Any feedback?
Information on EC 3.6.1.52 - diphosphoinositol-polyphosphate diphosphatase
for references in articles please use BRENDA:EC3.6.1.52Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.6.1.52 diphosphoinositol-polyphosphate diphosphataseIUBMB 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.
Specify your search results
Word Map
- 3.6.1.52
-
nudix
- dipps
-
diadenosine
- pentakisphosphate
- hexaphosphate
-
mutt
-
pp-insp5
- ap6a
-
5-phosphoribosyl
- tetrakisphosphate
- 1-pyrophosphate
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
diphosphoinositol polyphosphate phosphohydrolase, dipp2, dipp3, mudipp1, diphosphoinositol phosphohydrolase, diphosphoinositol phosphate phosphohydrolase, diphosphoinositol-polyphosphate phosphohydrolase, aps protein, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5PP-IP5 phosphatase
Aps protein
-
the Nudix hydrolase Aps is a product of the sole Drosophila melanogaster DIPP/Aps1/Ddp1-like gene CG6391
DDP1
diphosphoinositol phosphate phosphohydrolase
diphosphoinositol polyphosphate phosphatase
-
-
-
-
diphosphoinositol polyphosphate phosphohydrolase
diphosphoinositol-polyphosphate phosphohydrolase
-
-
-
-
DIPP
DIPP1
DIPP3
phosphatase, diphosphoinositol polyphosphate
-
-
-
-
Siw14
additional information
DIPP
-
-
-
-
additional information
see also EC 3.6.1.60 and EC 3.6.1.10
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
220324-74-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
-
-
-
r
5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-alpha-D-ribose 1-phosphate + phosphate
adenosine tetraphosphate + H2O
?
-
the substrate shows great hydrolysis by Aps
-
-
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
diadenosine 5',5'''-P1,P6-hexaphosphate + H2O
?
-
the substrate shows great hydrolysis by Aps
-
-
?
guanosine tetraphosphate + H2O
?
-
the substrate shows the greatest hydrolysis by Aps
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
reaction of EC 3.6.1.17
-
?
phosphatidylinositol 3,4,5-trisphosphate + H2O
?
-
poor substrate
-
-
?
phosphatidylinositol 3,4-bisphosphate + H2O
?
-
poor substrate
-
-
?
phosphatidylinositol 3,5-bisphosphate + H2O
?
-
poor substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-alpha-D-ribose 1-phosphate + phosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-alpha-D-ribose 1-phosphate + phosphate
not competes with diphosphoinositol pentakisphosphate
-
-
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
-
-
-
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
specificity constant of isoenzyme hDIPP3beta is 2.7fold higher than value for isoenzyme hDIPP3alpha
-
-
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
-
-
-
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
-
-
-
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
-
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
-
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
the diphosphate group that is attached to the 5-carbon is hydrolyzed, no release of diphosphate
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
isoenzyme hDIPP3beta is 2.3fold more active than isoenzyme hDIPP3alpha
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
-
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
-
regulation of stage of viral morphogenesis involving diphosphoinositol polyphosphate-mediated membrane trafficking
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
-
-
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
-
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
no activity with dGTP
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
vesicle trafficking, stress responses, DNA repair, apoptosis
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
metabolism of diphosphoinositol polyphosphate, not hydrolysis of diadenosine polyphosphates
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
preferred as substrate over diadenosine hexaphosphate
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
?
-
poor substrate
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
?
-
poor substrate
-
-
?
phosphatidylinositol 4-phosphate + H2O
?
-
poor substrate
-
-
?
additional information
?
-
-
no hydrolysis of diadenosine 5',5'''-P1,P3-polyphosphate, diadenosine 5',5'''-P1,P2-polyphosphate, ATP, ADP, dATP, diguanosine tetraphosphate, diguanosine triphosphate, diguanosine diphosphate, GTP, GDP, dGTP, P1-(5'-adenosyl) P5-(5'-guanosyl) polyphosphate, and P1-(5'-adenosyl) P4-(5'-guanosyl) polyphosphate
-
-
?
additional information
?
-
-
enzyme degrades Ap6A and Ap5A in preference to other diadenosine polyphosphates
-
-
?
additional information
?
-
-
the MuT domain of the enzyme participates in the hydrolysis of dATP, diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate
-
-
?
additional information
?
-
-
DIPP1, DIPP2 and DIPP3 are also capable of degrading polyphosphates
-
-
?
additional information
?
-
-
the MuT domain of the enzyme participates in the hydrolysis of dATP, diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate
-
-
?
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
?
-
-
no activity with inositol hexakisphosphate
-
-
-
additional information
?
-
endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
-
-
-
additional information
?
-
-
no activity with inositol hexakisphosphate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
-
-
-
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
-
regulation of stage of viral morphogenesis involving diphosphoinositol polyphosphate-mediated membrane trafficking
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
vesicle trafficking, stress responses, DNA repair, apoptosis
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
metabolism of diphosphoinositol polyphosphate, not hydrolysis of diadenosine polyphosphates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
-
Ca2+, Ni2+ or Zn2+ are ineffective in stimulating activity of Aps
Mn2+
-
divalent cation is required, 3 mM, pH 7.2, at 37ºC, 50% higher activity than Mg2+ at 10 to 15 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
inhibitory at 2 mM; inhibits the endopolyphophatase of the recombinant enzyme DDP1
diphosphate
inhibitory at 2 mM; inhibits the endopolyphophatase of the recombinant enzyme DDP1
F-
-
uncompetitive against bisdiphosphoinositol tetrakisphosphate, non-competitive against diphosphoinositol pentakisphosphate
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
competitive
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
phosphate
inhibitory at 2 mM; inhibits the endopolyphophatase of the recombinant enzyme DDP1
Triphosphate
inhibitory at 2 mM; inhibits the endopolyphophatase of the recombinant enzyme DDP1
additional information
ADP has no effect on the endopolyphophatase activity of recombinant DDP1
-
additional information
-
ADP has no effect on the endopolyphophatase activity of recombinant DDP1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
5-phospho-D-ribosyl 1-diphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
0.004
adenosine tetraphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
0.018
diadenosine 5',5'''-P1,P6-hexaphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
0.011
guanosine tetraphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
additional information
additional information
-
Km-values for hydrolysis of Ap6A and Ap5A
-
0.0000042
diphosphoinositol pentakisphosphate
-
isoenzyme hDIPP1 and hDIPP2alpha
0.00007
diphosphoinositol pentakisphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
5-phospho-D-ribosyl 1-diphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
0.24
adenosine tetraphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
0.34
diadenosine 5',5'''-P1,P6-hexaphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
0.8
guanosine tetraphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
additional information
additional information
-
turnover-numbers for hydrolysis of Ap6A and Ap5A
-
0.024
diphosphoinositol pentakisphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
5-phospho-D-ribosyl 1-diphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
60
adenosine tetraphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
19
diadenosine 5',5'''-P1,P6-hexaphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
342
diphosphoinositol pentakisphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
71
guanosine tetraphosphate
-
in the presence of 10 mM Mg2+, at pH 9.0 and 26°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00011
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
pH not specified in the publication, temperature not specified in the publication
0.00027
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
0.000023
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
pH 6.5: about 55% of maximal activity, pH 8.0: about 65% of maximal activity, hydrolysis of diphosphoinositol pentakisphosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.