Ligand myo-inositol

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Basic Ligand Information

Molecular Structure
Picture of myo-inositol (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C6H12O6
myo-inositol
CDAISMWEOUEBRE-GPIVLXJGSA-N
Synonyms:
1D-myo-inositol, D-Inositol, D-myo-inositol, DL-myo-inositol, i-inositol, Inositol, iso-inositol, L-myo-inositol, meso-Inositol, mesoinositol, myoinositol


Show all pahtways known for Show all BRENDA pathways known for myo-inositol

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (44 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-3-O-methyl-myo-inositol + H+
-
show the reaction diagram
S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + D-bornesitol
-

In Vivo Product in Enzyme-catalyzed Reactions (26 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
glycerophosphoinositol + H2O = glycerol 3-phosphate + inositol
-

Substrate in Enzyme-catalyzed Reactions (108 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
myo-inositol + NAD+ = keto-inositol + NADH
-
show the reaction diagram
inositol + NAD+ = ? + NADH + H+
-
show the reaction diagram
i-inositol + NAD+ = ?
-
show the reaction diagram
myo-inositol + 2,6-dichlorophenol indophenol = ?
-
show the reaction diagram
myo-inositol + S-adenosyl-L-methionine = ? + 5'-deoxyadenosine + L-methionine
-
show the reaction diagram
myo-inositol + S-adenosyl-L-methionine = ? + CO2 + L-methionine + 5'-deoxyadenosine
-
show the reaction diagram
S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-3-O-methyl-myo-inositol + H+
-
show the reaction diagram
S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + D-bornesitol
-
show the reaction diagram
sucrose + inositol = ?
-
show the reaction diagram
soluble starch + myo-inositol = ?
-
show the reaction diagram
beta-D-glucose 1-phosphate + myo-inositol = O-alpha-D-glucopyranosyl-(1,1)-myo-inositol + O-alpha-D-glucopyranosyl-(1,5)-myo-inositol + O-alpha-D-glucopyranosyl-(1,2)-O-alpha-D-glucopyranosyl-(1,1)-myo-inositol + O-alpha-D-glucopyranosyl-(1,2)-O-alpha-D-glucopyranosyl-(1,1)-myo-inositol
-
show the reaction diagram
1-alpha-D-galactosyl-myo-inositol + myo-inositol = myo-inositol + 1-alpha-D-galactosyl-myo-inositol
-
show the reaction diagram
meso-inositol + phenyl alpha-D-galactoside = ?
-
show the reaction diagram
di-N-acetylchitobiose + myoinositol = ?
-

Product in Enzyme-catalyzed Reactions (80 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
1-stearoyl-2-arachidonoylphosphatidylinositol + CMP = CDP-1-stearoyl-2-arachidonoylglycerol + myo-inositol
-
show the reaction diagram
myo-inositol 1-phosphate + H2O = myo-inositol + phosphate
-
show the reaction diagram
inositol phosphate + H2O = inositol + phosphate
-
show the reaction diagram
phosphatidylinositol + H2O = inositol + phosphatidate
-
-
show the reaction diagram
galactinol + H2O = alpha-D-galactopyranose + myoinositol
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Activator in Enzyme-catalyzed Reactions (5 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (39 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
strong, competitive
-
competitive against sucrose
-
decreases gene EKI1 expression, involving the transcription factors Ino2p, Ino4p, and Opi1p, the UASINO element of the EKI promotor is required for the repressive regulation, the inhibitory effect on the enzyme is correlated with a decrease of ethanolamine incorporation into CDP-ethanolamine pathway intermediates and into phosphatidylethanolamine and phosphatidylcholine
-
product inhibition
-
substrate inhibition above 1 mM
-
inhibits CMP-dependent incorporation of glycerol 3-phosphate by microsomes
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cells grown in the presence of myo-inositol
-
product inhibition, competitive
non-competitive inhibition
inhibition of alkaline phosphatase
-
at 0.075 mM in culture medium,reduction of enzyme activity by 30-40%
-
20% relative inhibition, poor inhibitor
-
competitive inhibition
-
weak competitive inhibitor
-
poor competitive inhibitor
poor competitive inhibitor
competitive
-
4 mM
-
feedback/product inhibition by inhibition of INO1 gene transcription, acts as a metabolic sensor
-

3D Structure of Enzyme-Ligand-Complex (PDB) (243 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (9 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
pH 9.0, 25°C, recombinant mutant D172N
1.9
-
pH 9.0, 25°C, recombinant mutant D179N
73
-
pH 9.0, 25°C, recombinant mutant H176A
0.23
-
pH 9.0, 25°C, recombinant mutant Y233F
47
-
pH 9.0, 25°C, recombinant mutant Y235F
34
-
pH 9.0, 25°C, recombinant wild-type enzyme
58
-
-
7.22
-
with Fe(2+) and L-cysteine as activators
0.183
-
at pH 7.5 and 85°C
23.2
-

KM Value (59 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
-
430
-
25°C, pH 9.0
18
-
pH 9.0, 25°C, recombinant mutant D172N
65
-
pH 9.0, 25°C, recombinant mutant D179N
28
-
pH 9.0, 25°C, recombinant mutant H176A
118
-
pH 9.0, 25°C, recombinant mutant Y233F
4
-
pH 9.0, 25°C, recombinant mutant Y235F
39
-
pH 9.0, 25°C, recombinant wild-type enzyme
4.4
-
-
18
-
with Fe(2+) and L-cysteine as activators
5.9
-
with Fe(II) and L-cysteine as activators
5
-
MIOX activity present in peak 3 of hydrophobic-interaction chromatography on Resource-PHE column
MIOX activity present in peak 2 of hydrophobic-interaction chromatography on Resource-PHE column
with Fe(II) and quinolinic acid as activators
0.2
-
MIOX activity present in peak 1 of hydrophobic-interaction chromatography on Resource-PHE column
-
45
-
30°C, pH 6.5
5
-
recombinant enzyme from Saccharomyces cerevisiae, at pH 7.4 and 30°C
0.83
-
native enzyme, at pH 7.4 and 30°C
1.38
-
recombinant enzyme from Escherichia coli, at pH 7.4 and 30°C
1
-
with 10 mM 1-alpha-D-galactosyl-myo-inositol in the exchange reaction
5.5
-
at pH 7.5 and 85°C
0.36
-
in 20 mM HEPES (pH 7.2), 6 mM MgCl2, 10 mM LiCl, 1 mM dithiothreitol, at 30°C
0.0531
-
pH 7.5, 37°C
0.06
-
pH 6.8, 37°C, 0.0001 mM Ca2+
1.6
-
pH 9.0, 37°C
0.28
-
pH 9.0, 30°C
0.55
-
pH 6.8, 37°C, 0.003 mM Ca2+
1.5
-
pH 6.8, 37°C, 0.01 mM Ca2+
0.6
-
pH 8.0, 30°C, CMP-stimulated exchange reaction
0.277
-
pH 8.0, 30°C
pH 8.0, 30°C, CMP-independent exchange reaction
0.066
-
pH 8.6, 37°C
pH 8.5, 37°C, exchange reaction
0.015
-
pH 8.5, 37°C
pH 8.0, 37°C
0.21
-
pH 8.0, 30°C, forward reaction
0.09
-
transferase reaction, in absence of alpha-lactalbumin
380
-
transferase reaction, in presence of 50 mM glycine/HCl buffer, pH 3.0, 80 mM lactose, 0.5 mg/ml alpha-lactalbumin
345
-

Ki Value (5 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
competitive against sucrose
10.1
-
noncompetitive against galactinol
22.3
-
pH 7.5, 37°C
39
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
440
-

References & Links

Links to other databases for myo-inositol

ChEBI
PubChem
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PubChem