in H+ transport; about 3fold lower Ki for vanadate than in wild type
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
E233Q
-
70% decrease in ATPase activity, 85% decrease in H+ transport; no turnover, 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
K379Q
-
abour 3fold lower Ki for vanadate than in wild type; mutation decreases activity and phosphorylation to a similar extent, ATPase activity is 70% of the activity of the wild type enzyme
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
D714A
-
22% of wild-type expression, intracellular trafficking is disrupted; 5fold decrease in expression, loss of catalytic activity
-
D714C
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mutation blocks trafficking, enzyme is not delivered to secretory vesicles. 4% of wild-type ATP hydrolysis
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D714E
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12% of wild-type expression, 7% of wild-type ATP hydrolysis; 12% of wild-type expression, intracellular trafficking is disrupted
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D714N
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67% of wild-type expression; 67% of wild-type expression, 97% of wild-type ATP hydrolysis
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D720A
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63% of wild-type expression; 65% of wild-type expression, 47% of wild-type ATP hydrolysis
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D720E
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61% of wild-type expression
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F796A
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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
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I794A
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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
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I799A
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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
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L797A
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20% ATPase and 17% H+ transport activity compared to the wild type enzyme
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Q798A
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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
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additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
best refolding conditions are 1 M NDSB-256, 1 mM dithiothreitol, 100 mM CHES, and pH 9.0
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
drug development
nutrition
Show AA Sequence (2265 entries)
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