EC Number   |
General Information |
Reference |
|---|
   3.6.1.10 | 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 |
-, 756125 |
| 3.6.1.10 | 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 |
-, 756125 |
| 3.6.1.10 | 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 |
-, 756125 |
| 3.6.1.10 | 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 |
-, 756231 |
| 3.6.1.10 | 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 |
-, 756069 |
| 3.6.1.10 | 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) |
-, 756125 |
| 3.6.1.10 | 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 |
-, 756069 |
| 3.6.1.10 | metabolism |
the enzyme PPN1 shows exo- and endopolyphosphatase activities, EC 3.6.1.11 and EC 3.6.1.10, respectively |
-, 756125 |
| 3.6.1.10 | 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 |
-, 756231 |
| 3.6.1.10 | 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 |
-, 756069 |
