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Information on EC 3.1.3.57 - inositol-1,4-bisphosphate 1-phosphatase and Organism(s) Rattus norvegicus and UniProt Accession Q9Z1N4

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.57 inositol-1,4-bisphosphate 1-phosphatase
IUBMB Comments
The enzyme acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar Vmax values for both substrates, but with a five-times higher affinity for the bisphosphate. Does not act on inositol 1-phosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q9Z1N4
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
inositol polyphosphate 1-phosphatase, inositol polyphosphate-1-phosphatase, rnpip, inositol-1,4-bisphosphate 1-phosphatase, inositol-polyphosphate 1-phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inositol-polyphosphate 1-phosphatase
-
-
-
-
INPP
-
-
-
-
IPP
-
-
-
-
IPPase
-
-
-
-
phosphatase, inositol 1,4-bisphosphate 1-
-
-
-
-
RnPIP
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
show the reaction diagram
mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-1,4-bisphosphate 1-phosphohydrolase
The enzyme acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar Vmax values for both substrates, but with a five-times higher affinity for the bisphosphate. Does not act on inositol 1-phosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
111070-17-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-phosphoadenosine 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
?
3'-phosphoadenosine 5'-phosphate + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
?
show the reaction diagram
-
-
-
?
D-myo-inositol 1,3,4-trisphosphate + H2O
D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
show the reaction diagram
-
-
?
D-myo-inositol 1,3,4-trisphosphate + H2O
D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
show the reaction diagram
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
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
show the reaction diagram
additional information
?
-
-
involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
strictily dependent on
Mg2+
-
requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
inositol 1,4-bisphosphate
-
inositol 1,3,4-trisphosphate as substrate
Mg2+
-
inhibition above 4 mM, activates below
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
inositol 1,4-bisphosphate
30°C, pH 7.5
0.02
inositol 1,3,4-trisphosphate
-
37°C
0.0009 - 0.0178
inositol 1,4-bisphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.9
-
about half-maximal activity at pH 7 and pH 7.9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular distribution
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BPNT1_RAT
308
0
33174
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
-
gel filtration
58000
-
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with AMP, phosphate and Mg2+
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
t1/2: 80 s, in crude cytosolic fraction
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kirk, C.J.; Michell, R.H.; Parry, J.B.; Shears, S.B.
Inositol trisphosphate and tetrakisphosphate phosphomonoesterases of rat liver
Biochem. Soc. Trans.
15
28-32
1987
Rattus norvegicus
Manually annotated by BRENDA team
Moyer, J.D.; Reizes, O.; Dean, N.M.; Malinowski, N.
D-myo-inositol (1,4)-bisphosphate 1-phosphate. Partial purification from rat liver and characterization
Biochem. Biophys. Res. Commun.
146
1018-1026
1987
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Morris, A.J.; Storey, D.J.; Downes, P.; Michell, R.H.
Dephosphorylation of 1D-myo-inositol 1,4-bisphosphate in rat liver
Biochem. J.
254
655-660
1988
Rattus norvegicus
Manually annotated by BRENDA team
Ruiz-Larrea, F.; Drummond, A.H.
Pathways of dephosphorylation of 1-D-myo-inositol 1,4,5-trisphosphate in GH3 pituitary tumor cells
Biochim. Biophys. Acta
1178
63-72
1993
Rattus norvegicus
Manually annotated by BRENDA team
Lopez-Coronado, J.M.; Belles, J.M.; Lesage, F.; Serrano, R.; Rodriguez, P.L.
A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3'-phosphoadenosine 5'-phosphate phosphatase and inositol-polyphosphate 1-phosphatase
J. Biol. Chem.
274
16034-16039
1999
Rattus norvegicus (Q9Z1N4), Rattus norvegicus
Manually annotated by BRENDA team
Patel, S.; Yenush, L.; Rodriguez, P.L.; Serrano, R.; Blundell, T.L.
Crystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a novel target of lithium therapy
J. Mol. Biol.
315
677-685
2002
Rattus norvegicus (Q9Z1N4), Rattus norvegicus
Manually annotated by BRENDA team
Woodcock, E.A.; Wang, B.H.; Arthur, J.F.; Lennard, A.; Matkovich, S.J.; Du, X.J.; Brown, J.H.; Hannan, R.D.
Inositol polyphosphate 1-phosphatase is a novel antihypertrophic factor
J. Biol. Chem.
277
22734-22742
2002
Rattus norvegicus
Manually annotated by BRENDA team