3.6.1.52: diphosphoinositol-polyphosphate diphosphatase
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For detailed information about diphosphoinositol-polyphosphate diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.52
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3.6.1.52
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nudix
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dipps
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diadenosine
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pentakisphosphate
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hexaphosphate
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mutt
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pp-insp5
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ap6a
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5-phosphoribosyl
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tetrakisphosphate
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1-pyrophosphate
- 3.6.1.52
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nudix
- dipps
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diadenosine
- pentakisphosphate
- hexaphosphate
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mutt
-
pp-insp5
- ap6a
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5-phosphoribosyl
- tetrakisphosphate
- 1-pyrophosphate
Reaction
Synonyms
5PP-IP5 phosphatase, Aps protein, D250, DDP1, diphosphoinositol phosphate phosphohydrolase, diphosphoinositol phosphohydrolase, diphosphoinositol polyphosphate phosphatase, diphosphoinositol polyphosphate phosphohydrolase, diphosphoinositol polyphosphate phosphohydrolase 1, diphosphoinositol-polyphosphate phosphohydrolase, DIPP, DIPP1, DIPP2, DIPP3, g5Rp, More, muDIPP1, phosphatase, diphosphoinositol polyphosphate, poly-P endopolyphosphatase, Siw14
ECTree
3.6.1.52 diphosphoinositol-polyphosphate diphosphataseAdvanced search results
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General Information on EC 3.6.1.52 - diphosphoinositol-polyphosphate diphosphatase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
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
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
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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
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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
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