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EC Tree
IUBMB Comments Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius The enzyme appears in selected viruses and cellular organisms
Synonyms
pyrophosphatase, inorganic pyrophosphatase, v-ppase, h+-ppase, vacuolar h(+)-pyrophosphatase, sppase, e-ppase, vacuolar h(+)-ppase, soluble inorganic pyrophosphatase, ippase,
more
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inorganic pyrophosphatase
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inorganic diphosphatase
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inorganic pyrophosphatase
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pyrophosphatase, inorganic
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Pyrophosphate phospho-hydrolase
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Pyrophosphate phosphohydrolase
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Pyrophosphate-energized inorganic pyrophosphatase
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phosphorous acid anhydride hydrolysis
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diphosphate phosphohydrolase
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
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ADP + H2O
?
hydrolyzed at 36.2% of the rate compared to diphosphate
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?
ATP + H2O
?
hydrolyzed at 19.4% of the rate compared to diphosphate
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?
cyclic tripolyphosphate + H2O
?
hydrolyzed at 32.3% of the rate compared to diphosphate
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?
diphosphate + H2O
2 phosphate
tripolyphosphate + H2O
?
hydrolyzed at 44.3% of the rate compared to diphosphate
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-
?
ADP + H2O
? + phosphate
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3-6% of the activity with diphosphate
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-
?
ATP + H2O
? + phosphate
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3-6% of the activity with diphosphate
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-
?
diphosphate + H2O
2 phosphate
ITP + H2O
? + phosphate
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10% of the activity with diphosphate
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-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
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1-2% of the activity with diphosphate
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?
triphosphate + H2O
3 phosphate
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?
triphosphate + H2O
? + phosphate
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3-6% of the activity with diphosphate
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?
TTP + H2O
? + phosphate
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10% of the activity with diphosphate
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-
?
additional information
?
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enzyme is specific for diphosphate and does not cleave nucleotide-polyphosphates
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?
diphosphate + H2O
2 phosphate
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?
diphosphate + H2O
2 phosphate
as far as the release of phosphate, is concerned, diphosphate, is the best substrate
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?
diphosphate + H2O
2 phosphate
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?
diphosphate + H2O
2 phosphate
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actual substrate is magnesium diphosphate or dimagnesium diphosphate
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?
diphosphate + H2O
2 phosphate
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high specificity
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?
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diphosphate + H2O
2 phosphate
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actual substrate is magnesium diphosphate or dimagnesium diphosphate
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?
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CdCl2
20 mM, 155% stimulation
Mg2+
one Mg2+ per active site
MgCl2
20 mM, 163% stimulation
NiCl2
20 mM, 156% stimulation
Ca2+
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2% of the activity with Mg2+
Co2+
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88% of the activity with Mg2+
Mn2+
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32% of the activity with Mg2+
Ni2+
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3% of the activity with Mg2+
Zn2+
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95% of the activity with Mg2+
Mg2+
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required for activity
Mg2+
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preferred divalent cation, Km value 0.9 mM
additional information
divalent cations are not essential for the acid PPase activity
additional information
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no divalent cation required
additional information
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divalent cation required. Activity in decreasing order: Mg2+, Zn2+, Co2+, Mn2+, Ni2+, Ca2+
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Ca2+
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50% at 0.012 mM: Mg2+ 0.4 mM
additional information
addition of EDTA up to 0.5 mM to the assay mixture does not result in any change in the PPase activity
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additional information
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enzyme is stimulated by presence of membrane lipids from Sulfolobus acidocaldarius
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0.161
diphosphate
pH 3.0, 55°C
0.0054
diphosphate
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pH 7.0, 75°C
0.189
ATP
pH 3.0, 55°C
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1700
diphosphate
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pH 7.0, 75°C
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617
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56°C
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6.5
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2.5 - 4.5
at pH 2.5 and 4.5, about 50% of the maximal activity is observed
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80
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70% of maximum activity, rapid decline in activity above
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5.1
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isoelectric focusing
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Uniprot
brenda
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brenda
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brenda
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brenda
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brenda
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19365
4 * 19365, calculated from sequence
26000
1 * 26000, SDS-PAGE
17000
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4 * 17000, SDS-PAGE, 4 * 19365, calculated
21000
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4 * 21000, SDS-PAGE
19365
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4 * 17000, SDS-PAGE, 4 * 19365, calculated
19365
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x * 19365, calculated
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monomer
1 * 26000, SDS-PAGE
tetramer
4 * 19365, calculated from sequence
?
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x * 19365, calculated
additional information
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analysis of amino acid composition and comparison with Escherichia coli, saccharomyces cerevisiae and Bacillus sp. enzymes
tetramer
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4 * 21000, SDS-PAGE
tetramer
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4 * 17000-18000, SDS-PAGE
tetramer
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4 * 17000, SDS-PAGE, 4 * 19365, calculated
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at 2.7 A resolution. Comparison with Thermus thermophilus and Escherichia coli enzymes
CD and FTIR spectra demonstrate a similar overall fold for enzyme and PPases from Escherichia coli and Thermus thermophilus
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strucutural model based on structure of Thermus thermophilus enzyme
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70
the purified enzyme is less thermostable than the membrane-bound enzyme in situ. The remaining activity after incubation at 70°C, pH 7, for 15 min, is about 70 and 100% for the purified enzyme and the membrane enzyme, respectively
80
half-time of inactivation is 10 h
85
24 h, 19% loss of activity
90
4 h, 60% loss of activity
95
4 h, 85% loss of activity
98
in the presence of 5 mM Mg2+ the midpoint of thermal denaturation is increased to 98°C
89
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melting temperature, presence of EDTA
95
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half-life of catalytic activity 2.5 h
99
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melting temperature, presence of Mg2+
100
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10 min, no loss of activity
100
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melting temperature above 100°C, prensence of Mn2+
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5 mM Mg2+ stabilizes, the midpoint of thermal denaturation is increased to 98°C
extremely stable. No dissociation into subunit or unfolding of polypeptide chain occurrs in the presence of 8 M
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urea. Unfolding using guanidine-HC1 suggests that the transition between a native tetrameric state and an unfolded state is completely reversible, and essentially independent of any additional factors such as divalent metal cation or dithiothreitol
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Ethanol
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20% v/v, 82% residual activity
isopropanol
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20% v/v, 82% residual activity
Methanol
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20% v/v, 82% residual activity
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expression in Escherichia coli
expression in Escherichia coli
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addition of phosphate and/or diphosphate, to the semi-synthetic media results in about twofold increase in the acid PPase activity. However, in the nutrient broth, no induction is observed even when diphosphate is supplemented
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unfolding using guanidine-HCl suggests that the transition between a native tetrameric state and an unfolded state is completely reversible, and essentially independent of any additional factors such as divalent metal cation or dithiothreitol
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Wakagi, T.; Lee, C.H.; Oshima, T.
An extemely stable inorganic pyrophosphatase purified from the cytosol of a thermoacidophilic archaebacterium, Sulfolobus acidcaldarius strain 7
Biochim. Biophys. Acta
1120
289-296
1992
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius 7
brenda
Meyer, W.; Moll, R.; Kath, T.; Schäfer, G.
Purification, cloning, and sequencing of archaebacterial pyrophosphatase from the extreme thermoacidophile Sulfolobus acidocaldarius
Arch. Biochem. Biophys.
319
149-156
1995
Sulfolobus acidocaldarius
brenda
Hansen, T.; Urbanke, C.; Leppänen, V.M.; Goldman, A.; Brandenburg, K.; Schäfer, G.
The extreme thermostable pyrophosphatase from Sulfolobus acidocaldarius: enzymatic and comparative biophysical characterization
Arch. Biochem. Biophys.
363
135-147
1999
Sulfolobus acidocaldarius
brenda
Schaefer, T.; Boenisch, H.; Kardinahl, S.; Schmidt, C.; Schaefer, G.
Three extremely thermostable proteins from Sulfolobuc and a reappraisal of the 'traffic rules'
Biol. Chem.
377
505-512
1996
Sulfolobus acidocaldarius (P50308), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (P50308)
brenda
Meyer, W.; Schäfer, G.
Characterization and purification of a membrane-bound archaebacterial pyrophosphatase from Sulfolobus acidocaldarius
Eur. J. Biochem.
207
741-746
1992
Sulfolobus acidocaldarius
brenda
Leppänen, V.M.; Nummelin, H.; Hansen, T.; Lahti, R.; Schäfer, G.; Goldman, A.
Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase
Protein Sci.
8
1218-1231
1999
Sulfolobus acidocaldarius (P50308), Sulfolobus acidocaldarius
brenda
Amano, T.; Wakagi, T.; Oshima, T.
An ecto-enzyme from Sulfolobus acidocaldarius strain 7 which catalyzes hydrolysis of inorganic pyrophosphate, ATP, and ADP: purification and characterization
J. Biochem.
114
329-333
1993
Sulfolobus acidocaldarius (P50308), Sulfolobus acidocaldarius 7 (P50308)
brenda