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Information on EC 3.6.1.1 - inorganic diphosphatase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession P50308

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.1 inorganic diphosphatase
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.
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Sulfolobus acidocaldarius
UNIPROT: P50308
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Word Map
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pyrophosphatase, inorganic pyrophosphatase, v-ppase, h+-ppase, vacuolar h(+)-pyrophosphatase, sppase, e-ppase, vacuolar h(+)-ppase, soluble inorganic pyrophosphatase, ippase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inorganic pyrophosphatase
-
H+-PPase
-
-
-
-
inorganic diphosphatase
-
-
-
-
inorganic pyrophosphatase
-
-
-
-
PPase
-
-
-
-
pyrophosphatase, inorganic
-
-
-
-
Pyrophosphate phospho-hydrolase
-
-
-
-
Pyrophosphate phosphohydrolase
-
-
-
-
Pyrophosphate-energized inorganic pyrophosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-82-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + H2O
?
show the reaction diagram
hydrolyzed at 36.2% of the rate compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
hydrolyzed at 19.4% of the rate compared to diphosphate
-
-
?
cyclic tripolyphosphate + H2O
?
show the reaction diagram
hydrolyzed at 32.3% of the rate compared to diphosphate
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
tripolyphosphate + H2O
?
show the reaction diagram
hydrolyzed at 44.3% of the rate compared to diphosphate
-
-
?
ADP + H2O
? + phosphate
show the reaction diagram
-
3-6% of the activity with diphosphate
-
-
?
ATP + H2O
? + phosphate
show the reaction diagram
-
3-6% of the activity with diphosphate
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
ITP + H2O
? + phosphate
show the reaction diagram
-
10% of the activity with diphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
1-2% of the activity with diphosphate
-
-
?
triphosphate + H2O
3 phosphate
show the reaction diagram
-
-
-
-
?
triphosphate + H2O
? + phosphate
show the reaction diagram
-
3-6% of the activity with diphosphate
-
-
?
TTP + H2O
? + phosphate
show the reaction diagram
-
10% of the activity with diphosphate
-
-
?
additional information
?
-
-
enzyme is specific for diphosphate and does not cleave nucleotide-polyphosphates
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CdCl2
20 mM, 155% stimulation
Mg2+
one Mg2+ per active site
MgCl2
20 mM, 163% stimulation
NiCl2
20 mM, 156% stimulation
Ca2+
-
2% of the activity with Mg2+
Co2+
-
88% of the activity with Mg2+
Mn2+
-
32% of the activity with Mg2+
Ni2+
-
3% of the activity with Mg2+
Zn2+
-
95% of the activity with Mg2+
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
above 10 mM
F-
20 mM, 80% inhibition
Ca2+
-
50% at 0.012 mM: Mg2+ 0.4 mM
diphosphate
-
free
additional information
addition of EDTA up to 0.5 mM to the assay mixture does not result in any change in the PPase activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme is stimulated by presence of membrane lipids from Sulfolobus acidocaldarius
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.189 - 0.237
ATP
0.161
diphosphate
pH 3.0, 55°C
0.0054
diphosphate
-
pH 7.0, 75°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1700
diphosphate
-
pH 7.0, 75°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30.8
pH 3.0, 55°C
650
-
pH 3.3, 70°C
672.2
-
pH 7.0, 70°C
860
-
pH 7.0, 75°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 4.5
at pH 2.5 and 4.5, about 50% of the maximal activity is observed
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
70% of maximum activity, rapid decline in activity above
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19365
4 * 19365, calculated from sequence
26000
1 * 26000, SDS-PAGE
35000
gel filtration
17000
-
4 * 17000, SDS-PAGE, 4 * 19365, calculated
19365
21000
-
4 * 21000, SDS-PAGE
71000
-
gel filtration
80000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 26000, SDS-PAGE
tetramer
4 * 19365, calculated from sequence
?
-
x * 19365, calculated
tetramer
additional information
-
analysis of amino acid composition and comparison with Escherichia coli, saccharomyces cerevisiae and Bacillus sp. enzymes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
strucutural model based on structure of Thermus thermophilus enzyme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9
-
-
677801
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
melting temperature, presence of EDTA
95
-
half-life of catalytic activity 2.5 h
99
-
melting temperature, presence of Mg2+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
-
20% v/v, 82% residual activity
isopropanol
-
20% v/v, 82% residual activity
Methanol
-
20% v/v, 82% residual activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team