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Information on EC 3.1.3.57 - inositol-1,4-bisphosphate 1-phosphatase
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3.1.3.57 inositol-1,4-bisphosphate 1-phosphataseIUBMB 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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Word Map
- 3.1.3.57
- lithium
-
monophosphatase
- 1,3,4-trisphosphate
-
nucleotidase
- li+
-
manic-depressive
- fiery1
-
1,6-bisphosphatase
-
3'2',5'-bisphosphate
-
majerus
- 3'-phosphoadenosine
-
lithium-sensitive
- phosphoinositols
- molecular biology
- 3,4-bisphosphate
-
li+-sensitive
- manic
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
inositol polyphosphate 1-phosphatase, inositol polyphosphate-1-phosphatase, inositol-1,4-bisphosphate 1-phosphatase, inositol-polyphosphate 1-phosphatase, INPP, IPP, IPPase, phosphatase, inositol 1,4-bisphosphate 1-, RnPIP, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
inositol polyphosphate 1-phosphatase
inositol polyphosphate-1-phosphatase
dual enzymatic activity: 3'(2'),5'-bisphosphate nucleosidase, gene FRY1, FIERY1
inositol-1,4-bisphosphate 1-phosphatase
inositol-polyphosphate 1-phosphatase
INPP
IPP
-
-
-
-
IPPase
-
-
-
-
phosphatase, inositol 1,4-bisphosphate 1-
-
-
-
-
RnPIP
-
-
-
-
inositol polyphosphate 1-phosphatase
dual activities: 3',5'-bisphosphate nucleotidase
inositol polyphosphate 1-phosphatase
dual activities: 3',5'-bisphosphate nucleotidase
-
inositol-polyphosphate 1-phosphatase
-
-
-
-
INPP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
mechanism
1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
the enzyme acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate, 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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
111070-17-8
-
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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
3'-phosphoadenosine 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
128% of activity observed with 3'(2'),5'-bisphosphate nucleotide
-
-
?
inositol 1,4,5-trisphosphate + H2O
? + phosphate
4.58% of activity observed with 3'(2'),5'-bisphosphate nucleotide
-
-
?
inositol 1,4-bisphosphate + H2O
? + phosphate
35% of activity observed with adenosine 3',5'-bisphosphate
-
-
?
1D-myo-inositol 1,4-bisphosphate + H2O
1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1D-myo-inositol 1,4-bisphosphate + H2O
1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
-
?
D-myo-inositol 1,3,4-trisphosphate + H2O
D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
?
D-myo-inositol 1,3,4-trisphosphate + H2O
D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
-
?
D-myo-inositol 1,3,4-trisphosphate + H2O
D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
?
D-myo-inositol 1,3,4-trisphosphate + H2O
D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
?
D-myo-inositol 1,3,4-trisphosphate + H2O
D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
additional information
?
-
-
involved in stress signal transduction and abscisic acid signaling
-
-
?
additional information
?
-
-
no substrate: inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate
-
-
?
additional information
?
-
-
no substrate: inositol 1-phosphate (D- or L-myo-isomer)
-
-
?
additional information
?
-
-
no substrates are inositol 2-phosphate, or inositol 4-phosphate
-
-
?
additional information
?
-
-
no substrate: inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate
-
-
?
additional information
?
-
-
involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
-
-
?
additional information
?
-
-
no substrate: inositol 1-phosphate (D- or L-myo-isomer)
-
-
?
additional information
?
-
-
no substrates are inositol 2-phosphate, or inositol 4-phosphate
-
-
?
additional information
?
-
-
no substrate: inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate
-
-
?
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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
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
-
-
-
?
additional information
?
-
-
involved in stress signal transduction and abscisic acid signaling
-
-
?
additional information
?
-
-
involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Na+
Mg2+
optimal concentration 2mM, 3',5'-bisphosphate nucleotide as substrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Colorectal Neoplasms
Transcription of the inositol polyphosphate 1-phosphatase gene (INPP1) is upregulated in human colorectal cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
3'-phosphoadenosine 5'-phosphosulfate
KM value lower than 0.01 mM
additional information
3'-phosphoadenosine 5'-phosphosulfate
-
KM value lower than 0.01 mM
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
200
K+
Gossypium hirsutum
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
0.2
lithium ion
Gossypium hirsutum
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
100
Na+
Gossypium hirsutum
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
0.01
Ca2+
Gossypium hirsutum
30°C, pH 7.5, 0.55 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
0.05
Ca2+
Gossypium hirsutum
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
pH 7.5, 2 mM Mg2+, adenosine 3',5'-bisphosphate as substrate
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme has additional activity of 3â-phosphoadenosine 5â-phosphate phosphatase
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). INPP_BOVIN
400
0
43965
Swiss-Prot
other Location (Reliability: 2)
INPP_HUMAN
399
0
43998
Swiss-Prot
other Location (Reliability: 2)
INPP_MOUSE
396
0
43346
Swiss-Prot
other Location (Reliability: 4)
DPNP1_ARATH
353
0
37564
Swiss-Prot
other Location (Reliability: 4)
DPNP2_ARATH
347
0
37509
Swiss-Prot
other Location (Reliability: 5)
DPNP3_ARATH
357
0
38385
Swiss-Prot
other Location (Reliability: 5)
DPNP4_ARATH
345
0
37489
Swiss-Prot
Mitochondrion (Reliability: 5)
DPNP_DICDI
332
0
36888
Swiss-Prot
other Location (Reliability: 3)
D9PMF9_9ZZZZ
47
0
4865
TrEMBL
other Location (Reliability: 1)
T1C4M7_9ZZZZ
94
0
10330
TrEMBL
other Location (Reliability: 1)
B7P6C6_IXOSC
394
0
42496
TrEMBL
other Location (Reliability: 3)
T0YED8_9ZZZZ
174
0
18028
TrEMBL
other Location (Reliability: 2)
A0A6J8DIA5_MYTCO
388
0
43006
TrEMBL
other Location (Reliability: 2)
A0A5B6YUV5_DAVIN
392
0
42130
TrEMBL
other Location (Reliability: 5)
A0A3R7LM26_9TRYP
386
0
41671
TrEMBL
Secretory Pathway (Reliability: 2)
B9SFC7_RICCO
414
0
45141
TrEMBL
Mitochondrion (Reliability: 4)
A0A5B6YUJ9_DAVIN
215
0
23207
TrEMBL
other Location (Reliability: 5)
A0A2I0ANM3_9ASPA
479
0
51391
TrEMBL
Chloroplast (Reliability: 3)
A0A0F3GUG0_9BACT
286
0
30362
TrEMBL
-
A4I797_LEIIN
295
0
31784
TrEMBL
other Location (Reliability: 2)
T0YW44_9ZZZZ
189
0
20733
TrEMBL
Mitochondrion (Reliability: 3)
A0A5B6YUR8_DAVIN
244
0
26047
TrEMBL
Secretory Pathway (Reliability: 2)
T0ZDT4_9ZZZZ
161
0
17153
TrEMBL
other Location (Reliability: 2)
M9PH13_DROME
355
1
39336
TrEMBL
Secretory Pathway (Reliability: 2)
T1CAV2_9ZZZZ
85
0
8798
TrEMBL
Secretory Pathway (Reliability: 5)
A0A3R7KA15_TRYRA
425
0
46497
TrEMBL
Secretory Pathway (Reliability: 2)
Q4Q5W6_LEIMA
295
0
31684
TrEMBL
other Location (Reliability: 3)
A0A7R8CJP4_LEPSM
142
0
15635
TrEMBL
other Location (Reliability: 1)
A0A2G9HM15_9LAMI
432
0
47945
TrEMBL
other Location (Reliability: 5)
Q9VFP6_DROME
375
0
40713
TrEMBL
other Location (Reliability: 2)
A0A088RXH5_9TRYP
433
0
46626
TrEMBL
Secretory Pathway (Reliability: 4)
A4HJT1_LEIBR
433
0
46479
TrEMBL
Secretory Pathway (Reliability: 4)
A0A176S1M0_9GAMM
67
0
7575
TrEMBL
-
A0A3S5H7Q8_LEIDO
295
0
31823
TrEMBL
other Location (Reliability: 2)
T1DBT2_9ZZZZ
184
0
19860
TrEMBL
other Location (Reliability: 1)
T1B1D8_9ZZZZ
138
0
14162
TrEMBL
other Location (Reliability: 5)
T0ZHK6_9ZZZZ
192
0
21304
TrEMBL
Mitochondrion (Reliability: 2)
Q8VWZ6_GOSHI
216
0
22920
TrEMBL
other Location (Reliability: 2)
BPNT1_RAT
308
0
33174
Swiss-Prot
Mitochondrion (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged version expressed in Escherichia coli BL21(DE3), expressed in Saccharomyces cerevisiae JRM4
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
molecular biology
molecular biology
contains a D-domain as mitogen-activated protein kinase docking site but no FXFP motif
molecular biology
contains no D-domain and no FXFP motif as mitogen-activated protein kinase docking site
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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
brenda
Inhorn, R.C.; Majerus, P.W.
Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li+, Ca2+, and Mn2+
J. Biol. Chem.
262
15946-15952
1987
Bos taurus
brenda
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
brenda
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
brenda
Howell, S.; Barnaby, R.J.; Rowe, T.; Ragan, C.I.; Gee, N.S.
Evidence for at least four different inositol bisphosphatases in bovine brain
Eur. J. Biochem.
183
169-172
1989
Bos taurus
brenda
Van Lookeren Campagne, M.M.; Erneux, C.; Van Eijk, R.; Van Haastert, P.J.M.
Two dephosphorylation pathways of inositol 1,4,5-trisphosphate in homogenates of the cellular slime mould Dictyostelium discoideum
Biochem. J.
254
343-350
1988
Dictyostelium discoideum
brenda
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
brenda
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
brenda
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
brenda
Xiong, L.; Lee, B.; Ishitani, M.; Lee, H.; Zhang, C.; Zhu, J.K.
FIERY1 encoding an inositol polyphosphate 1-phosphatase is a negative regulator of abscisic acid and stress signaling in Arabidopsis
Genes Dev.
15
1971-1984
2001
Arabidopsis thaliana
brenda
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
brenda
Caldwell, K.K.; Sosa, M.; Buckley, C.T.
Identification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates
Cell Commun. Signal.
4
2-18
2006
Homo sapiens (P49441), Homo sapiens, Mus musculus (P49442), Mus musculus
brenda
Lu, S.Y.; Zhao, G.R.; Wu, A.M.; Jenks, M.A.; Zhang, S.; Liu, J.Y.
Molecular cloning of a cotton phosphatase gene and its functional characterization
Biochemistry (Moscow)
75
85-94
2010
Gossypium hirsutum (Q8VWZ6), Gossypium hirsutum
brenda
Kim, B.H.; von Arnim, A.G.
FIERY1 regulates light-mediated repression of cell elongation and flowering time via its 3(2),5-bisphosphate nucleotidase activity
Plant J.
58
208-219
2009
Arabidopsis thaliana (Q42546)
brenda
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Server: brenda1 Ver: 9edf756-main (2022-05-17 10:30:03 +0200)