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Information on EC 3.6.1.11 - exopolyphosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38698
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3.6.1.11 exopolyphosphataseSpecify your search results
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
exopolyphosphatase, polyphosphate phosphatase, polyphosphate phosphohydrolase, exopolypase, rv0496, exopoly(p)ase, pappx, high molecular weight exopolyphosphatase, exopolyphosphatase 1, lmppx, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid phosphoanhydride phosphohydrolase
-
-
-
-
exopoly(P)ase
-
-
-
-
ExopolyPase
Gra-Pase
-
-
-
-
metaphosphatase
-
-
-
-
phosphatase, exopoly-
-
-
-
-
Ppn1
additional information
ExopolyPase
-
-
-
-
additional information
-
PPX belongs to the DHH phosphoesterase superfamily and is evolutionarily close to the well characterized family II pyrophosphatase, PPase
additional information
-
PPX1 belongs to the DHH family of phosphoesterases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
hydrolyzes poly-phosphates with an average chain length of 208 to 15 phosphate residues
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
phosphorous acid anhydride hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
polyphosphate phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9024-85-5
-
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
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
-
?
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
-
-
-
?
(phosphate)25 + H2O
(phosphate)24 + phosphate
100% activity
-
-
?
(phosphate)45 + H2O
(phosphate)44 + phosphate
100% activity
-
-
?
(phosphate)9 + H2O
(phosphate)8 + phosphate
45% of the activity with (phosphate)25
-
-
?
polyphosphate + H2O
?
-
chain length of more than 45 phosphate residues
-
-
?
(phosphate)15 + H2O
(phosphate)14 + phosphate
88% of the activity with (phosphate)25
-
-
?
(phosphate)208 + H2O
(phosphate)207 + phosphate
-
reaction continues to a chain length of about 15 residues
-
?
(phosphate)208 + H2O
(phosphate)207 + phosphate
100% activity
-
-
?
(phosphate)3 + H2O
(phosphate)2 + phosphate
14% of the activity with (phosphate)25
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
-
-
-
?
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
the cytosolic exopolyphosphatase that processively cleaves the terminal phosphate group from the polyphosphate chain, until inorganic diphosphate is all that remains, structure of the substrate binding channel, overview
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
the activity with polyP15 is 85% of that with polyP208, the activity with polyP9 is 24% of that with polyP208
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
poly P9-10, polyP33-36
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
n = 10, 25, 50, 100, 250 or 500. n = 250 is the preferred substrate
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
polyP15, polyP208
-
?
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
chain length of 10-200 phosphate residues
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
7.3% of the activity with polyP208
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
-
-
?
polyphosphate 208 + H2O
polyphosphate 207 + phosphate
-
-
-
-
?
tripolyphosphate + H2O
phosphate + ?
-
7.3% of the activity with polyP208
-
-
?
additional information
?
-
Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain
-
-
-
additional information
?
-
-
Ppx1 has high exopolyphosphatase activity (EC 3.6.1.11), but no endopolyphosphatase activity (EC 3.6.1.10). The Ppx1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppx1 does not hydrolyze ATP and dATP. Exopolyphosphatases (polyphosphate phosphohydrolases, EC 3.6.1.11) cleave phosphate from the end of the polyphosphate chain
-
-
-
additional information
?
-
-
ATP, diphosphate and p-nitrophenyl phosphate are not substrates
-
-
?
additional information
?
-
-
PPN1 splitting long polyphosphate chains to shorter ones
-
-
?
additional information
?
-
-
PPX1 splitting off phosphate from the end of the polyphosphate chain
-
-
?
additional information
?
-
enzyme is a bifunctional exo- and endopolyphosphatase, activities of EC 3.6.1.11 and EC 3.6.1.10, respectively. No activity with diphosphate, ATP and 4-nitrophenylphosphate
-
-
?
additional information
?
-
-
enzyme is a bifunctional exo- and endopolyphosphatase, activities of EC 3.6.1.11 and EC 3.6.1.10, respectively. No activity with diphosphate, ATP and 4-nitrophenylphosphate
-
-
?
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
(phosphate)n + H2O
(phosphate)n-1 + phosphate
-
-
-
-
?
additional information
?
-
-
PPN1 splitting long polyphosphate chains to shorter ones
-
-
?
additional information
?
-
-
PPX1 splitting off phosphate from the end of the polyphosphate chain
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
NH4Cl
-
50 and 200 mM, 42 and 67% activity enhancement, respectively
Ni2+
Zn2+
additional information
-
stimulated by divalent cations to a lesser extent
Co2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Co2+
-
stimulated by divalent cations, Co2+ is the best stimulator, 6fold at 0.05 mM
Co2+
Co2+ stimulates phosphate release from the polyphosphate chain end
Mg2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Mn2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
Ni2+
-
divalent cation required, order of decreasing stimulation: Co2+, Mn2+, Mg2+, Ni2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
-
0.05 mM, 30% inhibition in a reaction mixture containing Co2+ at its optimal concentration
Zn2+
-
0.05 mM, 71% inhibition in a reaction mixture containing Co2+ at its optimal concentration
heparin
inhibits the endopolyphosphatase activity by 50% at 0.05 mg/ml
additional information
not inhibited by 1 mM sodium fluoride
-
additional information
-
not inhibited by antibodies suppressing the activity of 40 kDa-exopolyphosphatase
-
additional information
in the presence of Mg2+, the enzyme shows a polyphosphate chain fragmentation activity. ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
-
additional information
-
in the presence of Mg2+, the enzyme shows a polyphosphate chain fragmentation activity. ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ammonium chloride
200 mM, stimulates almost twofold in the presence and absence of 0.1 mM Co2+
additional information
-
RNA does not alter the nuclear exopolyphosphatase activity
-
additional information
RNA does not alter the nuclear exopolyphosphatase activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
adenosine 5'-tetraphosphate
-
at pH 4.8, 50 mM sodium acetate, 5 mM CoCl2
additional information
additional information
-
steady-state kinetic analysis
-
0.025
(25R)-3beta-hydroxycholest-5-en-27-oate
polyphosphate 208, in the presence of 2.5 mM Mg2+
0.133
(25R)-3beta-hydroxycholest-5-en-27-oate
polyphosphate 15, in the presence of 2.5 mM Mg2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.006
-
strain CRX with inactivated ppx1 and ppN1 gene, cytosol preparation in exponential growth phase in phosphate-deficient medium
0.01
-
strain CRX with inactivated ppx1 and ppN1 gene, cytosol preparation in exponential growth phase in phosphate-rich medium
0.014
-
40-kDa-exopolyphosphatase from Saccharomyces cerevisiae strain CRN grown on glucose
0.034
0.035
-
high-molecular weight exopolyphosphatase from Saccharomyces cerevisiae strain CRX grown on glucose
0.04
0.05
1.25 mM polyphosphate 3 as substrate, in the presence of 2.5 mM Mg2+
0.055
-
strain CRX with inactivated ppx1 gene, cytosol preparation in exponential growth phase in phosphate-deficient medium
0.058
-
soluble form of exopolyphospatase from Saccharomyces cerevisiae strain CRX grown on lactate
0.07
-
strain CRX with inactivated ppn1 gene, cytosol preparation in exponential growth phase in phosphate-rich medium
0.08
-
membrane-bound exopolyphosphatase from Saccharomyces cerevisiae strain CRX grown on glucose
0.095
0.097
-
membrane-bound exopolyphosphatase from Saccharomyces cerevisiae strain CRY grown on glucose
0.1
0.119
-
soluble form of exopolyphospatase from Saccharomyces cerevisiae strain CRY grown on lactate
0.136
-
40-kDa-exopolyphosphatase from Saccharomyces cerevisiae strain CRY grown on glucose
0.18
-
parent strain CRY, cytosol preparation in exponential growth phase in phosphate-rich medium
0.21
0.13 mM polyphosphate 15 as substrate, in the presence of 1 mM Co2+
0.23
0.13 mM polyphosphate 15 as substrate, in the presence of 0.1 mM Co2+
0.28
0.01 mM polyphosphate 208 as substrate, in the presence of 1 mM Co2+
0.3
2.0 mM polyphosphate 208 as substrate, in the presence of 0.1 mM Co2+
150
240
substrate (phosphate)15, presence of 0.1 mM Co2+, pH 7.2, 30°C
290
substrate (phosphate)208, presence of 0.1 mM Co2+, pH 7.2, 30°C
3 - 8
substrate (phosphate)3, presence of 0.1 mM Co2+, pH 7.2, 30°C
additional information
0.034
-
membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRX grown on lactate
0.034
-
membrane-bound form of exopolyphospatase from Saccharomyces cerevisiae strain CRY grown on lactate
0.04
1.25 mM diphosphate as substrate, in the presence of 2.5 mM Mg2+
0.04
-
strain CRX with inactivated ppx1 gene, cytosol preparation in exponential growth phase in phosphate-rich medium
0.095
0.01 mM polyphosphate 208 as substrate, in the presence of 2.5 mM Mg2+
0.095
-
strain CRX with inactivated ppn1 gene, cytosol preparation in exponential growth phase in phosphate-deficient medium
0.1
0.13 mM polyphosphate 15 as substrate, in the presence of 2.5 mM Mg2+
0.1
-
parent strain CRY, cytosol preparation in exponential growth phase in phosphate-deficient medium
150
-
after 319fold purification with heparin agarose, at 30°C in 1 ml of reaction mixture containing 50 mM Tris-HCl buffer, pH 7.2, 0.1 mM CoSO4, 200 mM ammonium chloride, and 0.01 mM polyphosphate 208
additional information
-
the exopolyphosphatase activity is reduced 6.5fold in the mutant CRN lacking endopolyphosphatase activity
additional information
-
no specific activity on diphosphate, ATP and p-nitrophenyl phosphate
additional information
-
polyphosphate levels in different cell compartments, overview
additional information
-
polyphosphate hydrolysis in the CRX strain cytosol completes in 120 min
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 53
-
30°C: about 30% of maximal activity, 53°C: about 40% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
polyP metabolism in cytosol and mitochondria is substantially dependent on the carbon source, acid-soluble polyP accumulates mainly in cytosol using either glucose or ethanol. The level of the accumulation is lower during growth on ethanol compared to that on glucose. Increase in polyP content in mitochondria occurs during growth on glucose, but not on ethanol. In cytosol the activity of exopolyphosphatase PPN1 is increased and the activity of exopolyphosphatase PPX1 is decreased independently of the carbon source under phosphate surplus conditions, overview. Growth on ethanol induces exopolyphosphatase PPN1 in the soluble mitochondrial fraction, while during growth on glucose only exopolyphosphatase PPX1 is present in this fraction
-
-
-
209849, 654785, 654839, 654886, 667750, 667765, 668027, 670176, 670725, 685307, 687678, 688364, 696170
-
nuclear exopolyphosphatase activity does not depend on the growth phase
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the DHH family of phosphoesterases. Polyphosphatases Ppx1, Ppn1, Ddp1, and Ppn2 show distinct substrate specificities and levels of endo- and exopolyphosphatase activities, as well as distinct patterns of stimulation by metal ions. The differences in the mode of polyphosphate hydrolysis, substrate specificity, metal ion dependence and cell localization suggest distinct roles of these enzymes in yeast
metabolism
the enzyme PPN1 shows only exopolyphosphatase activity
physiological function
strong constitutive overexpression of exopolyphosphatase PPN1 results in 28- and 11fold increase in activity compared to the PPN1 mutant and wild-type strains, respectively. The content of acid-soluble polyphosphate decreases about 6fold and the content of acid-insoluble polyphosphate decreases about 2.5fold in the cells of the transformant compared to the mutant strain
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
-
Superose 6 column gel filtration, active but unstable enzyme complex
32000
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
33000
35000
40000
45000
500000
33000
-
SDS-PAGE, probably a product of mRNA splicing or/and protein processing
35000
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
500000
-
Superose 6 column gel filtration, stable enzyme complex composed of two polypeptides of 32 and 35 kDa and apparently polyphosphates
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 32000 + x * 35000, polyphosphate seems to stabilize the complex
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
PPN1 gene encodes a polypeptide with the predicted molecular mass of 78 kDa, the monomer molecular mass of the mature PPN1 is about 33-35 kDa
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzxme in complex with phosphate, sulfate, or ATP, X-ray diffraction structure determination and analysis at 1.6, 1.8, and 1.9 A resolution, multiple isomorphous replacement with anomalous scattering technique
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D127E
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
D127N
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
H148N
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat in comparison to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
H149N
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat in comparison to the wild-type enzyme, the activaion by divalent cations differs between wild-type and mutant enzymes, overview
N35H
-
site-directed mutagenesis, the mutant shows reduced the Mg2+ affinity of the tight binding site compared to the wild-type enzyme, the activation by divalent cations differs between wild-type and mutant enzymes, overview
additional information
additional information
construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppx1, that shows increased polyphosphate levels
additional information
-
construction of a Saccharomyces cerevisiae strain CRN overexpressing Ppn2 polyphosphatase and comparison the properties of polyphosphatases Ppn2, Ppx1, Ppn1, and Ddp1 purified from overexpressing strains of Saccharomyces cerevisiae, overview. Construction of deletion mutant DELTAppx1, that shows increased polyphosphate levels
additional information
-
inactivation of PPN1 affects the polyP level in the nuclei insignificantly in the stationary phase, while in the exponential phase the level increases 2.3fold as compared with the parent strain of Saccharomyces cerevisiae, overview
additional information
-
inactivation of the PPX1 gene has no effect on the polyP metabolism under cultivation of the yeast in medium with glucose and phosphate, while inactivation of the PPN1 gene results in elimination of the high-molecular-mass exopolyphosphatases of the cytosol, nuclei, vacuoles, and mitochondria of Saccharomyces cerevisiae, PPN1 inactivation has negligible effect on polyP levels, it results in increase in the long-chain polyPs in all the compartments under study
additional information
-
mutation of conserved residues Asp127, His148, His149 , and Asn35 lead to reduced activity compared to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 0.05 mM CoSO4 does not increase the enzyme stability independent of the presence of Triton X-100
-
more than 90% loss of activity after freezing in liquid nitrogen and subsequent thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl buffer, pH 7.6, 10 mM MgCl2, 0.5 mM EDTA, 150 mM NaCl, 20% loss of activity after 2 months
-
-4°C, enzyme desorbed from heparin-agarose with 1 M KCl and 0.1% Triton X-100, 4 days, no loss of activity
-
4°C, enzyme obtained by desorption with polyphosphate, 2 h, 30% loss of activity
-
4°C, in absence of detergents, complete loss of activity after 24 h, can be stabilized by 0.1% Triton X-100 and protease inhibitors
-
92°C, in the presence of 0.1% Triton X-100, 5 days, 8% loss of activity of the partially purified exopolyphosphatase preparation after DEAE-Toyopearl chromatography
-
92°C, without 0.1% Triton X-100, 5 days, 66% loss of activity of the partially purified exopolyphosphatase preparation after DEAE-Toyopearl chromatography
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme PPX1 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ppx1, recombinant overexpression in Saccharomyces cerevisiae strain CRN
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Andreeva, N.A.; Kulakovskaya, T.V.; Kualev, I.S.
Purification and properties of exopolyphosphatase isolated from Saccharomyces cerevisiae vacuoles
FEBS Lett.
429
194-196
1998
Saccharomyces cerevisiae
Lorenz, B.; Mueller, W.E.G.; Kualev, I.S.; Schroeder, H.C.
Purification and characterization of an exopolyphosphatase from Saccharomyces cerevisiae
J. Biol. Chem.
269
22198-22204
1994
Saccharomyces cerevisiae
Wurst, H.; Kornberg, A.
A soluble exopolyphosphatase of Saccharomyces cerevisiae. Purification and characterization
J. Biol. Chem.
269
10996-11001
1994
Saccharomyces cerevisiae
Kulakovskaya, T.V.; Andreeva, N.A.; Kualev, I.S.
Adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate: new substrates of the cytosolic exopolyphosphatase of the yeast Saccharomyces cerevisiae
Biochemistry
62
1051-1052
1997
Saccharomyces cerevisiae
Guranowski, A.; Starzynska, E.; Barnes, L.D.; Robinson, A.K.; Liu, S.
Adenosine 5'-tetraphosphate phosphohydrolase activity is an inherent property of soluble exopolyphosphatase from yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1380
232-238
1998
Saccharomyces cerevisiae
Lichko, L.P.; Kulakovskaya, T.V.; Kulaev, I.S.
Partial purification and characterization of nuclear exopolyphosphatase from Saccharomyces cerevisiae strain with inactivated PPX1 gene encoding a major yeast exopolyphosphatase
Biochemistry
69
270-274
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38698), Saccharomyces cerevisiae CRX
Andreeva, N.A.; Kulakovskaya, T.V.; Kulaev, I.S.
Purification and properties of exopolyphosphatase from the cytosol of Saccharomyces cerevisiae not encoded by the PPX1 gene
Biochemistry
69
387-393
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
Lichko, L.; Kulakovskaya, T.; Kulaev, I.
Effect of PPX1 inactivation on exopolyphosphatases of different cell compartments of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1599
102-105
2002
Saccharomyces cerevisiae
Lichko, L.; Kulakovskaya, T.; Kulaev, I.
Inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1 in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1674
98-102
2004
Saccharomyces cerevisiae
Kulakovskaya, T.V.; Andreeva, N.A.; Trilisenko, L.V.; Suetin, S.V.; Vagabov, V.M.; Kulaev, I.S.
Accumulation of polyphosphates and expression of high molecular weight exopolyphosphatase in the yeast Saccharomyces cerevisiae
Biochemistry
70
980-985
2005
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
Andreeva, N.A.; Kulakovskaya, T.V.; Kulaev, I.S.
High Molecular Mass Exopolyphosphatase from the Cytosol of the Yeast Saccharomyces cerevisiae Is Encoded by the PPN1 Gene
Biochemistry (Moscow)
71
975-977
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
Lichko, L.; Kulakovskaya, T.; Pestov, N.; Kulaev, I.
Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes
Biosci. Rep.
26
45-54
2006
Saccharomyces cerevisiae
Pestov, N.A.; Kulakovskaya, T.V.; Kulaev, I.S.
Effects of inactivation of the PPN1 gene on exopolyphosphatases, inorganic polyphosphates and function of mitochondria in the yeast Saccharomyces cerevisiae
FEMS Yeast Res.
5
823-828
2005
Saccharomyces cerevisiae
Kulakovskaya, T.V.; Trilisenko, L.V.; Lichko, L.P.; Vagabov, V.M.; Kulaev, I.S.
The effect of inactivation of the exo- and endopolyphosphatase genes PPX1 and PPN1 on the level of different polyphosphates in the yeast Saccharomyces cerevisiae
Microbiology
75
25-28
2006
Saccharomyces cerevisiae
-
Lichko, L.P.; Kulakovskaya, T.V.; Pestov, N.A.; Kulaev, I.S.
Inactivation of the PPN1 gene exerts different effects on the metabolism of inorganic polyphosphates in the cytosol and the vacuoles of the yeast Saccharomyces cerevisiae
Microbiology
75
253-258
2006
Saccharomyces cerevisiae
-
Kulakovskaya, T.V.; Andreeva, N.A.; Trilisenko, L.V.; Vagabov, V.M.; Kulaev, I.S.
Two exopolyphosphatases in Saccharomyces cerevisiae cytosol at different culture conditions
Process Biochem.
39
1625-1630
2004
Saccharomyces cerevisiae
-
Lichko, L.P.; Kulakovskaya, T.V.; Kulaev, I.S.
Inorganic polyphosphates and exopolyphosphatases in different cell compartments of Saccharomyces cerevisiae
Biochemistry (Moscow)
71
1171-1175
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae CRY
Andreeva, N.A.; Kulakovskaya, T.V.; Kulakovskaya, E.V.; Kulaev, I.S.
Polyphosphates and exopolyphosphatases in cytosol and mitochondria of Saccharomyces cerevisiae during growth on glucose or ethanol under phosphate surplus
Biochemistry (Moscow)
73
65-69
2008
Saccharomyces cerevisiae
Tammenkoski, M.; Moiseev, V.M.; Lahti, M.; Ugochukwu, E.; Brondijk, T.H.; White, S.A.; Lahti, R.; Baykov, A.A.
Kinetic and mutational analyses of the major cytosolic exopolyphosphatase from Saccharomyces cerevisiae
J. Biol. Chem.
282
9302-9311
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae AH22
Ugochukwu, E.; Lovering, A.L.; Mather, O.C.; Young, T.W.; White, S.A.
The crystal structure of the cytosolic exopolyphosphatase from Saccharomyces cerevisiae reveals the basis for substrate specificity
J. Mol. Biol.
371
1007-1021
2007
Saccharomyces cerevisiae
Lichko, L.P.; Kulakovskaya, T.V.; Kulaev, I.S.
Inorganic polyphosphate and exopolyphosphatase in the nuclei of Saccharomyces cerevisiae: dependence on the growth phase and inactivation of the PPX1 and PPN1 genes
Yeast
23
735-740
2006
Saccharomyces cerevisiae
Lichko, L.P.; Kulakovskaya, T.V.; Kulakovskaya, E.V.; Kulaev, I.S.
Inactivation of PPX1 and PPN1 genes encoding exopolyphosphatases of Saccharomyces cerevisiae does not prevent utilization of polyphosphates as phosphate reserve
Biochemistry (Moscow)
73
985-989
2008
Saccharomyces cerevisiae
Andreeva, N.; Trilisenko, L.; Kulakovskaya, T.; Dumina, M.; Eldarov, M.
Purification and properties of recombinant exopolyphosphatase PPN1 and effects of its overexpression on polyphosphate in Saccharomyces cerevisiae
J. Biosci. Bioeng.
119
52-56
2015
Saccharomyces cerevisiae (Q04119), Saccharomyces cerevisiae
Andreeva, N.; Trilisenko, L.; Eldarov, M.; Kulakovskaya, T.
Polyphosphatase PPN1 of Saccharomyces cerevisiae: switching of exopolyphosphatase and endopolyphosphatase activities
PLoS ONE
10
e0119594
2015
Saccharomyces cerevisiae (Q04119), Saccharomyces cerevisiae
Andreeva, N.; Ledova, L.; Ryazanova, L.; Tomashevsky, A.; Kulakovskaya, T.; Eldarov, M.
Ppn2 endopolyphosphatase overexpressed in Saccharomyces cerevisiae Comparison with Ppn1, Ppx1, and Ddp1 polyphosphatases
Biochimie
163
101-107
2019
Saccharomyces cerevisiae (P38698), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P38698)
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