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ATP + H2O
ADP + phosphate
cAMP + H2O
adenosine + phosphate
-
-
-
?
dATP + H2O
dADP + phosphate
diphosphate + H2O
2 phosphate
GTP + H2O
GDP + phosphate
guanosine tetraphosphate + H2O
guanosine triphosphate + phosphate
-
-
-
?
polyP750 + H2O
polyP749 + phosphate
-
-
-
-
?
polyphosphate + H2O
oligophosphate
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
-
?
additional information
?
-
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
-
-
-
?
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
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
polymetaphosphate
break down stops when the scission products are tetraphosphate or pentaphosphate
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
Chlamydomonas sp.
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
Pyrococcus islandicum
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
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
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate + H2O
oligophosphate
-
-
-
?
polyphosphate15 + H2O
?
-
-
-
?
polyphosphate15 + H2O
?
-
-
-
?
polyphosphate208 + H2O
?
-
-
-
?
polyphosphate208 + H2O
?
-
-
-
?
polyphosphate208 + H2O
?
-
-
-
?
polyphosphate208 + H2O
?
-
-
-
?
polyphosphate3 + H2O
?
-
-
-
?
polyphosphate3 + H2O
?
-
-
-
?
polyphosphate60 + H2O
?
-
-
-
?
polyphosphate60 + H2O
?
-
-
-
?
polyphosphate700 + H2O
?
-
-
-
?
polyphosphate700 + H2O
?
-
-
-
?
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
?
-
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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African Swine Fever
The g5R (D250) gene of African swine fever virus encodes a Nudix hydrolase that preferentially degrades diphosphoinositol polyphosphates.
Alopecia
Azathioprine-induced alopecia: rare adverse event early marker of myelotoxicity.
Alopecia
Thiopurines: Recent Topics and Their Role in the Treatment of Inflammatory Bowel Diseases.
Breast Neoplasms
Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells.
Carcinoma
NUDT1: A potential independent predictor for the prognosis of patients with oral squamous cell carcinoma.
Carcinoma, Hepatocellular
Nudix hydrolase 1 is a prognostic biomarker in hepatocellular carcinoma.
Cat-Scratch Disease
Structure of a Nudix hydrolase (MutT) in the Mg(2+)-bound state from Bartonella henselae, the bacterium responsible for cat scratch fever.
Infections
Genome sequence of a nephritogenic and highly transformable M49 strain of Streptococcus pyogenes.
Infections
InvA protein: a nudix hydrolase required for infection by pathogenic leptospira in cell lines and animals.
Infections
Oral vaccination of mice with Trichinella spiralis nudix hydrolase DNA vaccine delivered by attenuated Salmonella elicited protective immunity.
Infections
Retraction. InvA protein is a Nudix hydrolase required for infection by pathogenic Leptospira in cell lines and animals.
Infections
Subcellular localization of rickettsial invasion protein, InvA.
Inflammatory Bowel Diseases
NUDT15 C415T variant compared with TPMT genotyping in predicting azathioprine-induced leucopenia: prospective analysis of 1014 inflammatory bowel disease patients in India.
Leukemia
Development of a chemical probe against NUDT15.
Leukemia
[Effect of NUDT21 on Alternative Splicing of Transcripts in K562 Cells].
Leukopenia
An intronic FTO variant rs16952570 confers protection against thiopurine-induced myelotoxicities in multiethnic Asian IBD patients.
Leukopenia
Azathioprine-induced alopecia: rare adverse event early marker of myelotoxicity.
Leukopenia
Evolving Role of Thiopurines in Inflammatory Bowel Disease in the Era of Biologics and New Small Molecules.
Leukopenia
NUDT15 gene variants and thiopurine-induced leukopenia in patients with inflammatory bowel disease.
Leukopenia
Thiopurines: Recent Topics and Their Role in the Treatment of Inflammatory Bowel Diseases.
Neoplasms
High precision multi-genome scale reannotation of enzyme function by EFICAz.
Neoplasms
NUDT21 inhibits bladder cancer progression through ANXA2 and LIMK2 by alternative polyadenylation.
Neoplasms
The ADP-ribose reactive NUDIX hydrolase isoforms can modulate HIF-1? in cancer cells.
Obesity
The Obesity-Linked Gene Nudt3 Drosophila Homolog Aps Is Associated With Insulin Signaling.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Star Allele-Based Haplotyping versus Gene-Wise Variant Burden Scoring for Predicting 6-Mercaptopurine Intolerance in Pediatric Acute Lymphoblastic Leukemia Patients.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
The Role of TPMT, ITPA, and NUDT15 Variants during Mercaptopurine Treatment of Swedish Pediatric Patients with Acute Lymphoblastic Leukemia.
Squamous Cell Carcinoma of Head and Neck
NUDT1: A potential independent predictor for the prognosis of patients with oral squamous cell carcinoma.
Starvation
Derepression of polyphosphatase in Escherichia coli by starvation for inorganic phosphate.
Thrombosis
Localization of Short-Chain Polyphosphate Enhances its Ability to Clot Flowing Blood Plasma.
Trichinellosis
Molecular identification of Trichinella spiralis nudix hydrolase and its induced protective immunity against trichinellosis in BALB/c mice.
Trichinellosis
Serodiagnosis of trichinellosis by ELISA using recombinant nudix hydrolase of Trichinella spiralis.
Tuberculosis
Identification of Nudix Hydrolase Family Members with an Antimutator Role in Mycobacterium tuberculosis and Mycobacterium smegmatis.
Tuberculosis
Making sense of a missense mutation: characterization of MutT2, a Nudix hydrolase from Mycobacterium tuberculosis, and the G58R mutant encoded in W-Beijing strains of M. tuberculosis.
Tuberculosis
Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis.
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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
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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
-
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
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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
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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
-
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
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additional information
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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
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construction of Ppn1 mutants, overview
additional information
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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
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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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