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Information on EC 3.6.1.10 - endopolyphosphatase
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3.6.1.10 endopolyphosphataseIUBMB Comments
The product contains 4 or 5 phosphate residues.
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Word Map
- 3.6.1.10
- hydrolases
- adp-ribose
-
diadenosine
-
decapping
-
pyrophosphohydrolase
-
mutt
-
dinucleoside
-
diphosphoinositol
-
nudt15
- ap6a
- tripolyphosphate
- thiopurine
- pyrophosphatases
- tetraphosphate
- oligophosphate
- hexaphosphate
- 8-oxo-dgtp
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
nudix hydrolase, polyphosphatase, endopolyphosphatase, short-chain polyphosphate, tbnh4, yor163w, endopolypase, tbdcp2, polyphosphate depolymerase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DDP1
dual exo/endopolyphoshatase
endopolyphosphatase
Nudix hydrolase
Ppn1
Ppn2
TbDcp2
TbNH4
YDR452W
YNL217W
YOR163W
additional information
additional information
see also EC 3.6.1.60 and EC 3.6.1.52
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
polyphosphate + n H2O = (n+1) oligophosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
polyphosphate polyphosphohydrolase
The product contains 4 or 5 phosphate residues.
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CAS REGISTRY NUMBER
COMMENTARY
9024-86-6
-
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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
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
-
-
?
polyphosphate 208 + H2O
oligophosphate
-
-
the average polyphosphate chain lengths decrease from about 208 to about 10 phosphate residues
?
polyphosphate 208 + H2O
polyphosphate 193 + polyphosphate 15
-
-
-
?
polyphosphate3 + H2O
diphosphate + phosphate
-
-
?
polyphosphate700 + H2O
phosphate + triphosphate
progression via intermediate chain length polyphosphates
product analysis
?
ATP + H2O
ADP + phosphate
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
?
ATP + H2O
ADP + phosphate
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
?
dATP + H2O
dADP + phosphate
-
-
?
diphosphate + H2O
2 phosphate
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
?
diphosphate + H2O
2 phosphate
only in presence of Co2+, not with Mg2+, reaction of EC 3.6.1.1
-
?
polyphosphate + H2O
oligophosphate
-
polymetaphosphate
break down stops when the scission products are tetraphosphate or pentaphosphate
?
polyphosphate + H2O
oligophosphate
-
-
distributive action on polyP750 produces shorter chains to a limit of about polyP60 as well as the more abundant release of polyP3, limit digestion product is polyP3
?
additional information
?
-
-
inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
-
?
additional information
?
-
null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
-
?
additional information
?
-
-
null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
-
?
additional information
?
-
-
the pathway of particular polyphosphates in yeast is different with endo- and exopolyphosphatase playing critical roles
-
?
additional information
?
-
enzyme is a bifunctional exo- and endopolyphosphatase, activities of ECs 3.6.1.11 and 3.6.1.10, respectively. No activity with diphosphate, ATP and 4-nitrophenyl phosphate
-
?
additional information
?
-
-
enzyme is a bifunctional exo- and endopolyphosphatase, activities of ECs 3.6.1.11 and 3.6.1.10, respectively. No activity with diphosphate, ATP and 4-nitrophenyl phosphate
-
?
additional information
?
-
DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
-
DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
-
-
additional information
?
-
-
endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
-
-
additional information
?
-
Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
-
Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
-
Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn2 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
Ppn1 has endopolyphosphatase activity (EC 3.6.1.10), and high exopolyphosphatase activity (EC 3.6.1.11). The Ppn1 activity with guanosine tetraphosphate is nearly 80% of activity with long-chain polyphosphates. Ppn1 hydrolyzes dATP. Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
DPP1 has endopolyphosphatase activity (EC 3.6.1.10), and low exopolyphosphatase activity (EC 3.6.1.11). Exopolyphosphatases (polyphosphate phosphohydrolases) cleave phosphate from the end of the polyphosphate chain, whereas endopolyphosphatases (polyphosphate depolymerases) split long polyphosphate molecules into oligopolyphosphates
-
-
additional information
?
-
endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
-
-
additional information
?
-
TbNH4 is an endo- and exopolyphosphatase that has similar activity on polyP of various chain sizes. The enzyme has a higher affinity for polyP60 than for polyphosphate700. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). Malachite green assay
-
-
additional information
?
-
-
TbNH4 is an endo- and exopolyphosphatase that has similar activity on polyP of various chain sizes. The enzyme has a higher affinity for polyP60 than for polyphosphate700. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). Malachite green assay
-
-
additional information
?
-
Trypanosoma brucei 927/4 GUTat10.1
TbNH4 is an endo- and exopolyphosphatase that has similar activity on polyP of various chain sizes. The enzyme has a higher affinity for polyP60 than for polyphosphate700. No activity with 5-diphosphoinositol pentakisphosphate (5-IP7). Malachite green assay
-
-
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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
additional information
?
-
-
inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
-
-
?
additional information
?
-
null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
-
-
?
additional information
?
-
-
null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
-
-
?
additional information
?
-
-
the pathway of particular polyphosphates in yeast is different with endo- and exopolyphosphatase playing critical roles
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Zn2+
additional information
Co2+
stimulates the endopolyphosphatase activity at 0.01 mM
Co2+
stimulates the endopolyphosphatase activity at 0.1 mM
Mg2+
in the presence of Mg2+, the enzyme shows a polyphosphate chain fragmentation activity
Mg2+
stimulates the endopolyphosphatase activity at 1 mM
Zn2+
stimulates the endopolyphosphatase activity at 0.01 mM
Zn2+
stimulates the endopolyphosphatase activity at 0.1 mM
additional information
-
addition of 3 mM Mg2+ and 3 mM Co2+ has no effect on the cytosol endopolyphosphatase activity
additional information
Mg2+ or Mn2+ are the preferred cofactors while no activity is detected with Co2+
additional information
-
Mg2+ or Mn2+ are the preferred cofactors while no activity is detected with Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triphosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
ATP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
ATP
inhibits the endopolyphophatase of the recombinant enzyme DDP1
diphosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
heparin
inhibits the endopolyphosphatase activity by 50% at 0.01 mg/ml; inhibits the endopolyphosphatase activity slightly at 0.25 mg/ml
phosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
additional information
-
the enzyme is insensitive to 5 mM fluoride
-
additional information
ADP has no effect on the endopolyphophatase activity of recombinant DDP1
-
additional information
-
ADP has no effect on the endopolyphophatase activity of recombinant DDP1
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
ATP inhibits while ADP activates endopolyphosphatase activity in the presence of Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
80
purified recombinant enzyme, exopolyphosphatase activity in presence of 0.1 mM Co2+, substrate dATP, pH 7.2, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional exo- and endopolyphosphatase, EC 3.6.1.11 and EC 3.6.1.10
SwissProt
brenda
strain CRX, CRY, CRN, and CNX derived from strain W303-1A
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity is greater in mycorrhizal roots of Allium cepa than in non-mycorrhizal roots
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
the enzyme belongs to the endopolyphosphatase Ppn1 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
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
evolution
the enzyme belongs to the PPP superfamily of metallophosphatases. 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
evolution
the Nudix superfamily (Pfam PF00293) is found in archaea, bacteria, eukaryotes and viruses and includes pyrophosphohydrolases of nucleotide sugars and alcohols, nucleoside and deoxynucleoside triphosphates ([d]NTPs), dinucleoside polyphosphates, dinucleotide coenzymes and capped RNAs. Trypanosoma brucei has five Nudix hydrolases
evolution
-
the enzyme belongs to the PPP superfamily of metallophosphatases. 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
evolution
-
the enzyme belongs to the endopolyphosphatase Ppn1 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
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
evolution
Trypanosoma brucei 927/4 GUTat10.1
-
the Nudix superfamily (Pfam PF00293) is found in archaea, bacteria, eukaryotes and viruses and includes pyrophosphohydrolases of nucleotide sugars and alcohols, nucleoside and deoxynucleoside triphosphates ([d]NTPs), dinucleoside polyphosphates, dinucleotide coenzymes and capped RNAs. Trypanosoma brucei has five Nudix hydrolases
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
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
diphosphoinositol polyphosphate phosphohydrolase (DDP1, EC 3.6.1.52) is also a diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60) and shows endopolyphosphatase (EC 3.6.1.10) activity and exopolyphosphatase activity (EC 3.6.1.11)
metabolism
diphosphoinositol polyphosphate phosphohydrolase (DDP1, EC 3.6.1.52) is also a diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60) and shows endopolyphosphatase (EC 3.6.1.10) activity. The relationship between inositol pyrophosphate and polyphosphate metabolisms seems to be complicated
metabolism
the enzyme PPN1 shows exo- and endopolyphosphatase activities, EC 3.6.1.11 and EC 3.6.1.10, respectively
metabolism
-
the enzyme PPN1 shows exo- and endopolyphosphatase activities, EC 3.6.1.11 and EC 3.6.1.10, respectively
metabolism
-
diphosphoinositol polyphosphate phosphohydrolase (DDP1, EC 3.6.1.52) is also a diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60) and shows endopolyphosphatase (EC 3.6.1.10) activity and exopolyphosphatase activity (EC 3.6.1.11)
metabolism
-
diphosphoinositol polyphosphate phosphohydrolase (DDP1, EC 3.6.1.52) is also a diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60) and shows endopolyphosphatase (EC 3.6.1.10) activity. The relationship between inositol pyrophosphate and polyphosphate metabolisms seems to be complicated
physiological function
NHs can participate in polyphosphate homeostasis and therefore may help control polyphosphate levels in glycosomes, cytosol and nuclei of Trypanosoma brucei. Endopolyphosphatase (PPN) activity cleaves internal phosphoanhydride bonds generating shorter polyphosphate molecules. Nudix hydrolase 4 (TbNH4 or TbDcp2) is a mRNA de-capping enzyme that removes the 5' cap from processed mRNAs
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
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
physiological function
Trypanosoma brucei 927/4 GUTat10.1
-
NHs can participate in polyphosphate homeostasis and therefore may help control polyphosphate levels in glycosomes, cytosol and nuclei of Trypanosoma brucei. Endopolyphosphatase (PPN) activity cleaves internal phosphoanhydride bonds generating shorter polyphosphate molecules. Nudix hydrolase 4 (TbNH4 or TbDcp2) is a mRNA de-capping enzyme that removes the 5' cap from processed mRNAs
Show AA Sequence and Transmembrane Helices (857 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34500
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
monomer
tetramer
4 * 34500, native enzyme, SDS-PAGE and mass spectrometry
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
both the C-terminus and the N-terminus of Ppn1 are cleaved during enzyme activation
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
additional information
null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
additional information
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null mutants in Ppn1 accumulate long-chain polyphosphates and are defective in growth in minimal media
additional information
construction of Ppn1 mutants, overview
additional information
-
inactivation of gene ppn1 encoding the endopolyphosphatase PPN1 togehther with inactivation of exopolyphosphatase PPX1 leads to a two-fold increase in high-molecular weight alkali-soluble polyphosphates in yeast cells
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 DELTAdpp1, 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 DELTAdpp1, 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 DELTAdpp1, 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 DELTAdpp1, 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 DELTAppn1, 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 DELTAppn1, 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 DELTAppn1, 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 DELTAppn1, 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 DELTAppn2, 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 DELTAppn2, 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 DELTAppn2, 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 DELTAppn2, that shows increased polyphosphate levels
additional information
overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively
additional information
-
overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively
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 DELTAppn2, 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 DELTAppn1, 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 DELTAdpp1, that shows increased polyphosphate levels
additional information
-
overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Toyopearl 650M column chromatography, heparin agarose column chromatography, and Mono Q column chromatography
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native enzyme from exopolyphosphatase-deficient mutant strain CRX by heparin affinity and phosphocellulose chromatography, 3820fold to homogeneity
recombinant enzyme DPP1 from Saccharomyces cerevisiae strain CRN by anion exchange chromatography and ultrafiltration
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
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography and dialysis
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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
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
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malmgren, H.
Enzymatic breakdown of polymetaphosphate V. Purification and specificity of the enzyme
Acta Chem. Scand.
6
16-26
1952
Aspergillus niger
-
brenda
Capaccio, L.C.M.; Callow, J.A.
The enzymes of polyphosphate metabolism in vesicular-arbuscular mycorrhizas
New Phytol.
91
81-91
1982
Funneliformis mosseae
-
brenda
Kritsky, M.S.; Chernyshova, E.K.
The study of polyphosphate depolymerase activity of Neurospora crassa
React. Mech. Control Prop. Phosphotransferases, Int. Symp. Meeting, Akad. Verl. Berlin
49-56
1971
Neurospora crassa, Neurospora crassa 28610
-
brenda
Kowalczyk, T.H.; Phillips, N.F.B.
Determination of endopolyphosphatase using polyphosphate glucokinase
Anal. Biochem.
212
194-205
1993
Saccharomyces cerevisiae
brenda
Kumble, K.; Kornberg, A.
Endopolyphosphatase for long chain inorganic polyphosphate in yeast and mammals
J. Biol. Chem.
271
27146-27151
1996
Saccharomyces cerevisiae, Caenorhabditis elegans, Chlamydomonas sp., Dictyostelium discoideum, Drosophila melanogaster, Giardia intestinalis, Neurospora crassa, Phaeodactylum tricornutum, Pyrococcus islandicum, Rattus norvegicus, Sulfolobus acidocaldarius, Synechococcus sp.
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
Cordeiro, C.D.; Ahmed, M.A.; Windle, B.; Docampo, R.
NUDIX hydrolases with inorganic polyphosphate exo- and endopolyphosphatase activities in the glycosome, cytosol and nucleus of Trypanosoma brucei
Biosci. Rep.
39
BSR20190894
2019
Trypanosoma brucei (Q583R7), Trypanosoma brucei, Trypanosoma brucei 927/4 GUTat10.1 (Q583R7)
brenda
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