The taxonomic range for the selected organisms is: Saccharomyces cerevisiae The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
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
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
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
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
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
inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
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
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
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
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
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
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
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
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
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
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
inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
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
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
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
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
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
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
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
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
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
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
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
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
inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1
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
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
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
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
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
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
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
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
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
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
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
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
The effect of inactivation of the exo- and endopolyphosphatase genes PPX1 and PPN1 on the level of different polyphosphates in the yeast Saccharomyces cerevisiae