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Information on EC 3.6.1.52 - diphosphoinositol-polyphosphate diphosphatase
for references in articles please use BRENDA:EC3.6.1.52
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.52 diphosphoinositol-polyphosphate diphosphatase
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.
The enzyme appears in viruses and cellular organisms
- 3.6.1.52
-
nudix
- dipps
-
diadenosine
- pentakisphosphate
- hexaphosphate
-
mutt
-
pp-insp5
- ap6a
-
5-phosphoribosyl
- tetrakisphosphate
- 1-pyrophosphate
Reaction Schemes
showSynonyms
diphosphoinositol polyphosphate phosphohydrolase, dipp2, dipp3, mudipp1, diphosphoinositol-polyphosphate phosphohydrolase, aps protein, diphosphoinositol phosphohydrolase, diphosphoinositol phosphate phosphohydrolase, more
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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
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
220324-74-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate + H2O
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate + phosphate
Substrates: best substrate tested
Products: -
Products: -
?
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate + H2O
1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
2-diphosphoinositol 1,3,4,5,6-pentakisphosphate + H2O
1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
4-diphosphoinositol 1,2,3,5,6-pentakisphosphate + H2O
1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate + H2O
1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
5-diphosphoinositol 1,3,4,6-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4,5,6-pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-alpha-D-ribose 1-phosphate + phosphate
adenosine tetraphosphate + H2O
?
-
Substrates: the substrate shows great hydrolysis by Aps
Products: -
Products: -
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
diadenosine 5',5'''-P1,P5-pentaphosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
diadenosine 5',5'''-P1,P6-hexaphosphate + H2O
?
-
Substrates: the substrate shows great hydrolysis by Aps
Products: -
Products: -
?
diadenosine 5',5''-P1,P6-hexaphosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
diguanosine pentaphosphate + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
guanosine tetraphosphate + H2O
?
-
Substrates: the substrate shows the greatest hydrolysis by Aps
Products: -
Products: -
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
Substrates: -
Products: reaction of EC 3.6.1.17
Products: reaction of EC 3.6.1.17
?
phosphatidylinositol 3,4,5-trisphosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
phosphatidylinositol 3,4-bisphosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
phosphatidylinositol 3,5-bisphosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
phosphatidylinositol 4,5-bisphosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
phosphatidylinositol 4-phosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
phosphatidylinositol 5-phosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
polyP15 + H2O
polyP14 + phosphate
Substrates: -
Products: -
Products: -
?
polyP208 + H2O
polyP207 + phosphate
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-galactosamine + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
5-diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
r
5-diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
r
5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-alpha-D-ribose 1-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-alpha-D-ribose 1-phosphate + phosphate
Substrates: not competes with diphosphoinositol pentakisphosphate
Products: -
Products: -
?
bisdiphosphoinositol tetrakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
bisdiphosphoinositol tetrakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
Substrates: specificity constant of isoenzyme hDIPP3beta is 2.7fold higher than value for isoenzyme hDIPP3alpha
Products: -
Products: -
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
Substrates: the diphosphate group that is attached to the 5-carbon is hydrolyzed, no release of diphosphate
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
Substrates: isoenzyme hDIPP3beta is 2.3fold more active than isoenzyme hDIPP3alpha
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
-
Substrates: regulation of stage of viral morphogenesis involving diphosphoinositol polyphosphate-mediated membrane trafficking
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
Substrates: vesicle trafficking, stress responses, DNA repair, apoptosis
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
Substrates: no activity with dGTP
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
Substrates: metabolism of diphosphoinositol polyphosphate, not hydrolysis of diadenosine polyphosphates
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
Substrates: preferred as substrate over diadenosine hexaphosphate
Products: -
Products: -
?
phosphatidylinositol 3-phosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
phosphatidylinositol 3-phosphate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
polyphosphate208 + H2O
?
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme degrades Ap6A and Ap5A in preference to other diadenosine polyphosphates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the MuT domain of the enzyme participates in the hydrolysis of dATP, diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: DIPP1, DIPP2 and DIPP3 are also capable of degrading polyphosphates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme specifically targets the C1 position of 1-InsP7 and 1,5-InsP8
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with ATP
Products: -
Products: -
?
additional information
?
-
-
Substrates: the MuT domain of the enzyme participates in the hydrolysis of dATP, diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
Products: -
Products: -
?
additional information
?
-
-
Substrates: endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with inositol hexakisphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with inositol hexakisphosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
Substrates: -
Products: -
Products: -
?
diphospho-myo-inositol polyphosphate + H2O
myo-inositol polyphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
-
Substrates: regulation of stage of viral morphogenesis involving diphosphoinositol polyphosphate-mediated membrane trafficking
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
Substrates: vesicle trafficking, stress responses, DNA repair, apoptosis
Products: -
Products: -
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
Substrates: metabolism of diphosphoinositol polyphosphate, not hydrolysis of diadenosine polyphosphates
Products: -
Products: -
?
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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
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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
-
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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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.237
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
0.165
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
0.042
2-diphosphoinositol 1,3,4,5,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
-
0.029
4-diphosphoinositol 1,2,3,5,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
0.081
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
0.095
5-diphosphoinositol 1,3,4,6-tetrakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
460
2-diphosphoinositol 1,3,4,5,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
-
210
4-diphosphoinositol 1,2,3,5,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
380
5-diphosphoinositol 1,3,4,6-tetrakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
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
50
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate
mutant K18A, pH 7.2, temperature not specified in the publication
110
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate
mutant H42A/R45A, pH 7.2, temperature not specified in the publication
520
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate
mutant H42A, pH 7.2, temperature not specified in the publication
540
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate
mutant R45A, pH 7.2, temperature not specified in the publication
590
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate
mutant R41A, pH 7.2, temperature not specified in the publication
1500
1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
70
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate
mutant K18A, pH 7.2, temperature not specified in the publication
200
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate
mutant H42A/R45A, pH 7.2, temperature not specified in the publication
680
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate
mutant H42A, pH 7.2, temperature not specified in the publication
690
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate
mutant R41A, pH 7.2, temperature not specified in the publication
860
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate
mutant R45A, pH 7.2, temperature not specified in the publication
1790
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
40
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
mutant K18A, pH 7.2, temperature not specified in the publication
80
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
mutant H42A/R45A, pH 7.2, temperature not specified in the publication
150
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
mutant H42A, pH 7.2, temperature not specified in the publication
230
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
mutant R41A, pH 7.2, temperature not specified in the publication
300
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
mutant R45A, pH 7.2, temperature not specified in the publication
650
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
wild-type, pH 7.2, temperature not specified in the publication
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
plants defective in DDP1 exhibit elevated levels of 1/3-InsP7 and 1/3,5-InsP8. DDP1 controls thallus development and vegetative reproduction in Marchantia polymorpha. Upon expression in Saccharomyces cerevisiae, DDP1 can rescue the DELTAddp1-associated growth defects on H2O2. Expression in the leaves of Nicotiana benthamiana affects the accumulation of the InsP7 band
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
-
Show AA Sequence and Transmembrane Helices (5557 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray analysis of the catalytic core of DIPP1 in crystals complexed with either natural PP-InsPs, alternative PP-InsP stereoisomers, or non-hydrolysable methylene bisphosphonate analogs. In a V-shaped catalytic furrow with overhanging ridges constructed from flexible positively charged side chains, the labile phosphoanhydride bond is appropriately positioned at the catalytic site by an extensive series of interlocking polar contacts
structure in the presence of multiple inositide ligands and synthetic analogs. The inositide binds strongly to the active site producing at least 15 polar interactions with the enzyme, mostly with basic residues
structures in complex with diphosphoinositide, dinucleotide, and polyphosphate substrates
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E66Q
-
no significant activity towards diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate, activity with diadenosine 5',5'''-P1,P6-hexaphosphate is 2% of the activity of the wild-type enzyme
E70Q
F84Y
-
hydrolysis of bisdiphosphoinositol tetrakisphosphate at 63% of the activity of the wild-type enzyme, hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate is 75% of the activity of the wild-type enzyme, activity with diphosphoinositol pentakisphosphate is only slightly reduced
G50A
-
hydrolysis of diphosphoinositol polyphosphates is more than 85% less than that of the wild-type enzyme
G52A
-
hydrolysis of diphosphoinositol polyphosphates is more than 85% less than that of the wild-type enzyme
G72A
-
catalytic activity towards bisdiphosphoinositol tetrakisphosphate, diadenosine 5',5'''-P1,P6-hexaphosphateand diphosphoinositol pentakisphosphate is impaired by more than 95%
G75A
-
catalytic activity towards bisdiphosphoinositol tetrakisphosphate, diadenosine 5',5'''-P1,P6-hexaphosphateand diphosphoinositol pentakisphosphate is impaired by more than 95%
G78A
-
catalytic activity and CD spectrum is not significantly different from that of the wild.type enzyme
H91L
-
hydrolysis of bisdiphosphoinositol tetrakisphosphate at 4% of the activity of the wild-type enzyme, hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate is 26% of the activity of the wild-type enzyme, activity with diphosphoinositol pentakisphosphate is only slightly reduced
K18A
E70Q
-
greatly reduced rate of hydrolysis of diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate
E80Q
mutation impedes the metal coordination and the catalysis, no effect on substrate binding
E83A
mutation impedes the metal coordination and the catalysis, no effect on substrate binding
K63A
R102A
R171S
R32A
additional information
E70Q
-
inactive against dATP,diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate
K63A
prominent increase in thermal stability in the free state, marked decrease in thermal stabilization upon InsP6 binding
K63A
mutant shows increases in thermal stability in the free state, displays a marked decrease in thermal stabilization upon InsP6 binding as compared to the wild-type, displays less thermal stabilization upon binding of polyphosphates than the wild-type
R102A
marked decrease in thermal stabilization upon InsP6 binding
R102A
displays a marked decrease in thermal stabilization upon InsP6 binding as compared to the wild-type, displays less thermal stabilization upon binding of polyphosphates than the wild-type
R171S
prominent increase in thermal stability in the free state, marked decrease in thermal stabilization upon InsP6 binding
R171S
mutant shows increases in thermal stability in the free state, displays a marked decrease in thermal stabilization upon InsP6 binding as compared to the wild-type, displays less thermal stabilization upon binding of polyphosphates than the wild-type
R32A
marked decrease in thermal stabilization upon InsP6 binding
R32A
displays a marked decrease in thermal stabilization upon InsP6 binding as compared to the wild-type
additional information
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
additional information
-
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
additional information
on removing the protein insertion (nose) specific to yeast enzymes, protein retains catalytic activity and shows increases in thermal stability in the free state. The mutant displays less thermal stabilization upon binding of polyphosphates than the wild-type and some effect on inositide and Ap5A binding
additional information
-
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
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dithiothreitol
-
in the absence of dithiothreitol a 5 min pretreatment at 36°C lowers enzyme activity by 65%, with temperatures above 56°C virtually abolishing all activity, whereas in the presence of dithiothreitol a 5 min treatment at temperatures up to 76°C is without effect
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, by nickel-nitrilotriacetic acid-agarose chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells as a hexahistidine-tagged fusion protein
-
expression in Escherichia coli
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Aps expression is highest in embryos and declines throughout development
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Safrany, S.T.; Caffrey, J.J.; Yang, X.; Bembenek, M.E.; Moyer, M.B.; Burkhart, W.A.; Shears, S.B.
A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase
EMBO J.
17
6599-6607
1998
Rattus norvegicus, Homo sapiens
brenda
Safrany, S.T.; Ingram, S.W.; Cartwright, J.L.; Falck, J.R.; McLennan, A.G.; Barnes, L.D.; Shears, S.B.
The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein
J. Biol. Chem.
274
21735-21740
1999
Homo sapiens
brenda
Yang, X.; Safrany, S.T.; Shears, S.B.
Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates
J. Biol. Chem.
274
35434-35440
1999
Homo sapiens
brenda
Caffrey, J.J.; Safrany, S.T.; Yang, X.; Shears, S.B.
Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding NUDT family
J. Biol. Chem.
275
12730-12736
2000
Homo sapiens
brenda
Hua, L.V.; Hidaka, K.; Pesesse, X.; Barnes, L.D.; Shears, S.B.
Paralogous murine Nudt10 and Nudt11 genes have differential expression patterns but encode identical proteins that are physiologically competent diphosphoinositol polyphosphate phosphohydrolases
Biochem. J.
373
81-89
2003
Mus musculus (P0C028), Mus musculus
brenda
Hidaka, K.; Caffrey, J.J.; Hua, L.; Zhang, T.; Falck, J.R.; Nickel, G.C.; Carrel, L.; Barnes, L.D.; Shears, S.B.
An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase
J. Biol. Chem.
277
32730-32738
2002
Homo sapiens (P07202), Homo sapiens (Q96G61), Homo sapiens
brenda
Cartwright, J.L.; Safrany, S.T.; Dixon, L.K.; Darzynkiewicz, E.; Stepinski, J.; Burke, R.; McLennan, A.G.
The g5R (D250) gene of African swine fever virus encodes a Nudix hydrolase that preferentially degrades diphosphoinositol polyphosphates
J. Virol.
76
1415-1421
2002
African swine fever virus
brenda
Chu, C.; Alapat, D.; Wen, X.; Timo, K.; Burstein, D.; Lisanti, M.; Shears, S.; Kohtz, D.S.
Ectopic expression of murine diphosphoinositol polyphosphate phosphohydrolase 1 attenuates signaling through the ERK1/2 pathway
Cell. Signal.
16
1045-1059
2004
Mus musculus
brenda
Winward, L.; Whitfield, W.G.; McLennan, A.G.; Safrany, S.T.
Oxidation of the diphosphoinositol polyphosphate phosphohydrolase-like Nudix hydrolase Aps from Drosophila melanogaster induces thermolability--A possible regulatory switch?
Int. J. Biochem. Cell Biol.
42
1174-1181
2010
Drosophila melanogaster
brenda
Lonetti, A.; Szijgyarto, Z.; Bosch, D.; Loss, O.; Azevedo, C.; Saiardi, A.
Identification of an evolutionarily conserved family of inorganic polyphosphate endopolyphosphatases
J. Biol. Chem.
286
31966-31974
2011
Homo sapiens
brenda
Wu, M.; Chong, L.S.; Capolicchio, S.; Jessen, H.J.; Resnick, A.C.; Fiedler, D.
Elucidating diphosphoinositol polyphosphate function with nonhydrolyzable analogues
Angew. Chem. Int. Ed. Engl.
53
7192-7197
2014
Homo sapiens (O95989)
brenda
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)
brenda
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
brenda
Chalak, K.; Yadav, R.; Liu, G.; Rana, P.; Jessen, H.J.; Laha, D.
Functional conservation of the DDP1-type inositol pyrophosphate phosphohydrolases in land plant
Biochemistry
63
2723-2728
2024
Marchantia polymorpha subsp. ruderalis (A0AAF6BFM7)
brenda
Zong, G.; Jork, N.; Hostachy, S.; Fiedler, D.; Jessen, H.J.; Shears, S.B.; Wang, H.
New structural insights reveal an expanded reaction cycle for inositol pyrophosphate hydrolysis by human DIPP1
FASEB J.
35
e21275
2021
Homo sapiens (O95989)
brenda
Marquez-Monino, M.A.; Ortega-Garcia, R.; Shipton, M.L.; Franco-Echevarria, E.; Riley, A.M.; Sanz-Aparicio, J.; Potter, B.V.L.; Gonzalez, B.
Multiple substrate recognition by yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase through phosphate clamping
Sci. Adv.
7
eabf6744
2021
Saccharomyces cerevisiae (Q99321)
brenda
EXTERNAL LINKS (specific for EC-Number 3.6.1.52)
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