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Information on EC 3.6.1.52 - diphosphoinositol-polyphosphate diphosphatase and Organism(s) Homo sapiens and UniProt Accession P07202

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:
Homo sapiens
UNIPROT: P07202
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
-
DIPP3
isoenzyme hDIPP3alpha
diphosphoinositol phosphohydrolase
-
-
diphosphoinositol polyphosphate phosphatase
-
-
-
-
diphosphoinositol polyphosphate phosphohydrolase
-
diphosphoinositol-polyphosphate phosphohydrolase
-
-
-
-
DIPP
-
-
-
-
DIPP1
DIPP2
-
isoform
DIPP3
phosphatase, diphosphoinositol polyphosphate
-
-
-
-
poly-P endopolyphosphatase
-
-
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
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
show the reaction diagram
-
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
show the reaction diagram
-
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
show the reaction diagram
bisdiphosphoinositol tetrakisphosphate + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
bisdiphosphoinositol tetrakisphosphate + H2O
diphosphoinositol pentakisphosphate + phosphate
show the reaction diagram
specificity constant of isoenzyme hDIPP3beta is 2.7fold higher than value for isoenzyme hDIPP3alpha
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
-
-
?
diadenosine 5',5''-P1,P6-hexaphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
diphosphoinositol pentakisphosphate + H2O
inositol hexakisphosphate + phosphate
show the reaction diagram
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
show the reaction diagram
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
show the reaction diagram
-
reaction of EC 3.6.1.17
-
?
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
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
show the reaction diagram
vesicle trafficking, stress responses, DNA repair, apoptosis
-
-
?
diphosphoinositol polyphosphate + H2O
inositol polyphosphate + phosphate
show the reaction diagram
vesicle trafficking, stress responses, DNA repair, apoptosis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000042 - 0.0000048
diphosphoinositol pentakisphosphate
additional information
additional information
-
Km-values for hydrolysis of Ap6A and Ap5A
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.2
diphosphoinositol pentakisphosphate
additional information
additional information
-
turnover-numbers for hydrolysis of Ap6A and Ap5A
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
hydrolysis of diphosphoinositol pentakisphosphate
9
-
hydrolysis of dATP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
pH 6.5: about 55% of maximal activity, pH 8.0: about 65% of maximal activity, hydrolysis of diphosphoinositol pentakisphosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PERT_HUMAN
933
1
102963
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
recombinant enzyme, SDS-PAGE
19500
-
x * 19500, calculation from nucleotide sequence
20434
-
x * 20434, calculation from nucleotide sequence
25000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
-
no modification
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P89R
codes for isoenzyme hDIPP3beta
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
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
G82A
-
mutation promotes some unraveling of the normal secondary structure
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, by TALON metal affinity chromatography
recombinant enzyme, by TALON metal affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
isoenzyme hDIPP2alpha and hDIPP2beta
-
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
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team