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Information on EC 3.6.1.52 - diphosphoinositol-polyphosphate diphosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q99321

for references in articles please use BRENDA:EC3.6.1.52
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IUBMB Comments
This enzyme hydrolyses the diphosphate bond, leaving a phospho group where a diphospho group had been. It can also act on bis(adenosine) diphosphate.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q99321
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
diphosphoinositol polyphosphate phosphohydrolase, dipp2, dipp3, mudipp1, diphosphoinositol-polyphosphate phosphohydrolase, aps protein, diphosphoinositol phosphohydrolase, diphosphoinositol phosphate phosphohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphoinositol polyphosphate phosphohydrolase
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5PP-IP5 phosphatase
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-
diphosphoinositol phosphate phosphohydrolase
-
-
diphosphoinositol polyphosphate phosphatase
-
-
-
-
diphosphoinositol-polyphosphate phosphohydrolase
-
-
-
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DIPP
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-
-
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phosphatase, diphosphoinositol polyphosphate
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-
-
-
additional information
see also EC 3.6.1.60 and EC 3.6.1.10
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
diphospho-myo-inositol-polyphosphate diphosphohydrolase
This enzyme hydrolyses the diphosphate bond, leaving a phospho group where a diphospho group had been. It can also act on bis(adenosine) diphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
220324-74-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
show the reaction diagram
-
-
-
?
polyP15 + H2O
polyP14 + phosphate
show the reaction diagram
-
-
-
?
polyP208 + H2O
polyP207 + phosphate
show the reaction diagram
-
-
-
?
polyphosphate15 + H2O
?
show the reaction diagram
-
-
-
?
polyphosphate208 + H2O
?
show the reaction diagram
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
5-diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
show the reaction diagram
-
-
-
-
r
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol 3,4,5-trisphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
phosphatidylinositol 3,4-bisphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
phosphatidylinositol 3,5-bisphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
phosphatidylinositol 3-phosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
phosphatidylinositol 4-phosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
phosphatidylinositol 5-phosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
polyphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
show the reaction diagram
-
-
-
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required, activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
phosphate
Triphosphate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
4-nitrophenyl phosphate
-
at pH 6.0 and 37°C
0.035
5-diphosphoinositol pentakisphosphate
-
at pH 6.0 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000044
4-nitrophenyl phosphate
-
at pH 6.0 and 37°C
0.0025
5-diphosphoinositol pentakisphosphate
-
at pH 6.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
4-nitrophenyl phosphate
-
at pH 6.0 and 37°C
0.074
5-diphosphoinositol pentakisphosphate
-
at pH 6.0 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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. The relationship between inositol pyrophosphate and polyphosphate metabolisms seems to be complicated
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C214S
-
inactive
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-agarose resin column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expressed in Escherichia coli Rosetta(DE3)pLysS cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
Steidle, E.A.; Chong, L.S.; Wu, M.; Crooke, E.; Fiedler, D.; Resnick, A.C.; Rolfes, R.J.
A novel inositol pyrophosphate phosphatase in Saccharomyces cerevisiae Siw14 protein selectively cleaves the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5)
J. Biol. Chem.
291
6772-6783
2016
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team