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Information on EC 3.6.1.10 - endopolyphosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q99321

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.10 endopolyphosphatase
IUBMB Comments
The product contains 4 or 5 phosphate residues.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q99321
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
nudix hydrolase, polyphosphatase, endopolyphosphatase, short-chain polyphosphate, tbnh4, yor163w, endopolypase, tbdcp2, polyphosphate depolymerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dual exo/endopolyphoshatase
-
endopolyPase
-
-
metaphosphatase
-
-
-
-
phosphatase, endopoly-
-
-
-
-
polymetaphosphatase
-
-
-
-
polyphosphatase
-
-
-
-
polyphosphate depolymerase
-
-
-
-
PPN
-
-
-
-
short-chain polyphosphate
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
polyphosphate polyphosphohydrolase
The product contains 4 or 5 phosphate residues.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-86-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
polyphosphate15 + H2O
?
show the reaction diagram
-
-
-
?
polyphosphate208 + H2O
?
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
-
?
cAMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
show the reaction diagram
-
-
-
?
polyP750 + H2O
polyP749 + phosphate
show the reaction diagram
-
-
-
-
?
polyphosphate + H2O
oligophosphate
show the reaction diagram
polyphosphate 208 + H2O
oligophosphate
show the reaction diagram
-
-
the average polyphosphate chain lengths decrease from about 208 to about 10 phosphate residues
-
?
polyphosphate 208 + H2O
polyphosphate 193 + polyphosphate 15
show the reaction diagram
-
-
-
-
?
polyphosphate208 + H2O
?
show the reaction diagram
-
-
-
?
polyphosphate3 + H2O
?
show the reaction diagram
-
-
-
?
polyphosphate3 + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
?
polyphosphate700 + H2O
phosphate + triphosphate
show the reaction diagram
progression via intermediate chain length polyphosphates
product analysis
-
?
additional information
?
-
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
stimulates the endopolyphosphatase activity at 0.1 mM
Zn2+
stimulates the endopolyphosphatase activity at 0.1 mM
Zn2+
stimulates the endopolyphosphatase activity at 0.01 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
inhibits the endopolyphophatase of the recombinant enzyme DDP1
diphosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
phosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
Triphosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
ATP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
CaCl2
-
1 mM, 35% inhibition
diphosphate
-
10 mM, complete inhibition
EDTA
-
10 mM, complete inhibition
heparin
phosphate
-
20 mM, 50% inhibition
ZnCl2
-
1 mM, 35% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000185
polyP750
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
purified recombinant enzyme, exopolyphosphatase activity, pH 7.2, 30°C
0.1
purified recombinant enzyme, exopolyphosphatase activity, pH 7.2, 30°C
190
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate polyphosphate3, pH 7.2, 30°C
210
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate GTP, pH 7.2, 30°C
30
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate diphosphate, pH 7.2, 30°C
40
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate ATP, pH 7.2, 30°C
420
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate guanosine tetraphosphate, pH 7.2, 30°C
530
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate polyphosphate208, pH 7.2, 30°C
65000
purified native Ppn1
80
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate dATP, pH 7.2, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the Nudix hydrolase family. 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
malfunction
the content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively. The average chain length of salt-soluble and alkali-soluble fractions does not change in the overexpressing strain, and that of acid-soluble polyphosphate increases under phosphate excess. At the initial stage of polyphosphate recovery after phosphorus starvation, the chain length of the acid-soluble fraction in transformed cells is lower compared to the recipient strain. In DDP1 deletion mutant, the level of inositol pyrophosphate is twice higher, while the level of polyphosphate is reduced. The overexpression of DDP1 probably leads to a decrease in the level of diphosphoinositol pentakisphosphate and bis(diphosphoinositol) tetrakisphosphate in the cell. These compounds seem to be involved in the regulation of polyphosphate synthesis and degradation
metabolism
physiological function
yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) having endopolyphosphatase activity on inorganic polyphosphate metabolism in Saccharomyces cerevisiae. Complex nature of DDP1 involvement in the regulation of polyphosphate content and chain length in yeasts
evolution
metabolism
the enzyme PPN1 shows exo- and endopolyphosphatase activities, EC 3.6.1.11 and EC 3.6.1.10, respectively
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
142000
native enzyme, gel filtration
20000
-
gel filtration
34500
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
35000
-
2 * 35000, SDS-PAGE
80000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 21570, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
homotetramer
4 * 33000-35000, SDS-PAGE
monomer
1 * 37150, SDS-PAGE
tetramer
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme DPP1 from Saccharomyces cerevisiae strain CRN by anion exchange chromatography and ultrafiltration
DEAE Toyopearl 650M column chromatography, heparin agarose column chromatography, and Mono Q column chromatography
-
native enzyme from exopolyphosphatase-deficient mutant strain CRX by heparin affinity and phosphocellulose chromatography, 3820fold to homogeneity
recombinant enzyme PPN1 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps
recombinant enzyme PPN2 from Saccharomyces cerevisiae strain CRN by ammonium sulfate fractionation, anion exchange chromatography, heparin affinity chromatography, all alternating with ultrafiltration steps
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ddp1, recombinant overexpression in Saccharomyces cerevisiae strain CRN
gene DDP1, recombinant overexpression in Saccharomyces cerevisiae strain CRN. The initial strain CRN lacks the endopolyphosphatase PPN1, but has its own protein DDP1, which accounts for the low endopolyphosphatase activity in this strain. The recombinant DDP1 enzyme shows an endopolyphosphatase activity, the endopolyphosphatase activity of the transformant manifests itself both with long-chain polyP208 and with short-chain polyP15. Content of phosphate and polyphosphate in cells of CRN, overview
expression in Saccharomyces cerevisiae
gene ppn1, DNA and amino acid sequence determination and analysis, expression of wild-type pre-Ppn1 and mutants in Escherichia coli and in HEK-293 cells
gene ppn1, recombinant overexpression in Saccharomyces cerevisiae strain CRN
gene ppn2, recombinant overexpression of the soluble enzyme in Saccharomyces cerevisiae strain CRN
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
the overexpression of the processed form of the enzyme should provide a unique and powerful reagent to analyze inorganic polyphosphate when the chain termini are unavailable to the actions of polyPase and polyP kinase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kowalczyk, T.H.; Phillips, N.F.B.
Determination of endopolyphosphatase using polyphosphate glucokinase
Anal. Biochem.
212
194-205
1993
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kumble, K.; Kornberg, A.
Endopolyphosphatase for long chain inorganic polyphosphate in yeast and mammals
J. Biol. Chem.
271
27146-27151
1996
Caenorhabditis elegans, Chlamydomonas sp., Dictyostelium discoideum, Drosophila melanogaster, Giardia intestinalis, Neurospora crassa, Phaeodactylum tricornutum, Pyrococcus islandicum, Rattus norvegicus, Saccharomyces cerevisiae, Sulfolobus acidocaldarius, Synechococcus sp.
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Sethuraman, A.; Rao, N.N.; Kornberg, A.
The endopolyphosphatase gene: essential in Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
98
8542-8547
2001
Saccharomyces cerevisiae (Q04119), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Shi, X.; Kornberg, A.
Endopolyphosphatase in Saccharomyces cerevisiae undergoes post-translational activations to produce short-chain polyphosphates
FEBS Lett.
579
2014-2018
2005
Saccharomyces cerevisiae (Q04119), Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Lichko, L.P.; Kulakovskaya, T.V.; Kulakovskaya, E.V.; Kulaev, I.S.
Finding of endopolyphosphatase activity in the yeast Saccharomyces cerevisiae
Biochemistry
74
842-845
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lichko, L.P.; Kulakovskaya, T.V.; Kulaev, I.S.
Properties of partially purified endopolyphosphatase of the yeast Saccharomyces cerevisiae
Biochemistry (Moscow)
75
1404-1407
2010
Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Trilisenko, L.V.; Andreeva, N.A.; Eldarov, M.A.; Dumina, M.V.; Kulakovskaya, T.V.
Polyphosphates and polyphosphatase activity in the yeast Saccharomyces cerevisiae during overexpression of the DDP1 gene
Biochemistry
80
1312-1317
2015
Saccharomyces cerevisiae (Q99321), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q99321)
Manually annotated by BRENDA team
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 (P40152), Saccharomyces cerevisiae (Q04119), Saccharomyces cerevisiae (Q99321), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P40152), Saccharomyces cerevisiae ATCC 204508 (Q04119), Saccharomyces cerevisiae ATCC 204508 (Q99321)
Manually annotated by BRENDA team