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Information on EC 3.1.3.25 - inositol-phosphate phosphatase and Organism(s) Bos taurus and UniProt Accession P20456

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.25 inositol-phosphate phosphatase
IUBMB Comments
Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. It also acts on adenosine 2'-phosphate (but not the 3'- or 5'- phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate. Two isoforms are known .
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Bos taurus
UNIPROT: P20456
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
inositol monophosphatase, impase, inositol phosphatase, impa2, impa1, myo-inositol monophosphatase, inpp5f, impp, myo-inositol-1-phosphatase, inositol-1-phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inositol monophosphatase
-
myo-inositol monophosphatase
-
I-1-Pase
-
-
-
-
IMP
-
-
-
-
IMPase
inositol 1-phosphate phosphatase
-
-
-
-
inositol monophosphatase
-
-
-
-
inositol monophosphate phosphatase
-
-
-
-
inositol phosphatase
-
-
-
-
inositol phosphohydrolase
-
-
-
-
inositol-1(or 4)-monophosphatase
-
-
-
-
inositol-1-phosphatase
-
-
-
-
L-myo-inositol-1-phosphate phosphatase
-
-
-
-
Lithium-sensitive myo-inositol monophosphatase A1
-
-
-
-
myo-inositol 1 (or 4) -monophosphatase
-
-
-
-
myo-inositol 1-phosphatase
-
-
-
-
Myo-inositol monophosphatase A2
-
-
-
-
myo-inositol-1(or 4)-phosphate phosphohydrolase
-
-
-
-
myo-inositol-1-phosphatase
-
-
myo-inositol-1-phosphatase/aryl-phosphatase
-
exhibits also Zn-dependent aryl-phosphatase activity at acidic pH
myo-inositol-phosphatase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
myo-inositol phosphate + H2O = myo-inositol + phosphate
show the reaction diagram
the catalytic mechanism involves three Mg2+ ions, modeling of the reaction and the postreaction complex, active site structure, substrate binding structure, overview
myo-inositol phosphate + H2O = myo-inositol + phosphate
show the reaction diagram
catalytic mechanism and substrate-enzyme interactions, active site residues
-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol-phosphate phosphohydrolase
Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. It also acts on adenosine 2'-phosphate (but not the 3'- or 5'- phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate. Two isoforms are known [4].
CAS REGISTRY NUMBER
COMMENTARY hide
37184-63-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myo-inositol phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl cyclohexylammonium 1-hydroxyphosphonate + H2O
?
show the reaction diagram
-
-
-
-
?
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl-1-hydroxyphosphonate cyclohexylammonium salt + H2O
?
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
?
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
D-alpha-galactose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-alpha-glucose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-beta glucose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-mannose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
D-ribose 5-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
inositol 1,3-thiophosphate + H2O
?
show the reaction diagram
-
-
-
-
?
L-chiro-inositol-3-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 1,3-thiophosphate + H2O
?
show the reaction diagram
-
reaction 3times slower than reaction with inositol 1-phosphate
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
the reaction is only catalyzed in the presence of ZnCl2 at acidic pH
-
-
?
propan-1-ol 2-phosphate + H2O
1-propanol + 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
myo-inositol phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
3% activation at 3.5 mM
Cu2+
-
3% activation at 3.5 mM
Fe2+
-
3% activation at 3.5 mM
Mn2+
-
3% activation at 3.5 mM
Na+
-
-
NH4+
-
stimulatory
Zn2+
-
activation at 3.5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mg2+
inhibitory at high concentrations
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl 1-methylphosphonate
-
IC50 is 260 mM
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-ethylphosphonate
-
competitive inhibition
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
competitive inhibition
(-)-(1S,2R,4R,6R)-6-propyloxycyclohexane-1,2,4-triol
-
IC50 is about 150 mM
(-)-(1S,2R,4S,6R)-6-(2-aminoethyloxy)cyclohexane-1,2,4-triol
-
IC50 is 5 mM
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)amino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is above 54 mM
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)aminocyclohexane-1,2,4-triol
-
IC50 is 6 mM
(-)-(1S,2R,4S,6R)-6-(3-aminopropyloxy)cyclohexane-1,2,4-triol
-
IC50 is 10 mM
(-)-(1S,2R,4S,6R)-6-(4-phenylbutyl)aminocyclohexane-1,2,4-triol
-
non-competitive inhibition
(-)-(1S,2R,4S,6R)-6-aminocyclohexane-1,2,4-triol
-
IC50 is above 50 mM
(-)-(1S,2R,4S,6R)-6-butylaminocyclohexane-1,2,4-triol
-
non-competitive inhibition in absence of phosphate
(-)-(1S,2R,4S,6R)-6-ethylaminocyclohexane-1,2,4-triol
-
IC50 is above 50 mM
(-)-(1S,2R,4S,6R)-6-hexylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is 1.3 mM
(-)-(1S,2R,4S,6R)-6-hexylaminocyclohexane-1,2,4-triol
-
uncompetitive inhibition
(-)-(1S,2R,4S,6R)-6-hexyloxycyclohexane-1,2,4-triol
-
IC50 is about 10 mM
(-)-(1S,2R,4S,6R)-6-methylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is above 8 mM
(-)-(1S,2R,4S,6R)-6-octylaminocyclohexane-1,2,4-triol
-
IC50 is 4 mM
(-)-(1S,2R,4S,6R)-6-[4-(2-hydroxyphenyloxy)butyloxy]cyclohexane-1,2,4-triol
-
competitive inhibition
(-)-(1S,2R,4S,6R)-6-[N-(4-phenylbutyl)-N-(2-aminoethyl)-amino]cyclohexane-1,2,4-triol [hydrochloride salt]
-
IC50 is 9 mM
ATP
-
-
Co2+
-
inhibits hydrolysis of inositol-1-phosphate at high concentrations
Disulfiram
-
-
F-
-
50% inhibitory at 1 mM
Mg2+
-
inhibits hydrolysis of inositol-1-phosphate at high concentrations
Mn2+
-
-
myo-inositol
-
non-competitive inhibition
phosphate
phosphosulfate
-
-
SO42-
-
40% inhibitory at 17 mM
additional information
-
potency and structural features of product-like inhibitors, inhibitory mechanism, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calbindin
-
apo and Ca2+-bound form, strong activation, Kd: approximately 0.001 mM, at pH 6 very low activity in the absence of calbindin, almost no activity lost in the presence of calbindin compared to activity at pH 7
-
NH4+
-
stimulatory
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl-1-hydroxyphosphonate cyclohexylammonium salt
-
pH 8.0, 25°C
0.58
2'-AMP
-
-
5
4-nitrophenyl phosphate
-
-
0.13
D-inositol 1-phosphate
-
-
0.1
D-myo-Inositol 1-phosphate
-
pH 8.0, 25°C
0.89
DL-myo-inositol 1-phosphate
-
-
0.38
Glycerol 2-phosphate
-
-
0.21
inositol 1,3-thiophosphate
-
pH 9.0, 25°C
0.11
inositol 3-phosphate
-
pH 9.0, 25°C
0.87
L-glycerol 1-phosphate
-
-
0.1
L-myo-Inositol 1-phosphate
-
-
15
Propan-1-ol 2-phosphate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
inositol 1,3-thiophosphate
-
pH 9.0, 25°C
0.48
inositol 3-phosphate
-
pH 9.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-ethylphosphonate
-
pH 8.0, 25°C
0.04
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
pH 8.0, 25°C
9
(-)-(1S,2R,4S,6R)-6-(4-phenylbutyl)aminocyclohexane-1,2,4-triol
-
pH 8.0, 25°C
0.3
(-)-(1S,2R,4S,6R)-6-butylaminocyclohexane-1,2,4-triol
-
pH 8.0, 25°C
0.3
(-)-(1S,2R,4S,6R)-6-hexylaminocyclohexane-1,2,4-triol
-
pH 8.0, 25°C
4
(-)-(1S,2R,4S,6R)-6-[4-(2-hydroxyphenyloxy)butyloxy]cyclohexane-1,2,4-triol
-
pH 8.0, 25°C
0.5
phosphosulfate
-
pH 6.5 and pH 9.0
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl 1-methylphosphonate
Bos taurus
-
IC50 is 260 mM
150
(-)-(1S,2R,4R,6R)-6-propyloxycyclohexane-1,2,4-triol
Bos taurus
-
IC50 is about 150 mM
5
(-)-(1S,2R,4S,6R)-6-(2-aminoethyloxy)cyclohexane-1,2,4-triol
Bos taurus
-
IC50 is 5 mM
54
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)amino-2,4-dihydroxycyclohexyl 1-methylphosphonate
Bos taurus
-
IC50 is above 54 mM
6
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)aminocyclohexane-1,2,4-triol
Bos taurus
-
IC50 is 6 mM
10
(-)-(1S,2R,4S,6R)-6-(3-aminopropyloxy)cyclohexane-1,2,4-triol
Bos taurus
-
IC50 is 10 mM
50
(-)-(1S,2R,4S,6R)-6-aminocyclohexane-1,2,4-triol
Bos taurus
-
IC50 is above 50 mM
50
(-)-(1S,2R,4S,6R)-6-ethylaminocyclohexane-1,2,4-triol
Bos taurus
-
IC50 is above 50 mM
1.3
(-)-(1S,2R,4S,6R)-6-hexylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
Bos taurus
-
IC50 is 1.3 mM
10
(-)-(1S,2R,4S,6R)-6-hexyloxycyclohexane-1,2,4-triol
Bos taurus
-
IC50 is about 10 mM
8
(-)-(1S,2R,4S,6R)-6-methylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
Bos taurus
-
IC50 is above 8 mM
4
(-)-(1S,2R,4S,6R)-6-octylaminocyclohexane-1,2,4-triol
Bos taurus
-
IC50 is 4 mM
9
(-)-(1S,2R,4S,6R)-6-[N-(4-phenylbutyl)-N-(2-aminoethyl)-amino]cyclohexane-1,2,4-triol [hydrochloride salt]
Bos taurus
-
IC50 is 9 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
different assay methods, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
-
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
no significant changes in activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IMPA1_BOVIN
277
0
30056
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29920
-
ESI-MS
31000
-
2 * 31000, SDS-PAGE
58000
-
gel filtration
59000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complex with Mg2+, room temperature, hanging drop vapour diffusion method, 0.002 ml protein solution containing 20 mg/ml protein in 20 mm Tris-HCl, pH 7.5, and 20 mM MgCl2, is mixed with 0.002 ml reservoir solution containing 0.1 M sodium acetate, 0.1 M sodium HEPES, pH 8.5, and 15% PEG 4000, X-ray diffraction structure determination and analysis at 1.4 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by ion exchange chromatography, ammonium sulfate fractionation, and dialysis
2000fold
-
2800fold
-
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21(DE3)
expression in Escherichia coli strain BL21(DE3)pLysS
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
the enzyme is the putative target of lithium therapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Attwood, P.V.; Ducep, J.B.; Chanal, M.C.
Purification and properties of myo-inositol-1-phosphatase from bovine brain
Biochem. J.
253
387-394
1988
Bos taurus
Manually annotated by BRENDA team
Shute, J.K.; Baker, R.; Billington, D.C.; Gani, D.
Mechanism of the myo-inositol phosphatase reaction
J. Chem. Soc. Chem. Commun.
1988
626-628
1988
Bos taurus
-
Manually annotated by BRENDA team
Shute, J.K.; Baker, R.; Billington, D.C.; Gani, D.
Mechanism of the myo-inositol phosphatase reaction
J. Chem. Soc. Chem. Commun.
1988
422-423
1988
Bos taurus
-
Manually annotated by BRENDA team
Ragan, C.I.; Watling, K.J.; Gee, N.S.; Aspley, S.; Jackson, R.G.; Reid, G.G.; Baker, R.; Billington, D.C.; Barnaby, R.J.; Leeson, P.D.
The dephosphorylation of inositol 1,4-bisphosphate to inositol in liver and brain involves two distinct Li+-sensitive enzymes and proceeds via inositol 4-phosphate
Biochem. J.
249
143-148
1988
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Hallcher, L.M.; Sherman, W.R.
The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain
J. Biol. Chem.
255
10896-10901
1980
Bos taurus
Manually annotated by BRENDA team
Strasser, F.; Pelton, P.D.; Ganzhorn, A.J.
Kinetic characterization of enzyme forms involved in metal ion activation and inhibition of myo-inositol monophosphatase
Biochem. J.
307
585-593
1995
Bos taurus
Manually annotated by BRENDA team
McAllister, G.; Whiting, P.; Hammond, E.A.; Knowles, M.R.; Atack, J.R.; Bailey, F.J.; Maigetter, R.; Ragan, C.I.
cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme
Biochem. J.
284
749-754
1992
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ganzhorn, A.J.; Vincendon, P.; Pelton, J.T.
Structural characterization of myo-inositol monophosphatase from bovine brain by secondary structure prediction, fluorescence, circular dichroism and Raman spectroscopy
Biochim. Biophys. Acta
1161
303-310
1993
Bos taurus
Manually annotated by BRENDA team
Parthasarathy, L.; Vadnal, R.E.; Parthasarathy, R.; Shyamaldevi, C.S.
Minireview. Biochemical and molecular properties of lithium-sensitive myo-inositol monophosphatase
Life Sci.
54
1127-1142
1994
Bos taurus, Homo sapiens, Lilium longiflorum, Rattus norvegicus
Manually annotated by BRENDA team
Wang, X.L.; Akhtar, R.A.; Abdel-Latif, A.A.
Studies on the properties of myo-inositol-1,4,5-trisphosphate 5-phosphatase and myo-inositol monophosphatase in bovine iris sphincter smooth muscle: effects of okadaic acid and protein phosphorylation
Biochim. Biophys. Acta
1222
27-36
1994
Bos taurus
Manually annotated by BRENDA team
Berggard, T.; Szczepankiewicz, O.; Thulin, E.; Linse, S.
Myo-inositol monophosphatase is an activated target of calbindin D28k
J. Biol. Chem.
277
41954-41959
2002
Bos taurus
Manually annotated by BRENDA team
Fauroux, C.M.J.; Lee, M.; Cullis, P.M.; Douglas, K.T.; Gore, M.G.; Freeman, S.
Stereochemistry at phosphorus of the reaction catalyzed by myo-inositol monophosphatase
J. Med. Chem.
45
1363-1373
2002
Bos taurus
Manually annotated by BRENDA team
Gill, R.; Mohammed, F.; Badyal, R.; Coates, L.; Erskine, P.; Thompson, D.; Cooper, J.; Gore, M.; Wood, S.
High-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy
Acta Crystallogr. Sect. D
61
545-555
2005
Bos taurus (P20456), Bos taurus
Manually annotated by BRENDA team
Miller, D.J.; Bashir-Uddin Surfraz, M.; Akhtar, M.; Gani, D.; Allemann, R.K.
Removal of the phosphate group in mechanism-based inhibitors of inositol monophosphatase leads to unusual inhibitory activity
Org. Biomol. Chem.
2
671-688
2004
Bos taurus
Manually annotated by BRENDA team
Caselli, A.; Casolaro, M.; Ranaldi, F.; Manao, G.; Camici, G.; Giachetti, E.
Kinetic mechanism of the Zn-dependent aryl-phosphatase activity of myo-inositol-1-phosphatase
Biophys. Chem.
125
435-443
2007
Bos taurus
Manually annotated by BRENDA team
Lu, S.; Huang, W.; Li, X.; Huang, Z.; Liu, X.; Chen, Y.; Shi, T.; Zhang, J.
Insights into the role of magnesium triad in myo-inositol monophosphatase: metal mechanism, substrate binding, and lithium therapy
J. Chem. Inf. Model.
52
2398-2409
2012
Bos taurus (P20456)
Manually annotated by BRENDA team
Wang, X.; Hirao, H.
ONIOM (DFT:MM) study of the catalytic mechanism of myo-inositol monophosphatase: essential role of water in enzyme catalysis in the two-metal mechanism
J. Phys. Chem. B
117
833-842
2013
Bos taurus (P20456)
Manually annotated by BRENDA team