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Information on EC 3.1.3.57 - inositol-1,4-bisphosphate 1-phosphatase for references in articles please use BRENDA:EC3.1.3.57Word Map on EC 3.1.3.57
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The enzyme appears in viruses and cellular organisms
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inositol-1,4-bisphosphate 1-phosphatase
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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
; 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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1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
mechanism
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hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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hydrolysis of phosphoric ester
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hydrolysis of phosphoric ester
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D-myo-inositol (1,4,5)-trisphosphate degradation
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Inositol phosphate metabolism
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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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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
phosphatase, inositol 1,4-bisphosphate 1-
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-
-
-
inositol polyphosphate 1-phosphatase
dual activities: 3',5'-bisphosphate nucleotidase
inositol polyphosphate 1-phosphatase
dual activities: 3',5'-bisphosphate nucleotidase
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inositol-1,4-bisphosphate 1-phosphatase
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inositol-1,4-bisphosphate 1-phosphatase
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inositol-polyphosphate 1-phosphatase
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inositol-polyphosphate 1-phosphatase
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inositol-polyphosphate 1-phosphatase
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INPP
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brenda
cv. CRI 121
UniProt
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SwissProt
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SwissProt
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Sprague-Dawley
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brenda
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SwissProt
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-
brenda
calf
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
enzyme has additional activity of 3ā-phosphoadenosine 5ā-phosphate phosphatase
SwissProt
brenda
Sprague-Dawley
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-
brenda
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1D-myo-inositol 1,4-bisphosphate + H2O
1D-myo-inositol 4-phosphate + phosphate
2'-phosphoadenosine 5'-phosphate + H2O
?
-
-
-
?
3'-phosphoadenosine 5'-phosphate + H2O
AMP + phosphate
-
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
128% of activity observed with 3'(2'),5'-bisphosphate nucleotide
-
-
?
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 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
inositol 1,4,5-trisphosphate + H2O
? + phosphate
4.58% of activity observed with 3'(2'),5'-bisphosphate nucleotide
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-
?
inositol 1,4-bisphosphate + H2O
? + phosphate
35% of activity observed with adenosine 3',5'-bisphosphate
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-
?
additional information
?
-
1D-myo-inositol 1,4-bisphosphate + H2O
1D-myo-inositol 4-phosphate + phosphate
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-
-
?
1D-myo-inositol 1,4-bisphosphate + H2O
1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
?
-
-
-
-
3'-phosphoadenosine 5'-phosphosulfate + H2O
?
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-
-
-
-
3'-phosphoadenosine 5'-phosphosulfate + H2O
?
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
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-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
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-
-
-
?
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
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-
-
?
additional information
?
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involved in stress signal transduction and abscisic acid signaling
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-
additional information
?
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no substrate: inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate
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-
additional information
?
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no substrate: inositol 1-phosphate (D- or L-myo-isomer)
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-
additional information
?
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no substrates are inositol 2-phosphate, or inositol 4-phosphate
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additional information
?
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no substrate: inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate
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-
additional information
?
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involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
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additional information
?
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no substrate: inositol 1-phosphate (D- or L-myo-isomer)
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additional information
?
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no substrates are inositol 2-phosphate, or inositol 4-phosphate
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additional information
?
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no substrate: inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate
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-
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D-myo-inositol 1,4-bisphosphate + H2O
D-myo-inositol 4-phosphate + phosphate
additional information
?
-
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
?
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-
involved in stress signal transduction and abscisic acid signaling
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-
additional information
?
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involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
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K+
-
activation, 0.05-0.1 M
Mg2+
-
kinetics; requirement
Mg2+
optimal concentration 2mM, 3',5'-bisphosphate nucleotide as substrate
Mg2+
strictily dependent on
Na+
-
0.05-0.1 M; activation
Na+
-
activation; activation below 4 mM, inhibition above
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5,5'-dithiobis(nitrobenzoic acid)
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inositol 1,4-bisphosphate
Mg2+
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inhibition above 4 mM, activates below
additional information
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no inhibition by 2,3-bisphosphoglycerate
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Ca2+
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inositol 1,4-bisphosphate
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inositol 1,3,4-trisphosphate as substrate
inositol 1,4-bisphosphate
-
inositol 1,3,4-trisphosphate as substrate
Li+
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-
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0.02
inositol 1,3,4-trisphosphate
-
37°C
0.0009 - 0.2
inositol 1,4-bisphosphate
additional information
3'-phosphoadenosine 5'-phosphosulfate
0.0009
inositol 1,4-bisphosphate
-
37°C
0.004 - 0.005
inositol 1,4-bisphosphate
-
37°C, pH 7.5
0.004 - 0.005
inositol 1,4-bisphosphate
-
-
0.0178
inositol 1,4-bisphosphate
-
37°C, pH 7.2
0.2
inositol 1,4-bisphosphate
30°C, pH 7.5
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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200
K+
Gossypium hirsutum;
Q8VWZ6
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
0.2
lithium ion
Gossypium hirsutum;
Q8VWZ6
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
100
Na+
Gossypium hirsutum;
Q8VWZ6
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
0.01
Ca2+
Gossypium hirsutum;
Q8VWZ6
30°C, pH 7.5, 0.55 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
0.05
Ca2+
Gossypium hirsutum;
Q8VWZ6
30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
0.8
Ca2+
Gossypium hirsutum;
Q8VWZ6
30°C, pH 7.5, 5 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate
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7.5
30°C, 2 mM Mg2+, adenosine 3',5'-bisphosphate as substrate
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6.5 - 9
adenosine 3',5'-bisphosphate as substrate
7 - 7.9
-
about half-maximal activity at pH 7 and pH 7.9
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30 - 60
pH 7.5, 2 mM Mg2+, adenosine 3',5'-bisphosphate as substrate
37
-
assay at
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brenda
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brenda
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brenda
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brenda
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brenda
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additional information
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subcellular distribution
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
-
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brenda
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Q42546
Arabidopsis thaliana;
C4M633
Entamoeba histolytica;
Q9Z1N4
Rattus norvegicus;
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37000
x * 37000, SDS-PAGE
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?
x * 37000, SDS-PAGE
?
-
x * 37000, SDS-PAGE
-
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in complex with AMP, phosphate and Mg2+
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70
-
t1/2: 80 s, in crude cytosolic fraction
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immobilized metal ion affinity chromatography (Ni2+)
partial
-
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for genetic complementation
His-tagged version expressed in Escherichia coli BL21(DE3), expressed in Saccharomyces cerevisiae JRM4
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medicine
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involvement of enzyme in hypertrophic signaling pathways in ventricular myocytes
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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INPP_BOVIN
400
43965
Swiss-Prot
INPP_HUMAN
399
43998
Swiss-Prot
INPP_MOUSE
396
43346
Swiss-Prot
DPNP1_ARATH
353
37564
Swiss-Prot
DPNP2_ARATH
347
37509
Swiss-Prot
DPNP3_ARATH
357
38385
Swiss-Prot
DPNP4_ARATH
345
37489
Swiss-Prot
DPNP_DICDI
332
36888
Swiss-Prot
A0A088RXH5_9TRYP
433
46626
TrEMBL
A0A0B2QJM9_GLYSO
383
41493
TrEMBL
K1SYQ1_9ZZZZ
242
26551
TrEMBL
B7P6C6_IXOSC
394
42496
TrEMBL
B9S600_RICCO
392
42577
TrEMBL
B0EFK5_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
317
35021
TrEMBL
A0A2H3EVS3_9HELO
354
37270
TrEMBL
A4I797_LEIIN
295
31784
TrEMBL
B9SFC7_RICCO
414
45141
TrEMBL
T0YED8_9ZZZZ
174
18028
TrEMBL
A0A2G9HM15_9LAMI
432
47945
TrEMBL
Q9VFP6_DROME
375
40713
TrEMBL
T1DBT2_9ZZZZ
184
19860
TrEMBL
A0A1F2P564_9EURY
276
30421
TrEMBL
T1CAV2_9ZZZZ
85
8798
TrEMBL
T1C4M7_9ZZZZ
94
10330
TrEMBL
T0ZHK6_9ZZZZ
192
21304
TrEMBL
A0A2I0ANM3_9ASPA
479
51391
TrEMBL
D9PMF9_9ZZZZ
47
4865
TrEMBL
T0YW44_9ZZZZ
189
20733
TrEMBL
T1B1D8_9ZZZZ
138
14162
TrEMBL
G8PQW8_PSEUV
Pseudovibrio sp. (strain FO-BEG1)
260
27986
TrEMBL
A0A1W2TWA9_ROSNE
353
36924
TrEMBL
A0A0F3GUG0_9BACT
286
30362
TrEMBL
A0A0B2RVV2_GLYSO
382
41372
TrEMBL
A0A2G9HU18_9LAMI
399
42765
TrEMBL
A0A2H3FJP2_9HELO
354
37239
TrEMBL
M9PH13_DROME
355
39336
TrEMBL
BPNT1_RAT
308
33174
Swiss-Prot
Q8VWZ6_GOSHI
216
22920
TrEMBL
C4M633_ENTHI
285
32051
TrEMBL
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Colorectal Neoplasms
Transcription of the inositol polyphosphate 1-phosphatase gene (INPP1) is upregulated in human colorectal cancer.
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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, Homo sapiens (P49441), Mus musculus, Mus musculus (P49442)
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, Gossypium hirsutum (Q8VWZ6)
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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