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Information on EC 7.1.3.1 - H+-exporting diphosphatase
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7.1.3.1 H+-exporting diphosphataseIUBMB Comments
This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
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Word Map
- 7.1.3.1
- vacuole
- h+-ppases
-
tonoplasts
- acidocalcisomes
- v-atpase
- ppases
- pyrophosphatases
- imidodiphosphate
-
3.6.1.1
- v-h+-atpase
- aminomethylenediphosphonate
-
h+-pumping
-
ppi-dependent
- medicine
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
h(+)-pyrophosphatase, vacuolar h+ -atpase, proton pyrophosphatase, vacuolar h+-ppase, v-h+-ppase, h+ -ppase, proton pumping pyrophosphatase, proton-pumping pyrophosphatase, proton-pyrophosphatase, vp1-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acidocalcisomal pyrophosphatase
AVP1
H(+)-pyrophosphatase
H+-inorganic pyrophosphatase
H+-PPase
H+-pyrophosphatase
H+-translocating inorganic pyrophosphatase
hydrogen-translocating pyrophosphatase
inorganic pyrophosphatase
membrane-bound proton-translocating pyrophosphatase
PPase
PPi-energized H+-PPase
proton-pumping dihosphatase
proton-pumping inorganic pyrophosphatase
proton-pumping pyrophosphatase
proton-pyrophosphatase
-
electrogenic proton-pump that couples diphosphate hydrolysis to the active transport of protons across membranes
proton-translocating inorganic pyrophosphatase
Pyrophosphate-energized inorganic pyrophosphatase
pyrophosphate-energized proton pump
soluble pyrophosphatase
tonoplast H+-PPase
V-PPase
vacuolar H+-pyrophosphatase
vacuolar H+-translocating inorganic pyrophosphatase
vacuolar pyrophosphatase
VHP1
VP1
VSP1
H(+)-pyrophosphatase
Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
-
-
-
H+-PPase
-
-
ambiguous
-
H+-PPase
Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
-
-
-
hydrogen-translocating pyrophosphatase
-
-
-
-
proton-pumping dihosphatase
-
-
-
-
proton-pumping inorganic pyrophosphatase
-
-
proton-pumping pyrophosphatase
-
-
-
-
vacuolar H+-pyrophosphatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphosphate + H2O + H+[side 1] = 2 phosphate + H+[side 2]
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase (H+-transporting)
This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Mg(H2O)4-thiodiphosphate + H2O + H+[side 1]
?
-
17% activity compared to Mg(H2O)4-diphosphate
-
-
?
tripolyphosphate + H2O
?
hydrolyzed only in the presence of Zn2+
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
Mg2+ is absolutely required for determination of substrate specificity
-
-
?
diphosphate + H2O
2 phosphate
Mg2+ is absolutely required for determination of substrate specificity
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions, essential for growth of bloodstream forms in mammalian host
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
V-PPase, localized in plant vacuolar membranes, translocates H+ into the vacuoles in conjunction with the vacuolar H+-ATPase, VATPase, EC 3.6.1.3, regulation, overview
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
the enzyme and its proton pumping activity have important roles in the accumulation of sugars in vacuoles, the enzyme expression is regulated by phytohormones in a complex manner
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
r
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
-
r
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
-
-
-
-
r
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
-
r
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation from cytosol to vacuole lumen
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, reaction coupled with proton pumping through the vacuole membrane
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
polyphosphate + H2O
?
polyphosphate of 28 residues, hydrolyzed only in the presence of Zn2+, central role in the regulation of polyphosphate metabolism, supports recovery from hypoosmotic stress
-
-
?
polyphosphate + H2O
?
polyphosphate of 28 residues, poor substrate, hydrolyzed only in the presence of Zn2+
-
-
?
polyphosphate-n28 + H2O
?
chain length of 28 phosphates
-
-
?
additional information
?
-
proton-translocation activities are assayed by monitoring the fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine
-
-
?
additional information
?
-
-
proton-translocation activities are assayed by monitoring the fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine
-
-
?
additional information
?
-
-
the enzyme acts as diphosphate-dependent H+-translocation pump, the organism regulates the intracellular distribution of H+ and Ca2+ in the plant host cell, mechanism
-
-
?
additional information
?
-
-
the enzyme acts as diphosphate-dependent H+-translocation pump dependent on K+ in acidic vacuoles
-
-
?
additional information
?
-
-
the hormones abscisic acid, auxin, and 2,4-dinitrophenol are responsible for regulation of the inorganic pyrophosphatase enzyme activity, overview
-
-
?
additional information
?
-
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
?
additional information
?
-
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
?
additional information
?
-
Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
-
the enzyme is a membrane H+-pump
-
-
?
additional information
?
-
-
the enzyme is unable to catalyze the hydrolysis of Mg(H2O)4-imidodiphosphate and Co(NH3)4-imidodiphosphate
-
-
?
additional information
?
-
-
trimetaphosphate and tripolyphosphate are hydrolyzed with 2% of the rate with diphosphate, no other phosphorylated compounds are hydrolyzed
-
-
?
additional information
?
-
-
the enzyme also shows H+-translocation activity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
polyphosphate + H2O
?
polyphosphate of 28 residues, hydrolyzed only in the presence of Zn2+, central role in the regulation of polyphosphate metabolism, supports recovery from hypoosmotic stress
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions, essential for growth of bloodstream forms in mammalian host
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
V-PPase, localized in plant vacuolar membranes, translocates H+ into the vacuoles in conjunction with the vacuolar H+-ATPase, VATPase, EC 3.6.1.3, regulation, overview
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
the enzyme and its proton pumping activity have important roles in the accumulation of sugars in vacuoles, the enzyme expression is regulated by phytohormones in a complex manner
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
-
r
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
-
r
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation from cytosol to vacuole lumen
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, reaction coupled with proton pumping through the vacuole membrane
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
additional information
?
-
-
the enzyme acts as diphosphate-dependent H+-translocation pump, the organism regulates the intracellular distribution of H+ and Ca2+ in the plant host cell, mechanism
-
-
?
additional information
?
-
-
the hormones abscisic acid, auxin, and 2,4-dinitrophenol are responsible for regulation of the inorganic pyrophosphatase enzyme activity, overview
-
-
?
additional information
?
-
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
?
additional information
?
-
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Na+
Rb+
Zn2+
additional information
K+
-
the enzyme is most stimulated by K+. KCl and K2SO4 support similar rates of diphosphate hydrolysis and diphosphate-dependent proton translocation
K+
-
enzyme activity is maximal in the presence of K+ (K50 approximately 3 mM)
Mg2+
required, highest activity at 5 mM, decrease of activity at higher concentrations
Mg2+
-
the enzyme has a requirement for a Mg/diphosphate complex as substrate and free Mg2+ for activation. Half-maximal enzyme activity occurs at free 1.1 mM Mg2+
Mg2+
VSP1 is dependent on divalent cations Mg2+ or Zn2+, Mg2+ is absolutely required for determination of substrate specificity and cannot be substituted by other metal ions
Mg2+
-
dependent on, maximum activity is obtained in the presence of 5 mM Mg2+, no diphosphate hydrolysis is detected in the absence of Mg2+
Mg2+
-
required, the ER H+-pyrophosphatase requires higher concentrations as the vacuolar H+-pyrophosphatase
Na+
-
NaCl has a small stimulatory effect (139% compared to the control) on diphosphate hydrolysis and diphosphate-dependent proton translocation
Zn2+
required for the hydrolysis of tripolyphosphate and polyphosphate
additional information
-
other metal ions can partially replace Mg2+, activation decreases in the order Mg2+, Co2+, Cu2+, Fe2+, Zn2+, Mn2+
additional information
-
Co2+ and Ca2+ have no stimulatory effect on the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Imidodiphosphate
-
when diphosphate concentration in the medium is adjusted to 0.05 mM, the enzyme is totally inhibited by 0.5 mM imidodiphosphate, the same concentration of imidodiphosphate only decreases the enzyme activity by 70% and 50% when diphosphate concentration in the medium is increased to 0.15 mM and 0.3 mM, respectively
additional information
-
nitrate (50 mM), molybdate (0.5 mM), and azide (2 mM) have essentially no effect on the enzyme reaction
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dinitrophenol
-
2,4-dinitrophenol increases the expression of HVP1, treatment with abscisic acid and 2,4-dinitrophenol increases Na+/H+ antiport activity and proton translocating activities by H+-PPase and H+-ATPase in tonoplast vesicles, and treatment with abscisic acid also increases the amount of V-PPase protein of tonoplast vesicles, overview
abscisic acid
-
abscisic acid markedly induces the expression of HVP1 and slightly increased the expression of HVP10, treatment with abscisic acid and 2,4-dinitrophenol increases Na+/H+ antiport activity and proton translocating activities by H+-PPase and H+-ATPase in tonoplast vesicles, and treatment with abscisic acid also increases the amount of V-PPase protein of tonoplast vesicles, overview
gibberellic acid
-
phytohormone gibberellic acid increases V-PPase expression and activity by 20%
Phospholipid
-
the enzyme reaction is stimulated by exogenous phospholipid in the presence of detergent
additional information
-
HVP1 transcripts also increase 5 h after treatment with another synthetic auxin, 1-naphthaleneacetic acid, and native auxin, 3-indoleacetic acid, while the level of HVP10 transcript does not increase after treatment with the two auxins, no effect on gene expression by gibberellic acid, salt stress increases the levels of HVP and HVP10 transcripts in the roots of barley seedlings, osmotic stress also increases the levels of HVP1 transcripts in the roots
-
additional information
-
phytohormones indole acetic acid and 6-benzyladenine increase V-PPase expression, but not the enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Presence of serum autoantibodies to vacuolar H+ -ATPase in patients with renal tubular acidosis.
Acidosis
Vacuolar H+ -ATPase B1 subunit mutations that cause inherited distal renal tubular acidosis affect proton pump assembly and trafficking in inner medullary collecting duct cells.
Acidosis, Renal Tubular
Presence of serum autoantibodies to vacuolar H+ -ATPase in patients with renal tubular acidosis.
Acidosis, Renal Tubular
Vacuolar H+ -ATPase B1 subunit mutations that cause inherited distal renal tubular acidosis affect proton pump assembly and trafficking in inner medullary collecting duct cells.
African Horse Sickness
African horse sickness virus serotype 4 antigens, VP1-1, VP2-2, VP4, VP7 and NS3, induce cytotoxic T cell responses in vitro.
Glioma
Protective effects of vacuolar H+ -ATPase c on hydrogen peroxide-induced cell death in C6 glioma cells.
Granular Cell Tumor
Frequent mutations of genes encoding vacuolar H+ -ATPase components in granular cell tumors.
Neoplasms
Frequent mutations of genes encoding vacuolar H+ -ATPase components in granular cell tumors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
the structural orientation of Lys78 is very important for the kinetic properties of the enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
Ca2+
hydrolysis of diphosphate, pH 7.5, 25°C, no inhibition of tripolyphosphate and polyphosphate hydrolysis
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
calculated from predicted amino acid sequence and detected in isoelectric focusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a deep-subsurface alpha-proteobacterium isolated from North Atlantic coastal sediments
-
-
brenda
soluble and membrane bound form present in anaerobic phototrophic batch cultures, only soluble and no membrane bound form present in aerobic, dark grown cultures, highest level of membrane bound form in aerobic cultures grown under acute salt stress (1 M NaCl)
SwissProt
brenda
soluble and membrane bound form present in anaerobic phototrophic batch cultures, only soluble and no membrane bound form present in aerobic, dark grown cultures, highest level of membrane bound form in aerobic cultures grown under acute salt stress (1 M NaCl)
SwissProt
brenda
vacuolar-type proton translocating pyrophosphatase 1 precursor
SwissProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression pattern analysis in endosperm and in situ hydridization
brenda
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
endoplasmic reticulum-enriched vesicles, ER H+-pyrophosphatase
-
brenda
vesicular acidic compartment, VSP1 occurs in metacyclic forms
brenda
-
vesicular acidic compartment, VSP1 occurs in metacyclic forms
-
brenda
-
commonly present in membranes of acidocalcisomes
brenda
-
polyphosphate-rich, predominant location, co-localization of the H+-PPase with diphosphate and short and long chain polyphosphates, light-dependent, overview
brenda
Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
-
polyphosphate-rich, predominant location, co-localization of the H+-PPase with diphosphate and short and long chain polyphosphates, light-dependent, overview
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
implication of H+-PPase in postgerminative oilseed metabolism, overview
physiological function
additional information
malfunction
-
defects in PPase activity cause severe developmental defects and/or growth arrest in several organisms. The fugu5 mutant phenotype, caused by a defect in H+-PPase activity, shows a postgerminative growth phenotype, but is rescued by complementation with the yeast cytosolic PPase IPP1, overview. Increased cytosolic PPi levels Impaired postgerminative development in fugu5 by inhibiting gluconeogenesis
malfunction
the fugu5 mutant is defective in AVP1, i.e. vacuolar H+-pyrophosphatase, due to point mutations A709T, A553T, or E272K, and fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic diphosphatase1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
physiological function
-
proton-translocating vacuolar PPase, H+-PPase, uses the energy of diphosphate hydrolysis to acidify the vacuole in higher plants. H+-PPase is a master regulator of cytosolic diphosphate homeostasis, another role of H+-PPase in plants is vacuolar acidification, the role of H+-PPase as a proton-pump is negligible
physiological function
vacuolar H+ -ATPases are a specific class of multisubunit pumps that play an essential role in the generation of proton gradients across eukaryotic endomembranes. The plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance when recombinantly expressed in yeast
physiological function
vacuolar H+-diphosphatase, AVP1, is a key enzyme in phosphate hydrolysis
physiological function
-
a co-ordinated action of the enzyme with H+-ATPase at the tonoplast can allow a higher transport capacity at the vacuolar membrane when plants perform high crassulacean acid metabolism
physiological function
-
co-expression of the enzyme and a vacuolar Na+/H+ antiporter gene from Pennisetum glaucum confers enhanced salt tolerance to the transformed tomato compared with the single gene transgenic plants and the wild type. Co-expression of the enzymes improves the osmoregulatory capacity of double transgenic lines by enhanced sequestration of ions into the vacuole by increasing the availability of protons and thus alleviating the toxic effect of Na+
physiological function
-
compared with wild type plants, transgenic alfalfa plants, co-expressing the enzyme and tonoplast cation/H+ antiporter, grow better with greater plant height and dry mass under normal or stress conditions (NaCl or water-deficit) in the greenhouse. Furthermore, the transgenic alfalfa co-expressing both enzymes also grow faster than wild type plants under field conditions and exhibit enhanced photosynthesis capacity by maintaining higher net photosynthetic rate, stomatal conductance, and water-use efficiency than wild type plants
physiological function
enzyme overexpression confers enhanced tolerance to abiotic stresses, including heat shock and H2O2, as well as NaCl, Cd, Mn, Zn, Ca, and Al. Enzyme overexpression results in hypersensitivity to menadione and cobalt
physiological function
enzyme overexpression confers enhanced tolerance to abiotic stresses, including heat shock and H2O2, as well as NaCl, Cd, Mn, Zn, Ca, and Al. Enzyme overexpression results in hypersensitivity to menadione and cobalt
physiological function
-
enzyme overexpression in transgenic finger millet enhances the plant's performance under salt stress
physiological function
enzyme overexpression leads to higher vacuolar proton currents and vacuolar acidification. After 3 d in salt-untreated conditions, enzyme-overexpressing leaves show a drop in photosynthetic capacity, plasma membrane depolarization and eventual leaf necrosis. Salt, however, rescues enzyme-hyperactive cells from cell death. Under normal growth conditions, plants need to regulate the enzyme activity to avoid hyperactivity and its negative feedback on cell viability
physiological function
-
enzyme overexpression markedly stimulates growth and increase stolerance to biotic and abiotic stresses
physiological function
-
enzyme overexpression markedly stimulates growth and increases tolerance to biotic and abiotic stresses
physiological function
-
enzyme overexpression mediates enhanced phloem loading and long-distance transport leading to growth enhancement
physiological function
-
enzyme-expressing transgenic tobacco plants are more tolerant to cadmium compared to wild type plants
physiological function
-
heterologous expression of the enzyme at the fungal vacuolar membrane alleviates growth inhibition by tridemorph, reduces apoptosis levels in yeast and increases resistance to amine fungicides
physiological function
-
the ancillary enzyme maintains the proton-motive force across the vacuolar membrane when the activity of the tonoplast H+-ATPase is restricted by substrate availability
physiological function
-
the enzyme can reduce Na+ toxicity in plant cells through increased sequestration of ions into vacuoles by enhanced enzyme activity
physiological function
-
the enzyme catalyzes a coupled reaction of diphosphate hydrolysis and active proton translocation across the tonoplast. Additional enzyme expression improves plant growth by increasing cell number, predominantly as a consequence of the diphosphate hydrolyzing activity of the enzyme
physiological function
-
the enzyme facilitates vacuolar K+ accumulation in vivo
physiological function
-
the enzyme is required for pyrophosphate metabolism and photosynthate partitioning in phloem function
physiological function
-
the enzyme is responsible for generating an internal acidic environment in the vacuole and a proton gradient across the membrane
physiological function
-
the enzyme regulates root and shoot development via facilitation of auxin flux, and enhances plant resistance to salt and drought stresses. Perennial creeping bentgrass plants over-expressing the enzyme exhibit improved resistance to salinity (100-300 mM naCl) than wild type controls
physiological function
-
the enzyme transports protons into the vacuole and polarizes the membrane potential (positive inside the vacuole). The electrochemical gradient provided by the enzyme stimulates effectively the uptake of various metabolites such as malate, citrate and sucrose
additional information
vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane
additional information
-
vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38770
calculated from the predicted amino acid sequence after removal of the signal peptide
60000
73000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
-
composed of two trimers, hexameric form required for full activity and thermostability, gel filtration
homodimer
additional information
additional information
VSP1 is preferably expressed in metacyclic forms
additional information
-
VSP1 is preferably expressed in metacyclic forms
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation or poly-phosphorylation at S46, S47, S48, K55, Y61, T129, Y130, Y170, T576, T618, T633, and Y700
proteolytic modification
vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A553T
naturally occuring point mutation A553T plus deletion of residues from Leu554 to Ala558 in the transmembrane domain 12. The mutant fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
A709T
the naturally occuring fugu5 mutant is defective in AVP1, i.e. vacuolar H+-pyrophosphatase, due to a point mutation A709T and fails to support heterotrophic growth after germination. Cell division is almost totally inhibited in cotyledons postembryonically, phenotype, overview, fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
E272K
naturally occuring point mutation, fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
P14A
-
large decrease in activity, formation of trimers during heat treatment
P43A
-
large decrease in activity, formation of trimers during heat treatment
D217A
-
almost complete loss of hydrolytic and proton translocation activity
D217E
-
almost complete loss of hydrolytic and proton translocation activity
D428N
-
almost complete loss of hydrolytic and proton translocation activity
E231D
-
almost complete loss of hydrolytic and proton translocation activity
E231Q
-
almost complete loss of hydrolytic and proton translocation activity
E384D
-
10% of hydrolytic activity, 35% of proton translocating activity, increased tolerance to high salt concentrations
K469A
-
almost complete loss of hydrolytic and proton translocation activity
K469D
-
almost complete loss of hydrolytic and proton translocation activity
K469R
-
almost complete loss of hydrolytic and proton translocation activity
R176A
-
almost complete loss of hydrolytic and proton translocation activity
R176K
-
50% of hydrolytic activity, 20% of proton translocating activity, increased tolerance to high salt concentrations
D325E
D204H/R206L
-
90% loss in proton translocating but only 50% loss in hydrolytic activity
D217A
-
almost complete loss of hydrolytic and proton translocating activity, less Mg2+ required for activity
D217H
-
almost complete loss of hydrolytic and proton translocating activity, less Mg2+ required for activity
H469R
-
almost complete loss of hydrolytic and proton translocating activity
E263D
K261R
V259A
additional information
D325E
site-directed mutagenesis, inactive mutant, the dominant negative mutant shows the requirement of Leishmania VSP1 functional expression for metacyclogenesis and virulence in mice, overview
D325E
-
site-directed mutagenesis, inactive mutant, the dominant negative mutant shows the requirement of Leishmania VSP1 functional expression for metacyclogenesis and virulence in mice, overview
-
additional information
expression of a chimaeric derivative of the Arabidopsis thaliana H+ -PPase AVP1, which is preferentially targeted to internal membranes of yeast, alleviates the phenotypes associated with V-ATPase deficiency. Phenotypic complementation was achieved both with a yeast strain with its V-ATPase specifically inhibited by bafilomycin A1 and with a vma1-null mutant lacking a catalytic V-ATPase subunit. Cells expressing the different AVP1 chimaeras show a somewhat smaller sensitivity to this CaCl2. In the presence of Zn2+ , only those cells transformed with plasmids pTcAVP1 and pTcGFPAVP1 expressing internal membrane-targeted chimaeras grows after 4 days, particularly the latter. Phenotypes, overview. In yeast strain YPC4, the presence of GFP at the N-terminus of AVP1 increased the specific activity of the resulting protein 3-4-fold with respect to AVP1 and TcAVP1
additional information
-
expression of a chimaeric derivative of the Arabidopsis thaliana H+ -PPase AVP1, which is preferentially targeted to internal membranes of yeast, alleviates the phenotypes associated with V-ATPase deficiency. Phenotypic complementation was achieved both with a yeast strain with its V-ATPase specifically inhibited by bafilomycin A1 and with a vma1-null mutant lacking a catalytic V-ATPase subunit. Cells expressing the different AVP1 chimaeras show a somewhat smaller sensitivity to this CaCl2. In the presence of Zn2+ , only those cells transformed with plasmids pTcAVP1 and pTcGFPAVP1 expressing internal membrane-targeted chimaeras grows after 4 days, particularly the latter. Phenotypes, overview. In yeast strain YPC4, the presence of GFP at the N-terminus of AVP1 increased the specific activity of the resulting protein 3-4-fold with respect to AVP1 and TcAVP1
additional information
mutant Dap3 is characterised by the appearance of colourless patches on otherwise fully coloured, purple kernels due to the presence of an abnormal aleurone layer, Vpp1 is expressed in colourless patches of Dap3 mutant kernels, expression in mutant strains compared to wild-type A188, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mg2+/diphosphate protects against inhibition by all inhibitors in the study
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE Sephacel column chromatography, and Sephacryl S400HR gel filtration
-
Mono Q column chromatography and Sephacryl S400 gel filtration
partially by purification of acidocalcisomes using iodixanol gradients
-
recombinant protein using His-tag
recombinant wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
solubilization with lysophosphatidylcholine and QAE-Toyopearl column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
DNA and amino acid seuqnece determination and analysis, expression profile in maize plants, overview
expressed in Escherichia coli BL21 (DE3) cells and Saccharomyces cerevisiae BY4741 cells
expressed in Escherichia coli C43(DE3)
expressed in Populusr davidiana x Populus bolleana and in an Arabidopsis thaliana knock out mutant of vacuolar H+-pyrophosphatase AVP1
-
expression of AVP1, preferentially targeted to internal membranes, in Saccharomyces cerevisiae YPC3 mutant strain, generated from haploid strain W303-1A, and YPC4 mutant strain, generated from strain RS-1144
gene hppA, DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
gene VSP1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli, overexpression of wild-type and mutant enzymes in Leishmania amazonensis
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
expressed in Escherichia coli BL21 (DE3) cells and Saccharomyces cerevisiae BY4741 cells
expressed in Escherichia coli BL21 (DE3) cells and Saccharomyces cerevisiae BY4741 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is up-regulated by salt stress (200 mM NaCl treatment for 24 h)
-
the highest mRNA level of all isoforms VP1, VP2, and VP3 are observed at 2-4 days in fruit after anthesis
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
VSP1 enzyme an attractive drug target against trypanosomatid parasites
drug development
-
VSP1 enzyme an attractive drug target against trypanosomatid parasites
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Leigh, R.A.; Kaestner, K.H.; Sze, H.
Electrogenic H+-pumping pyrophosphatase in tonoplast vesicles of oat roots
Plant Physiol.
81
497-502
1986
Avena sativa
brenda
Maeshima, M.
H+-translocating inorganic pyrophosphatase of plant vacuoles. Inhibition by Ca2+, stabilization by Mg2+ and immunological comparison with other inorganic pyrophosphatases
Eur. J. Biochem.
196
11-17
1991
Vigna radiata
brenda
Gordon-Weeks, R.; Steele, S.H.; Leigh, R.A.
The role of magnesium, pyrophosphate, and their complexes as substrates and activators of the vacuolar H+-pumping inorganic pyrophosphatase
Plant Physiol.
111
195-202
1996
Beta vulgaris, Vigna radiata
brenda
Lerchl, J.; Konig, S.; Zrenner, R.; Sonnewald, U.
Molecular cloning, characterization and expression analysis of isoforms encoding tonoplast-bound proton-translocating inorganic pyrophosphatase in tobacco
Plant Mol. Biol.
29
833-840
1995
Nicotiana tabacum
brenda
Hemalatha, K.P.; Prasad, D.S.
Purification, physicochemical properties, and subcellular location of alkaline inorganic pyrophosphatase from sesame (Sesamum indicum L.) cotyledons
Biochem. Cell Biol.
80
215-224
2002
Sesamum indicum
brenda
Schultz, A.; Baltscheffsky, M.
Properties of mutated Rhodospirillum rubrum H+-pyrophosphatase expressed in Escherichia coli
Biochim. Biophys. Acta
1607
141-151
2003
Escherichia coli
brenda
Schultz, A.; Baltscheffsky, M.
Inhibition studies on Rhodospirillum rubrum H(+)-pyrophosphatase expressed in Escherichia coli
Biochim. Biophys. Acta
1656
156-165
2004
Rhodospirillum rubrum
brenda
Yang, S.J.; Jiang, S.S.; Hsiao, Y.Y.; Van, R.C.; Pan, Y.J.; Pan, R.L.
Thermoinactivation analysis of vacuolar H(+)-pyrophosphatase
Biochim. Biophys. Acta
1656
88-95
2004
Vigna radiata
brenda
Islam, M.K.; Miyoshi, T.; Kasuga-Aoki, H.; Isobe, T.; Arakawa, T.; Matsumoto, Y.; Tsuji, N.
Inorganic pyrophosphatase in the roundworm Ascaris and its role in the development and molting process of the larval stage parasites
Eur. J. Biochem.
270
2814-2826
2003
Ascaris lumbricoides, Toxocara canis, Ascaris suum (Q86M43)
brenda
McIntosh, M.T.; Vaidya, A.B.
Vacuolar type H+ pumping pyrophosphatases of parasitic protozoa
Int. J. Parasitol.
32
1-14
2002
Arabidopsis thaliana, Vigna radiata, Plasmodium falciparum, Pyrobaculum aerophilum, Rhodospirillum rubrum, Thermotoga maritima, Toxoplasma gondii, Trypanosoma cruzi, Zea mays
brenda
Lopez-Marques, R.L.; Perez-Castineira, J.R.; Losada, M.; Serrano, A.
Differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics
J. Bacteriol.
186
5418-5426
2004
Rhodospirillum rubrum (O68460), Rhodospirillum rubrum S1 (O68460)
brenda
Masuda, H.; Uchiumi, T.; Wada, M.; Ichiba, T.; Hachimori, A.
Effects of replacement of prolines with alanines on the catalytic activity and thermostability of inorganic pyrophosphatase from thermophilic bacterium PS-3
J. Biochem.
131
53-58
2002
Bacillus sp. PS3
brenda
Nakanishi, Y.; Saijo, T.; Wada, Y.; Maeshima, M.
Mutagenic analysis of functional residues in putative substrate-binding site and acidic domains of vacuolar H+-pyrophosphatase
J. Biol. Chem.
276
7654-7660
2001
Vigna radiata
brenda
Drozdowicz, Y.M.; Shaw, M.; Nishi, M.; Striepen, B.; Liwinski, H.A.; Roos, D.S.; Rea, P.A.
Isolation and characterization of TgVP1, a type I vacuolar H+-translocating pyrophosphatase from Toxoplasma gondii. The dynamics of subcellular localization and the cellular effects of a diphosphonate inhibitor
J. Biol. Chem.
278
1075-1085
2003
Toxoplasma gondii (Q9BK08), Toxoplasma gondii, Toxoplasma gondii RH (Q9BK08)
brenda
Lemercier, G.; Espiau, B.; Ruiz, F.A.; Vieira, M.; Luo, S.; Baltz, T.; Docampo, R.; Bakalara, N.
A pyrophosphatase regulating polyphosphate metabolism in acidocalcisomes is essential for Trypanosoma brucei virulence in mice
J. Biol. Chem.
279
3420-3425
2004
Trypanosoma brucei (Q7Z029)
brenda
Islam, K.M.; Miyoshi, T.; Isobe, T.; Kasuga-Aoki, H.; Arakawa, T.; Matsumoto, Y.; Yokomizo, Y.; Tsuji, N.
Temperature and metal ions-dependent activity of the family I inorganic pyrophosphatase from the swine roundworm Ascaris suum
J. Vet. Med. Sci.
66
221-223
2004
Ascaris suum
brenda
Serrano, A.; Perez-Castineira, J.R.; Baltscheffsky, H.; Baltscheffsky, M.
Proton-pumping inorganic pyrophosphatases in some archaea and other extremophilic prokaryotes
J. Bioenerg. Biomembr.
36
127-133
2004
Chlorobaculum tepidum, Chloroflexus aurantiacus, Novosphingobium aromaticivorans, Thermobifida fusca, Caldanaerobacter subterraneus subsp. tengcongensis, Rhodospirillum rubrum (O68460), Arabidopsis thaliana (P31414), Arabidopsis thaliana (Q56ZN6), Pyrobaculum aerophilum (Q8ZWI8), Trypanosoma cruzi (Q9NDF0), Thermotoga maritima (Q9S5X0), Streptomyces coelicolor (Q9X913)
brenda
Seufferheld, M.; Lea, C.R.; Vieira, M.; Oldfield, E.; Docampo, R.
The H(+)-pyrophosphatase of Rhodospirillum rubrum is predominantly located in polyphosphate-rich acidocalcisomes
J. Biol. Chem.
279
51193-51202
2004
Rhodospirillum rubrum, Rhodospirillum rubrum Esmarch / Molisch / ATCC 17031
brenda
Espiau, B.; Lemercier, G.; Ambit, A.; Bringaud, F.; Merlin, G.; Baltz, T.; Bakalara, N.
A soluble pyrophosphatase, a key enzyme for polyphosphate metabolism in Leishmania
J. Biol. Chem.
281
1516-1523
2006
Leishmania amazonensis (Q7Z031), Leishmania amazonensis MHOM/BR/1987/BA125 (Q7Z031)
brenda
Amemiya, T.; Kawai, Y.; Yamaki, S.; Shiratake, K.
Enhancement of vacuolar H+-ATPase and H+-pyrophosphatase expression by phytohormones in pear fruit
J. Jpn. Soc. Horticult. Sci.
74
353-360
2005
Pyrus communis
-
brenda
Kuo, S.Y.; Chien, L.F.; Hsiao, Y.Y.; Van Ru, C.; Yan, K.H.; Liu, P.F.; Mao, S.J.; Pan, R.L.
Proton pumping inorganic pyrophosphatase of endoplasmic reticulum-enriched vesicles from etiolated mung bean seedlings
J. Plant Physiol.
162
129-138
2005
Vigna radiata
brenda
Soares Medeiros, L.C.; Moreira, B.L.; Miranda, K.; de Souza, W.; Plattner, H.; Hentschel, J.; Barrabin, H.
A proton pumping pyrophosphatase in acidocalcisomes of Herpetomonas sp.
Mol. Biochem. Parasitol.
140
175-182
2005
Herpetomonas sp.
brenda
Wisniewski, J.P.; Rogowsky, P.M.
Vacuolar H+-translocating inorganic pyrophosphatase (Vpp1) marks partial aleurone cell fate in cereal endosperm development
Plant Mol. Biol.
56
325-337
2004
Zea mays (Q41758)
brenda
Fukuda, A.; Tanaka, Y.
Effects of ABA, auxin, and gibberellin on the expression of genes for vacuolar H+ -inorganic pyrophosphatase, H+ -ATPase subunit A, and Na+/H+ antiporter in barley
Plant Physiol. Biochem.
44
351-358
2006
Hordeum vulgare
brenda
Motta, L.S.; Ramos, I.B.; Gomes, F.M.; de Souza, W.; Champagne, D.E.; Santiago, M.F.; Docampo, R.; Miranda, K.; Machado, E.A.
Proton-pyrophosphatase and polyphosphate in acidocalcisome-like vesicles from oocytes and eggs of Periplaneta americana
Insect Biochem. Mol. Biol.
39
198-206
2009
Periplaneta americana
brenda
Perez-Castineira, J.R.; Hernandez, A.; Drake, R.; Serrano, A.
A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast
Biochem. J.
437
269-278
2011
Arabidopsis thaliana (P31414), Arabidopsis thaliana
brenda
Ferjani, A.; Segami, S.; Horiguchi, G.; Muto, Y.; Maeshima, M.; Tsukaya, H.
Keep an eye on PPi: the vacuolar-type H+-pyrophosphatase regulates postgerminative development in Arabidopsis
Plant Cell
23
2895-2908
2011
Arabidopsis thaliana (A8MQH1)
brenda
Ferjani, A.; Segami, S.; Horiguchi, G.; Sakata, A.; Maeshima, M.; Tsukaya, H.
Regulation of pyrophosphate levels by H+-PPase is central for proper resumption of early plant development
Plant Signal. Behav.
7
38-42
2012
Arabidopsis thaliana
brenda
Mohammed, S.A.; Nishio, S.; Takahashi, H.; Shiratake, K.; Ikeda, H.; Kanahama, K.; Kanayama, Y.
Role of Vacuolar H+-inorganic pyrophosphatase in tomato fruit development
J. Exp. Bot.
63
5613-5621
2012
Solanum lycopersicum
brenda
Schmidt, A.L.; Briskin, D.P.
Energy transduction in tonoplast vesicles from red beet (Beta vulgaris L.) storage tissue H+/substrate stoichiometries for the H+-ATPase and H+-PPase
Arch. Biochem. Biophys.
301
165-173
1993
Beta vulgaris
brenda
Maeshima, M.
Oligomeric structure of H+-translocating inorganic pyrophosphatase of plant vacuoles
Biochem. Biophys. Res. Commun.
168
1157-1162
1990
Vigna radiata
brenda
Sarafian, V.; Potier, M.; Poole, R.J.
Radiation-inactivation analysis of vacuolar H+-ATPase and H+-pyrophosphatase from Beta vulgaris L. Functional sizes for substrate hydrolysis and for H+ transport
Biochem. J.
283
493-497
1992
Beta vulgaris
brenda
Lin, I.; Knight, W.B.; Hsueh, A.; Dunaway-Mariano, D.
Investigation of the regiospecificity and stereospecificity of proton transfer in the yeast inorganic pyrophosphatase catalyzed reaction
Biochemistry
25
4688-4692
1986
Saccharomyces cerevisiae
brenda
Fischer-Schliebs, E.; Mariaux, J.; Lttge, U.
Stimulation of H+-transport activity of vacuolar H+-ATPase by activation of H+-PPase in Kalanchoe blossfeldiana
Biol. Plant.
39
169-177
1997
Kalanchoe blossfeldiana
-
brenda
Hedrich, R.; Kurkdjian, A.; Guern, J.; Fluegge, U.I.
Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment
EMBO J.
8
2835-2841
1989
Beta vulgaris
brenda
Asaoka, M.M.; Segami, S.; Ferjani, A.; Maeshima, M.
Contribution of PPi-hydrolyzing function of vacuolar H+-pyrophosphatase in vegetative growth of Arabidopsis evidenced by expression of uncoupling mutated enzymes
Front. Plant Sci.
7
415
2016
Arabidopsis thaliana
brenda
Hernandez, A.; Herrera-Palau, R.; Madronal, J.M.; Albi, T.; Lopez-Lluch, G.; Perez-Castineira, J.R.; Navas, P.; Valverde, F.; Serrano, A.
Vacuolar H+-pyrophosphatase AVP1 is involved in amine fungicide tolerance in Arabidopsis thaliana and provides tridemorph resistance in yeast
Front. Plant Sci.
7
85
2016
Arabidopsis thaliana
brenda
Pizzio, G.A.; Hirschi, K.D.; Gaxiola, R.A.
Conjecture regarding posttranslational modifications to the Arabidopsis type I proton-pumping pyrophosphatase (AVP1)
Front. Plant Sci.
8
1572
2017
Arabidopsis thaliana
brenda
Yoon, H.S.; Kim, S.Y.; Kim, I.S.
Stress response of plant H+-PPase-expressing transgenic Escherichia coli and Saccharomyces cerevisiae a potentially useful mechanism for the development of stress-tolerant organisms
J. Appl. Genet.
54
129-133
2013
Arabidopsis thaliana (P31414), Oryza sativa (P93409)
brenda
Maeshima, M.; Yoshida, S.
Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean
J. Biol. Chem.
264
20068-20073
1989
Vigna radiata
brenda
Britten, C.J.; Zhen, R.G.; Kim, E.J.; Rea, P.A.
Reconstitution of transport function of vacuolar H+-translocating inorganic pyrophosphatase
J. Biol. Chem.
267
21850-21855
1992
Vigna radiata
brenda
Bhaskaran, S.; Savithramma, D.L.
Co-expression of Pennisetum glaucum vacuolar Na+/H+ antiporter and Arabidopsis H+-pyrophosphatase enhances salt tolerance in transgenic tomato
J. Exp. Bot.
62
5561-5570
2011
Arabidopsis thaliana
brenda
Khoudi, H.; Maatar, Y.; Gouiaa, S.; Masmoudi, K.
Transgenic tobacco plants expressing ectopically wheat H+-pyrophosphatase (H+-PPase) gene TaVP1 show enhanced accumulation and tolerance to cadmium
J. Plant Physiol.
169
98-103
2012
Triticum aestivum
brenda
Anjaneyulu, E.; Reddy, P.S.; Sunita, M.S.; Kishor, P.B.; Meriga, B.
Salt tolerance and activity of antioxidative enzymes of transgenic finger millet overexpressing a vacuolar H+-pyrophosphatase gene (SbVPPase) from Sorghum bicolor
J. Plant Physiol.
171
789-798
2014
Sorghum bicolor
brenda
Graus, D.; Konrad, K.R.; Bemm, F.; Patir Nebioglu, M.G.; Lorey, C.; Duscha, K.; Guethoff, T.; Herrmann, J.; Ferjani, A.; Cuin, T.A.; Roelfsema, M.R.G.; Schumacher, K.; Neuhaus, H.E.; Marten, I.; Hedrich, R.
High V-PPase activity is beneficial under high salt loads, but detrimental without salinity
New Phytol.
219
1421-1432
2018
Nicotiana benthamiana (A0A238ML06), Nicotiana benthamiana (A0A238MN04), Nicotiana benthamiana
brenda
Marsh, K.; Gonzalez, P.; Echeverria, E.
Partial characterization of H+-translocating inorganic pyrophosphatase from 3 citrus varieties differing in vacuolar pH
Physiol. Plant.
111
519-526
2001
Citrus aurantiifolia, Citrus sinensis, Citrus limettioides
brenda
Bao, A.K.; Du, B.Q.; Touil, L.; Kang, P.; Wang, Q.L.; Wang, S.M.
Co-expression of tonoplast cation/H+ antiporter and H+-pyrophosphatase from xerophyte Zygophyllum xanthoxylum improves alfalfa plant growth under salinity, drought and field conditions
Plant Biotechnol. J.
14
964-975
2016
Zygophyllum xanthoxylon
brenda
Li, Z.; Baldwin, C.M.; Hu, Q.; Liu, H.; Luo, H.
Heterologous expression of Arabidopsis H+-pyrophosphatase enhances salt tolerance in transgenic creeping bentgrass (Agrostis stolonifera L.)
Plant Cell Environ.
33
272-289
2010
Arabidopsis thaliana
brenda
Segami, S.; Asaoka, M.; Kinoshita, S.; Fukuda, M.; Nakanishi, Y.; Maeshima, M.
Biochemical, structural and physiological characteristics of vacuolar H+-pyrophosphatase
Plant Cell Physiol.
59
1300-1308
2018
Arabidopsis thaliana, Vigna radiata
brenda
Rea, P.A.; Britten, C.J.; Sarafian, V.
Common identity of substrate binding subunit of vacuolar H+-translocating inorganic pyrophosphatase of higher plant cells
Plant Physiol.
100
723-732
1992
Arabidopsis thaliana, Beta vulgaris, Vigna radiata, Zea mays
brenda
Pizzio, G.A.; Paez-Valencia, J.; Khadilkar, A.S.; Regmi, K.; Patron-Soberano, A.; Zhang, S.; Sanchez-Lares, J.; Furstenau, T.; Li, J.; Sanchez-Gomez, C.; Valencia-Mayoral, P.; Yadav, U.P.; Ayre, B.G.; Gaxiola, R.A.
Arabidopsis type I proton-pumping pyrophosphatase expresses strongly in phloem, where it is required for pyrophosphate metabolism and photosynthate partitioning
Plant Physiol.
167
1541-1553
2015
Arabidopsis thaliana
brenda
Khadilkar, A.S.; Yadav, U.P.; Salazar, C.; Shulaev, V.; Paez-Valencia, J.; Pizzio, G.A.; Gaxiola, R.A.; Ayre, B.G.
Constitutive and companion cell-specific overexpression of AVP1, encoding a proton-pumping pyrophosphatase, enhances biomass accumulation, phloem loading, and long-distance transport
Plant Physiol.
170
401-414
2016
Arabidopsis thaliana
brenda
Rea, P.A.; Poole, R.J.
Proton-translocating inorganic pyrophosphatase in red beet (Beta vulgaris L.) tonoplast vesicles
Plant Physiol.
77
46-52
1985
Beta vulgaris
brenda
Sarafian, V.; Poole, R.J.
Purification of an H+-translocating inorganic pyrophosphatase from vacuole membranes of red beet
Plant Physiol.
91
34-38
1989
Beta vulgaris
brenda
White, P.J.; Marshall, J.; Smith, J.A.
Substrate kinetics of the tonoplast H+-translocating inorganic pyrophosphatase and its activation by free Mg
Plant Physiol.
93
1063-1070
1990
Kalanchoe daigremontiana
brenda
Torabian, S.; Farhangi-Abriz, S.; Rathjen, J.
Biochar and lignite affect H+-ATPase and H+-PPase activities in root tonoplast and nutrient contents of mung bean under salt stress
Plant Physiol. Biochem.
129
141-149
2018
Vigna radiata
brenda
Regmi, K.C.; Pizzio, G.A.; Gaxiola, R.A.
Structural basis for the reversibility of proton pyrophosphatase
Plant Signal. Behav.
11
e1231294
2016
Vigna radiata
brenda
Davies, J.M.; Poole, R.J.; Rea, P.A.; Sanders, D.
Potassium transport into plant vacuoles energized directly by a proton-pumping inorganic pyrophosphatase
Proc. Natl. Acad. Sci. USA
89
11701-11705
1992
Beta vulgaris
brenda
Meng, L.; Li, S.; Guo, J.; Guo, Q.; Mao, P.; Tian, X.
Molecular cloning and functional characterisation of an H+-pyrophosphatase from Iris lactea
Sci. Rep.
7
17779
2017
Iris lactea
brenda
Yang, Y.; Tang, R.J.; Li, B.; Wang, H.H.; Jin, Y.L.; Jiang, C.M.; Bao, Y.; Su, H.Y.; Zhao, N.; Ma, X.J.; Yang, L.; Chen, S.L.; Cheng, X.H.; Zhang, H.X.
Overexpression of a Populus trichocarpa H+-pyrophosphatase gene PtVP1.1 confers salt tolerance on transgenic poplar
Tree Physiol.
35
663-677
2015
Populus trichocarpa
brenda
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Transporter Classification Database (TCDB): 3.A.10.3.1, 3.A.10.2.1, 3.A.10.1.1, 3.A.10.2.3, 3.A.10.1.8, 3.A.10.2.4, 3.A.10.1.17, 3.A.10.2.2, 3.A.10.3.3, 3.A.10.1.9, 3.A.10.1.2, 3.A.10.3.4, 3.A.10.3.5, 3.A.10.3.2, 3.A.10.1.16, 3.A.10.1.15
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