Information on EC 3.6.3.6 - H+-exporting ATPase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
3.6.3.6
-
RECOMMENDED NAME
GeneOntology No.
H+-exporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
mechanism involves a covalent phosphoryl-enzyme intermediate
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
mechanism and transport function; mechanism involves a covalent phosphoryl-enzyme intermediate
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
mechanism involves a covalent phosphoryl-enzyme intermediate; the phosphorylated amino acid being an aspartate
-
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
binding of the nucleotide to the N-domain is coupled to the movement of a loop beta structure and to the exposure of the W505 residue located in the loop
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphate bond
-
-
-
-
transmembrane transport
-
-
-
-
PATHWAY
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP phosphohydrolase
-
-
-
-
auto-inhibited H+-ATPase isoform 2
P19456
-
EC 3.6.1.3
-
-
related
-
EC 3.6.1.35
-
-
formerly
-
EC 3.6.1.35
-
formerly
H+-ATPase
-
-
-
-
H+-ATPase
P19456
-
H+-ATPase
-
-
H+-ATPase
-
-
H+-ATPase
P05030
-
H+-ATPase
Saccharomyces cerevisiae SY4
P05030
-
-
H+-ATPase
-
-
H+-ATPase
-
-
HA1
-
isoform of penultimate threonine-containing H+-ATPase
HA10
-
isoform
HA2
B3VDR8
isoform
HA2
I4DSU9
isoform of penultimate threonine-containing H+-ATPase
HA3
A8JP99
isoform
HA3
I4DSV0
isoform of penultimate threonine-containing H+-ATPase
HA4
-
isoform
HA4
I4DSV1
isoform of penultimate threonine-containing H+-ATPase
HA5
-
isoform of non-penultimate threonine-containing H+-ATPase
HA6
I4DSV3
isoform of non-penultimate threonine-containing H+-ATPase
HA7
I4DSV4
isoform of non-penultimate threonine-containing H+-ATPase
HA8
-
isoform
HA8
I4DSV5
isoform of non-penultimate threonine-containing H+-ATPase
HA9
-
isoform
LDH1A protein
-
-
-
-
LDH1B protein
-
-
-
-
non-penultimate threonine-containing H+-ATPase
I4DSV3, I4DSV4, I4DSV5
non-pT H+-ATPase
P-ATPase proton pump
Q1A4H1
-
P-type H+-ATPase
-
-
P3A H+-ATPase
Q1A4H1
-
PAT2
-
-
-
-
penultimate threonine-containing H+-ATPase
-, I4DSU9, I4DSV0, I4DSV1
pT H+-ATPase
plasma membrane ATPase
-
-
plasma membrane H*-ATPase pump
-
-
plasma membrane H*-ATPase pump
Saccharomyces cerevisiae AH109
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
Candida albicans ATCC 96901
-
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
A8JP99
-
plasma membrane H+-ATPase
B3VDR8
-
plasma membrane H+-ATPase
-, I4DSU9, I4DSV0, I4DSV1, I4DSV3, I4DSV4, I4DSV5
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
Saccharomyces cerevisiae AH109, Saccharomyces cerevisiae CG1945, Saccharomyces cerevisiae EGY48
-
-
-
plasma membrane H+-ATPase
P22180, Q96578, Q9SPD5
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase
-
-
plasma membrane H+-ATPase isoform 2
-
-
plasma membrane H+-ATPase LHA1
Q4VCM0
-
plasma membrane H+-ATPase LHA2
Q4VCL8
-
plasma membrane H+-ATPase LHA3
Q4VCL9
-
plasma membrane P-type H+-ATPase
-
-
plasma membrane V-ATPase
-
-
plasma membrane vacuolar H+-ATPase
-
-
PM H+-ATPase
-
-
PM H+-ATPase
-
-
PM H+-ATPase
A8JP99, B3VDR8
-
PM H+-ATPase
P22180, Q96578, Q9SPD5
-
PM H+-ATPase
-
-
PM proton pump
-, A8JP99, B3VDR8
-
PMA1
Saccharomyces cerevisiae SY4
P05030
-
-
Pma1p
Candida albicans ATCC 96901
-
-
-
Pma1p
Saccharomyces cerevisiae AH109
-
;
-
Pma1p
Saccharomyces cerevisiae CG1945, Saccharomyces cerevisiae EGY48
-
-
-
Proton pump
-
-
-
-
Proton pump 10
-
-
-
-
Proton pump 11
-
-
-
-
proton-translocating ATPase
-
-
-
-
TbHA1
Q86DE0
-
TbHA2
Q7Z1X2
-
TbHA3
Q6WZI6
-
V-ATPase
B3VBE3
-
V-ATPase
-
-
V-ATPase
Q9Y487
-
V-ATPase
-
-
V-ATPase
Saccharomyces cerevisiae BY4741, Saccharomyces cerevisiae SF838-5A
-
-
-
V-ATPase
-
-
vacuolar ATPase
-
-
vacuolar ATPase
Saccharomyces cerevisiae AH109
-
-
-
vacuolar H+-ATPase
-
-
vacuolar H+-ATPase
-
-
vacuolar H+-ATPase
-
-
vacuolar proton-translocating ATPase
-
-
vacuolar proton-translocating ATPase
Saccharomyces cerevisiae BY4741, Saccharomyces cerevisiae SF838-5A
-
-
-
vacuolar-type ATPase
B3VBE3
-
vacuolar-type ATPase
-
-
vacuolar-type H+-ATPase
Q9Y487
-
yeast plasma membrane ATPase
-
-
-
-
yeast plasma membrane H+-ATPase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isozymes AHA1 and AHA2
-
-
Manually annotated by BRENDA team
B subunit; strains strain NB and 306
UniProt
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
variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix
-
-
Manually annotated by BRENDA team
isoform HA2; variant Krak
B3VDR8
UniProt
Manually annotated by BRENDA team
isoform HA3; variant Krak
SwissProt
Manually annotated by BRENDA team
variant Krak
-
-
Manually annotated by BRENDA team
cv. Amiga
Q4VCL8, Q4VCL9, Q4VCM0
SwissProt
Manually annotated by BRENDA team
isoform HA2
UniProt
Manually annotated by BRENDA team
isoform HA3
UniProt
Manually annotated by BRENDA team
isoform HA4
UniProt
Manually annotated by BRENDA team
isoform HA6
UniProt
Manually annotated by BRENDA team
isoform HA7
I4DSV4
UniProt
Manually annotated by BRENDA team
isoform HA8
I4DSV5
UniProt
Manually annotated by BRENDA team
cell wall-less mutants
-
-
Manually annotated by BRENDA team
ssp. japonica cv. Hitomebore
-
-
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
; strain AH109
-
-
Manually annotated by BRENDA team
different wine yeast strains. Wine yeast can be distinguished in terms of ATPase activity and oleic acid and palmitoic acid in plasma membrane
-
-
Manually annotated by BRENDA team
enzyme displays a rapid 5-10fold increase in activity when carbon-starved cells are exposed to glucose. Phosphorylation at S911and T921 is related to glucose activation
-
-
Manually annotated by BRENDA team
strain BY4741
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH109
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH109
gene PMA1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CG1945
gene PMA1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae EGY48
gene PMA1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae NY13
strain NY13
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae SF838-5A
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae SY4
-
Uniprot
Manually annotated by BRENDA team
isoform LHA1; variant Hezuo903
UniProt
Manually annotated by BRENDA team
isoform LHA2; variant Hezuo903
UniProt
Manually annotated by BRENDA team
isoform LHA4; variant Hezuo903
UniProt
Manually annotated by BRENDA team
cultivars Pioneer 3906 and Amadeo (KWS)
-
-
Manually annotated by BRENDA team
highly boron- and salt-tolerant cultivar amylacea
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
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
-
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
-
vacuolar proton-translocating ATPase is responsible for organelle acidification
physiological function
-
plasma membrane H+-ATPases play a major role in the apoplastic acidification by H+ transport from cytosol to the apoplast
physiological function
I4DSU9, I4DSV0, I4DSV1, I4DSV3, I4DSV4, I4DSV5, -
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; 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; 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; 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; 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; 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; 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
Saccharomyces cerevisiae AH109
-
the high capacity proton pump Pma1p plays a critical role in the intracellular regulation of pH and in nutrient uptake of yeast
-
physiological function
Saccharomyces cerevisiae SF838-5A
-
vacuolar proton-translocating ATPase is responsible for organelle acidification
-
physiological function
Saccharomyces cerevisiae SY4
-
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
-
additional information
-
Ca2+ facilitates a dynamin- and V-ATPase-dependent endocytosis in association with with an inhibition of the plasma membrane V-ATPase, overview
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P05030
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
A8JP99, B3VDR8, -
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q4VCL8, Q4VCL9, Q4VCM0
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
P22180, Q96578, Q9SPD5
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Q9Y487
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
specific for ATP
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
mechanism involves a covalent phosphoryl-enzyme intermediate
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
high substrate specificity for ATP
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
high substrate specificity for ATP
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
activity is independent of growth phase
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Saccharomyces cerevisiae AH109
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Saccharomyces cerevisiae SF838-5A
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
Saccharomyces cerevisiae SY4
P05030
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
Saccharomyces cerevisiae AH109
-
-
-
-
?
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
-
-
?
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
-
9.5% of the activity with ATP
-
-
?
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
-
9.5% of the activity with ATP
-
-
?
additional information
?
-
I4DSU9, I4DSV0, I4DSV1, I4DSV3, I4DSV4, I4DSV5, -
14-3-3a protein binds to phosphorylated H+-ATPase
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
activity is independent of growth phase
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
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
show the reaction diagram
Saccharomyces cerevisiae AH109
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
-
-
-
-
?
ATP + H2O + H+in
ADP + phosphate + H+out
show the reaction diagram
Saccharomyces cerevisiae AH109
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
19% of the activity with Mg2+
Co2+
-
43% of the activity with Mg2+
Co2+
-
can substitute for the physiological cofactor Mg2+
K+
-
KCl stimulates
K+
-
K+ stimulates enzyme
Mg2+
-
Mg2+ may bring about an increase in the affinity of the enzyme for MgATP2-; required
Mg2+
-
Mg2+ binding site
Mg2+
-
activates
Mg2+
-
required
Mg2+
-
stimulation. The effect is additive to that of spermine
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required for activity. Activity without inhibition is measured in the presence of 3 mM Mg2+ in excess of total ATP
Mg2+
-
dependent on
Mg2+
-
required
Mn2+
-
36% of the activity with Mg2+
Mn2+
-
can substitute for the physiological cofactor Mg2+
Zn2+
-
33% of the activity with Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
-
an ebselen analogue
-
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. 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, 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 1-oxide
-
an ebselen analogue
-
adenosine 5'-(beta,gamma-imido)-triphosphate
-
5 mM, 60% inhibition
ADP
-
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
-
-
Ca2+
-
completely inactive when Mg2+ is substituted by Ca2+, strongly inhibited by Ca2+ in presence of Mg2+
Ca2+
-
extracellular, inhibits the enzym ein osteoclast membranes, Ca2+ behaves as a negative feedback signal for osteoclast function
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
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
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
no protection by MgATP2-
Dicyclohexylcarbodiimide
-
-
Dicyclohexylcarbodiimide
-
-
Diethylstilbestrol
-
-
distilbestrol
-
-
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
K-252a
-
a potent inhibitor of protein kinase
molybdate
-
86% residual activity at 1 mM
N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline
-
no protection by MgADP-, protection by MgATP2- or Mg-vanadate
N-ethylmaleimide
-
2 mM, 26% inhibition
Na2MO4
-
weak
NEM
-
pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
oxidized glutathione
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
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
-
Triton X-100
-
strong inhibition
Trypsin
-
85% inhibition of the enzyme in plasma membrane vesicles in absence of MgATP2-, no inhibition in presence of MgATP2-
-
vanadate
-
Na3VO4, non-competitive
vanadate
-
inhibition of enzyme, treatment additionally leads to severe suppression of phosphorus uptake by roots in low-phosphorus nutrient solution
vanadate
-
-
vanadate
Q4VCL8, Q4VCL9, Q4VCM0
-
vanadate
-
about 7% residual activity at 0.3 mM
vanadate
A8JP99, B3VDR8, -
-
vanadate
-
8% residual activity at 0.1 mM
vanadate
P22180, Q96578, Q9SPD5
significant inhibition at 0.1 mM; significant inhibition at 0.1 mM; significant inhibition at 0.1 mM
molybdate
-
87% residual activity at 1 mM
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 inhibitory: SCH28080
-
additional information
-
not inhibitory: Ni2+
-
additional information
-
inhibitior screening, overview
-
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
-
ebselen is at least 10fold more potent as antifungal compound compared the azoles fluconazole, itraconazole, and ketoconatzole, and as amphotericin B
-
additional information
-
not inhibited by nitrate, azide, and molybdate
-
additional information
-
not inhibited by azide and nitrate
-
additional information
P22180, Q96578, Q9SPD5
phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
14-3-3-protein
Q4VCL8, Q4VCL9, Q4VCM0
-
-
AlK(SO4)2
-
treatment of cells results in increase in vandate-sensitive H+-transport and in enzymatic activity, whereas yeast-hypha transition is inhibited
D-glucose
-
activates, brings about a global conformational change in H+-ATPase
dithiothreitol
-
2 mM, 26% stimulation
fusicoccin
-
activation of enzyme, treatment additionally leads to 35% increase in phosphorus uptake by roots in low-phosphorus nutrient solution
fusicoccin
Q4VCL8, Q4VCL9, Q4VCM0
-
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
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+
-
markedly increases activity
Phospholipid
-
requires added phospholid for maximal activity
Phospholipid
-
activated by exogenous phospholipids
Phospholipid
-
activated 3fold to 6fold by soybean phospholipids
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
-
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+
Mg-ATP
-
activation of H+-ATPase occurs by the addition of 5 mM Mg-ATP
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
0.3
-
ATP
-
-
0.4
-
ATP
-
mutant M795A, pH 5.7, 30C
0.434
-
ATP
-
wild-type, pH 6.5
0.636
-
ATP
-
wild-type lacking C-terminal 40 amino acids, pH 6.5
0.65
-
ATP
-
pH 6.5, 37C
0.7
-
ATP
-
mutant E803A, pH 5.7, 30C; mutant L797A, pH 5.7, 30C
0.7
-
ATP
-
mutant enzyme E803A, at pH 5.7 and 30C; mutant enzyme L797A, at pH 5.7 and 30C
0.8
-
ATP
-
mutant F808A, pH 5.7, 30C; mutant G793E, pH 5.7, 30C
0.9
-
ATP
-
mutant R811A, pH 5.7, 30C; mutant W805A, pH 5.7, 30C
1
-
ATP
-
wild type enzyme and histidine-tagged enzyme
1.1
-
ATP
-
mutant G793A, pH 5.7, 30C; mutant N792A, pH 5.7, 30C; mutant N792H, pH 5.7, 30C; mutant Q798E, pH 5.7, 30C; mutant T802A, pH 5.7, 30C; mutant T810A, pH 5.7, 30C
1.2
-
ATP
-
mutant N792Q, pH 5.7, 30C
1.24
-
ATP
-
pH 6.5, 37C, Colombia variety
1.26
-
ATP
-
pH 6.5, 37C, Caturra variety
1.3
-
ATP
-
mutant M791A, pH 5.7, 30C; mutant N792D, pH 5.7, 30C
1.4
-
ATP
-
mutant S800A, pH 5.7, 30C; wild-type, pH 5.7, 30C
1.4
-
ATP
-
wild type enzyme, at pH 5.7 and 30C
1.5
-
ATP
-
mutant I809A, pH 5.7, 30C
1.6
-
ATP
-
mutant N804A, pH 5.7, 30C
1.8
-
ATP
-
mutant L806A, pH 5.7, 30C
1.9
-
ATP
-
glucose-starved cells
1.5
-
MgATP2-
-
-
0.05
-
vanadate
-
mutant D617A, pH 6.5, 30C
0.052
-
vanadate
-
mutant D617A/D684N, pH 6.5, 30C
0.056
-
vanadate
-
mutant D684N, pH 6.5, 30C
0.064
-
vanadate
-
wild-type, pH 6.5, 30C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
6
ATP
-
pH 6.8, 25C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01
-
vanadate
-
mutant D617A, pH 6.5, 30C; wild-type, pH 6.5, 30C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0067
-
2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
-
pH 6.5, 30C
-
0.0025
-
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
pH 6.5, 30C
0.003
-
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
pH not specified in the publication, 30C
0.006
-
2-phenyl-1,2-benzisoselenazol-3(2H)-one
-
pH not specified in the publication, 30C
0.004
-
2-phenyl-1,2-benzisoselenazol-3(2H)-one 1-oxide
-
pH 6.5, 30C
-
0.0013
-
vanadate
-
mutant N792D, pH 5.7, 30C
0.0015
-
vanadate
-
mutant M791A, pH 5.7, 30C; mutant N792H, pH 5.7, 30C; mutant N792Q, pH 5.7, 30C; mutant Q798E, pH 5.7, 30C; wild-type, pH 5.7, 30C
0.0018
-
vanadate
-
mutant I809A, pH 5.7, 30C; mutant L797A, pH 5.7, 30C; mutant T802A, pH 5.7, 30C
0.0019
-
vanadate
-
mutant M795A, pH 5.7, 30C
0.002
-
vanadate
-
mutant G793E, pH 5.7, 30C; mutant L806A, pH 5.7, 30C
0.0021
-
vanadate
-
mutant S800A, pH 5.7, 30C; mutant T810A, pH 5.7, 30C
0.0022
-
vanadate
-
mutant N792A, pH 5.7, 30C; mutant R811A, pH 5.7, 30C; mutant W805A, pH 5.7, 30C
0.0026
-
vanadate
-
mutant F808A, pH 5.7, 30C
0.0027
-
vanadate
-
mutant N804A, pH 5.7, 30C
0.0029
-
vanadate
-
mutant G793A, pH 5.7, 30C
0.0042
-
vanadate
-
mutant E803A, pH 5.7, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25.4
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
-
mutants G793A, G793E
5.6
-
-
mutant L797A
5.7
-
-
wild-type, mutants M791A, M795A, S800A, T802A, E803A, N804A, W805A, L806A, F808A, I809A, T810A, R811A, N792D, N792Q, N792H, Q798E
6.3
-
-
wild type enzyme
6.4
-
-
mutants D684N, D617A/D684N
6.5
-
-
-
6.5
-
-
-
6.5
-
-
enzyme from both variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix
6.5
-
Q4VCL8, Q4VCL9, Q4VCM0
at beginning of the light period; at beginning of the light period; at beginning of the light period
6.5
-
-
assay at
6.6
-
-
histidine-tagged enzyme
6.8
-
-
wild-type, mutant D217A
6.8
-
Q4VCL8, Q4VCL9, Q4VCM0
3 hours after light start; 3 hours after light start; 3 hours after light start
6.9
7
-
assay at
7
-
Q4VCL8, Q4VCL9, Q4VCM0
5 hours after light start; 5 hours after light start; 5 hours after light start
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
7
-
about 45% of maximal activity at pH 5.4 and at pH 7.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
enzyme from both variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
Q6WZI6, Q7Z1X2, Q86DE0, -
calculated; calculated
7.3
-
Q6WZI6, Q7Z1X2, Q86DE0, -
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
two plasma membrane H+-ATPase genes are differentially expressed in iron-deficient cucumber plants. CsHA2 transcript is detected both in roots and leaves and is unaffected by Fe
Manually annotated by BRENDA team
-
vacuolar H+-ATPase
Manually annotated by BRENDA team
-
two plasma membrane H+-ATPase genes are differentially expressed in iron-deficient cucumber plants. Enhanced accumulation of CsHA1 gene transcripts in Fe-deficient roots. Supply of iron to deficient plants causes a decrease in the transcript level of CsHA1. CsHA2 transcript is detected both in roots and leaves and is unaffected by Fe
Manually annotated by BRENDA team
-
involvement of plasma membrane H+-ATPase in the adaptation to phosphorus starvation
Manually annotated by BRENDA team
-
plasma membrane H+-ATPase activity is related directly to the amount of enzyme protein and Na+ concentration
Manually annotated by BRENDA team
-
sugar depletion inhibits the association of 14-3-3 regulatory proteins with the enzyme by hampering phosphorylation of the 14-3-3 binding site of the enzyme
Manually annotated by BRENDA team
Q4VCL8, Q4VCL9, Q4VCM0
cluster root; cluster root; cluster root
Manually annotated by BRENDA team
P22180, Q96578, Q9SPD5
-
Manually annotated by BRENDA team
I4DSU9, I4DSV0, I4DSV1, I4DSV3, I4DSV4, I4DSV5, -
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q9Y487
a-subunit
Manually annotated by BRENDA team
B3VBE3
goblet cell apical membrane
Manually annotated by BRENDA team
-
characteristics of phospholipid fatty acid composition of plasma membrane leading to the enhanced ethanol tolerance of the strain, are also efficicious to increase the percentage of activation of plasma membrane ATPase per unit of ethanol
Manually annotated by BRENDA team
-
characteristics of phospholipid fatty acid composition of plasma membrane leading to the enhanced ethanol tolerance of the strain, arew also efficiacious to increase the percentage of activation of plasma membrane ATPase per unit of ethanol
Manually annotated by BRENDA team
-
inside-out vesicles
Manually annotated by BRENDA team
-
specific activity of H+-ATPase increases more than 2fold following cold acclimation. During de-acclimation, decreases in enzyme activity and freezing tolerance are accompanied by decreases in the proportions of oleic and linoloeic acids and increases in the proportions of palmitic and linolenic acids in total glycerolipids
Manually annotated by BRENDA team
-
high enzyme content in the ruffled membrane facing the the bone surface
Manually annotated by BRENDA team
I4DSU9, I4DSV0, I4DSV1, I4DSV3, I4DSV4, I4DSV5, -
-
Manually annotated by BRENDA team
Candida albicans ATCC 96901
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH109
-
;
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae CG1945, Saccharomyces cerevisiae EGY48, Saccharomyces cerevisiae NY13, Saccharomyces cerevisiae SY4
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae SY4
-
-
-
-
Manually annotated by BRENDA team
-
vacuolar H+-ATPase
Manually annotated by BRENDA team
Saccharomyces cerevisiae AH109, Saccharomyces cerevisiae SF838-5A
-
-
-
Manually annotated by BRENDA team
additional information
-
enzyme localization study, overview
-
Manually annotated by BRENDA team
additional information
-
enzyme localization study, overview
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48000
-
Q9Y487
recombinant N-terminal cytosolic tail of V-ATPase a2-subunit isoform a2N1-402, NuPAGE
48500
-
Q9Y487
recombinant N-terminal cytosolic tail of V-ATPase a2-subunit isoform a2N1-402, calculated from amino acid sequence
600000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 96000, SDS-PAGE
?
-
x * 100000, SDS-PAGE
?
-
x * 105000, SDS-PAGE
?
Q0Q5F2
x * 116300, calculated
?
Q6WZI6, Q7Z1X2, Q86DE0, -
x * 100200, calculated; x * 100600, calculated; x * 99500, calculated
?
Q1A4H1
x * 105000, SDS-PAGE
?
-
x * 95000, SDS-PAGE
?
-
x * 66000 + x * 55000 + x * 36000 + x * 18000 + ?, SDS-PAGE. Plant V-ATPase is composed of two subcomplexes: the peripheral V1 complex consisting of eight subunits (VHA-A, -B, -C, -D, -E, -F, -G and -H) responsible for ATP hydrolysis, and the membrane-integral V0 complex consisting of five subunits (VHA-a, -c, -c, -d and -e) responsible for proton translocation
?
A8JP99, B3VDR8, -
x * 120000, SDS-PAGE; x * 120000, SDS-PAGE; x * 120000, SDS-PAGE
?
I4DSU9, I4DSV0, I4DSV1, I4DSV3, I4DSV4, I4DSV5, -
x * 95000, SDS-PAGE; x * 95000, SDS-PAGE; x * 95000, SDS-PAGE; x * 95000, SDS-PAGE
homodimer
-
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
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
activation
phosphoprotein
-
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. H+-ATPase is phosphorylated in vitro on the penultimate threonine in the C-terminus in isolated microsomes from guard cell protoplasts of Vicia faba. Phosphorylated H+-ATPase is dephosphorylated in vitro, dephosphorylation is inhibited by EDTA, but not by calyculin A, an inhibitor of type 1 and 2A protein phosphatases. Dephosphorylation requires Mg2+ but not Ca2+
side-chain modification
-
contains 80 mol of phospholipid per mol of 100000 Da ATPase, 60% phosphatidylcholine, 30% phosphatidylethanolamine, 5% lysophosphatidylcholine
phosphoprotein
A8JP99
phosphothreonine, lower activity after dephosphorylation
phosphoprotein
I4DSU9, I4DSV0, I4DSV1, I4DSV3, I4DSV4, I4DSV5, -
the penultimate threonine-containing H+-ATPase is regulated by phosphorylation of its penultimate threonine in response to light, sucrose, and osmotic shock. Light-induced phosphorylation of the H+-ATPase is regulated by photosynthesis; the penultimate threonine-containing H+-ATPase is regulated by phosphorylation of its penultimate threonine in response to light, sucrose, and osmotic shock. Light-induced phosphorylation of the H+-ATPase is regulated by photosynthesis; the penultimate threonine-containing H+-ATPase is regulated by phosphorylation of its penultimate threonine in response to light, sucrose, and osmotic shock. Light-induced phosphorylation of the H+-ATPase is regulated by photosynthesis; the penultimate threonine-containing H+-ATPase is regulated by phosphorylation of its penultimate threonine in response to light, sucrose, and osmotic shock. Light-induced phosphorylation of the H+-ATPase is regulated by photosynthesis
phosphoprotein
-
activation
phosphoprotein
-
in carbon-starved cells with low enzymic activity, enzyme is singly phosphorylated at residue T512. In glucose-metabolizing cells with high ATPase activity, enzyme is doubly phosphorylated at S911 and T912
phosphoprotein
-
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. H+-ATPase is phosphorylated in vitro on the penultimate threonine in the C-terminus in isolated microsomes from guard cell protoplasts of Vicia faba. Phosphorylated H+-ATPase is dephosphorylated in vitro, dephosphorylation is inhibited by EDTA, but not by calyculin A, an inhibitor of type 1 and 2A protein phosphatases. Dephosphorylation requires Mg2+ but not Ca2+
phosphoprotein
-
sugar depletion inhibits the association of 14-3-3 regulatory proteins with the enzyme by hampering phosphorylation of the 14-3-3 binding site of the enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
two-dimensional crystallization of the reconstituted enzyme
-
dodecylmaltoside complex
-
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
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NDSB-256 is required not only during protein refolding but also afterward for stabilization of a2N1-402 protein in the solution
Q9Y487
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni2+-affinity chromatography
-
Talon bead chromatography, HisTrap column chromatography, and Superdex 200 gel filtration
Q9Y487
large-scale purification
-
enzyme fused to glutathione S-transferase, expressed in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
AHA2, overexpression in Saccharomyces cerevisiae
-
expression in Arabidopsis thaliana
-
subunit a2N1-402 is expressed in Escherichia coli BL21(DE3) cells
Q9Y487
expression in Saccharomyces cerevisiae
-
expression in Nicotiana tabacum, either wild-type gene or gene lacking the C-terminal 103 residues corresponding to the autoinhibitory domain
-
expression in Saccharomyces cerevisiae
-
cloning of pma-1-A135V revertant alleles
-
enzyme fused to glutathione S-transferase, expressed in Escherichia coli
-
expressed in Saccharomyces cerevisiae NY13 cells
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
P22180, Q96578, Q9SPD5
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the active H+ flux is decreased to 60% when 100 mM K+ are substituted by 100 mM Na+
-
plasma membrane H+-ATPase hydrolytic and pumping activities are not affected by application of 150 mM NaCl
-
at 25 mM Na+ concentration, hydrolytic activity is not affected (reduction in active H+ flux is 5%)
-
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
B3VBE3
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
A8JP99, B3VDR8, -
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
A8JP99, B3VDR8, -
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
Saccharomyces cerevisiae SF838-5A
-
-
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
P22180, Q96578, Q9SPD5
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+
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D617A
-
35% increase in catalytic activity
D617A/D684N
-
22% of wild-type activity, insensitive 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
-
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
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
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
-
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
T931A/S938A
-
phosphorylation sites
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
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
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
F808A
-
83% of wild-type activity
G793A
-
38% of wild-type activity
G793E
-
36% of wild-type activity
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
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
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
L806A
-
120% of wild-type activity
M791A
-
49% of wild-type activity
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
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
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
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
F796A
Saccharomyces cerevisiae SY4
-
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
Saccharomyces cerevisiae SY4
-
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
Saccharomyces cerevisiae SY4
-
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
Saccharomyces cerevisiae SY4
-
20% ATPase and 17% H+ transport activity compared to the wild type enzyme
-
D684N
-
24% of wild-type activity, insensitve to vanadate
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
T931D
-
phosphorylation site
additional information
-
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
Q0Q5F2
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
M795A
-
45% of wild-type activity
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
Q798A
Saccharomyces cerevisiae SY4
-
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
-
additional information
Q6WZI6, Q7Z1X2, Q86DE0, -
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; 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; 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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
best refolding conditions are 1 M NDSB-256, 1 mM dithiothreitol, 100 mM CHES, and pH 9.0
Q9Y487
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
treatment of coffee variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix, with soluble fraction of Hemileia vastatrix urediospores induces specific inhibition of resistant variety's Colombia H+-ATPase and proton pump activities
drug development
-
the enzyme is a target for development of specific inhibitors
nutrition
-
in wine yeast strains, ergosterol, oleic acid and palmitoleic acid contents in plasma membrane are highly correlated with ATPase activity and ethanol tolerance. Saccharomyces cerevisiae var. capensis flor yeast strain exhibits the highest ergosterol concentration in plasma membrane when grown in 4% ethanol and is the most ethanol-tolerant
drug development
-
the enzyme is a target for development of specific inhibitors
-
agriculture
-
addition of magnesium to toxic aluminium treatment helps maintain the tissue magnesium content and the activity of the plasma membrane H+-ATPase. These changes enhance the aluminium-dependent efflux of vitrate which provides extra protection from aluminium stress