Information on EC 2.1.1.129 - inositol 4-methyltransferase

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The expected taxonomic range for this enzyme is: Magnoliophyta

EC NUMBER
COMMENTARY
2.1.1.129
-
RECOMMENDED NAME
GeneOntology No.
inositol 4-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
pinitol biosynthesis I
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:1D-myo-inositol 4-methyltransferase
The enzyme from the rice bean Vigna umbellata (Fabaceae) is highly specific for S-adenosyl-L-methionine. The enzyme also methylates 1L-1,2,4/3,5-cyclohexanepentol, 2,4,6/3,5-pentahydroxycyclohexanone, D,L-2,3,4,6/5-pentacyclohexanone and 2,2'-anhydro-2-C-hydroxymethyl-myo-inositol, but at lower rates than that of myo-inositol.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 2.1.1.134
-
-
formerly
-
IMT1 protein
-
-
-
-
inositol 6-O-methyltransferase
-
-
-
-
inositol methyl transferase
P45986
-
m6OMT
-
-
-
-
methyltransferase, inositol 6-O
-
-
-
-
methyltransferase, inositol L-1- (Mesembryanthemum crystallinum clone Imt1 reduced)
-
-
-
-
myo-inositol 4-O-methyltransferase
-
-
-
-
myo-inositol 6-O-methyltransferase
-
-
-
-
myo-inositol O-methyltransferase
-
-
PcIMT1
-
-
S-adenosyl-L-methionine:myo-inositol 6-O-methyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
146048-86-4
-
169277-48-9
formerly EC 2.1.1.134
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
no activity in Oryza sativa
-
-
-
Manually annotated by BRENDA team
Roxb. Tateoka
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
after cold stress, the Imt1 transgenic Arabidopsis plants exhibit stronger growth than the wild type plants
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 1L-1,3,4/2,5-cyclohexanepentol
?
show the reaction diagram
-
i.e. L-viburnitol
-
-
-
S-adenosyl-L-methionine + 2,4,6/3,5-pentahydroxy-cyclohexanone
?
show the reaction diagram
-
i.e. myo-inosose-2
-
-
-
S-adenosyl-L-methionine + D,L-2,3,4,6/5-pentahydroxy-cyclohexanone
?
show the reaction diagram
-
i.e. myo-inosose-4
-
-
-
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 4-methyl-myo-inositol
show the reaction diagram
-
-
-
-
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
-
-
1D-4-O-methyl-myo-inositol is accumulated in response to abiotic stresses
-
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
P45986
during normal growth IMT is repressed, after salinity stress IMT is induced. By inducing expression of IMT and increasing myo-inositol synthesis, metabolic end products accumulate, facilitating sodium sequestration and protecting photosynthesis
-
-
?
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
-
involved in the biosynthesis of pinitol, which is important for osmotic stress response
-
-
?
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
-
accumulation of methylated inositol in plants under salt-stress
-
-
?
S-adenosyl-L-methionine + myo-inositol
?
show the reaction diagram
-
the product 1D-4-O-methyl-myo-inositol is accumulated in response to abiotic stress
-
-
-
S-adenosyl-L-methionine + myo-inositol
?
show the reaction diagram
-
the enzyme catalyzes the first step in the biosynthesis of the cyclic sugar alcohol pinitol. The presence of high levels of sugar alcohols correlates with osmotolerance
-
-
-
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + D-ononitol
show the reaction diagram
-
-
D-ononitol is 1-D-4-O-methyl-myo-inositol
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
P45986
during normal growth IMT is repressed, after salinity stress IMT is induced. By inducing expression of IMT and increasing myo-inositol synthesis, metabolic end products accumulate, facilitating sodium sequestration and protecting photosynthesis
-
-
?
S-adenosyl-L-methionine + myo-inositol
S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
show the reaction diagram
-
involved in the biosynthesis of pinitol, which is important for osmotic stress response
-
-
?
S-adenosyl-L-methionine + myo-inositol
?
show the reaction diagram
-
the product 1D-4-O-methyl-myo-inositol is accumulated in response to abiotic stress
-
-
-
S-adenosyl-L-methionine + myo-inositol
?
show the reaction diagram
-
the enzyme catalyzes the first step in the biosynthesis of the cyclic sugar alcohol pinitol. The presence of high levels of sugar alcohols correlates with osmotolerance
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
5 mM, slight stimulation
Na+
-
5 mM, slight stimulation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1L-1,3,4/2,5-cyclohexanepentol
-
i.e. L-viburnitol
2,2'-Anhydro-2-C-hydroxymethyl-myo-inositol
-
-
2,4,6/3,5-pentahydroxy-cyclohexanone
-
i.e. myo-inosose-2
D,L-2,3,4,6/5-pentahydroxy-cyclohexanone
-
i.e. myo-inosose-4
EDTA
-
not EGTA
Fe2+
-
5 mM
-
p-chloromercuribenzenesulfonic acid
-
0.02 mM
S-adenosyl-L-homocysteine
-
most potent inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
1-20 mM, slight activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.47
-
1-L-1,3,4/2,5-cyclohexanepentol
-
-
0.67
-
2,4,6/3,5-pentahydroxy-cyclohexanone
-
-
0.3
-
D,L-2,3,4,6/5-pentahydroxy-cyclohexanone
-
-
2.92
-
myo-Inositol
-
-
0.063
-
S-adenosyl-L-methionine
-
with myo-inositol as cosubstrate
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
proteome profile during salt-stress, up-regulation of RNA and protein expression following exposure to salinity, profiling of reaction product by gas chromatography, functional characterization of recombinant protein, regulation of pinitol synthesis pathway under different abiotic stresses, different plant species known to produce pinitol in response to stress listed, accumulation of D-pinitol via inositol is a stress-regulated pathway, presence of D-pinitol synthesizing protein/gene in a wild halophytic rice, absence in domesticated rice, adaptive feature in salt tolerance
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8.8
-
about 35% of maximal activity at pH 7.0 and pH 8.8
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
55
-
30C: about 40% of maximal activity, 55C: about 30% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
during normal growth IMT is repressed, after salinity stress IMT is induced
Manually annotated by BRENDA team
-
abiotic stress treatment
Manually annotated by BRENDA team
-
during normal growth IMT is repressed, after salinity stress IMT is induced
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
106200
-
-
gel filtration
additional information
-
-
40 kDa immunoreactive protein under stressed and unstressed conditions in wild rice, an about 60 kDa major band detected by antibodies in domesticated and in wild rice
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, SDS-PAGE; x * 40250, calculation from nucleotide sequence
?
-
2 * or 3 * 40300, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
3 h, at room temperature, about 45% loss of activity compared to maximal stability at pH 7.0-7.6
6.5
-
-
3 h, at room temperature, about 10% loss of activity compared to maximal stability at pH 7.0-7.6
7
7.6
-
3 h, at room temperature, maximal stability
8
-
-
3 h, at room temperature, about 30% loss of activity compared to maximal stability at pH 7.0-7.6
9
-
-
3 h, at room temperature, about 70% loss of activity compared to maximal stability at pH 7.0-7.6
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
-
30 min, stable up to
50
-
-
30 min, about 40% loss of activity
60
-
-
30 min, complete loss of activity
70
-
-
15 min, sensitive to heat
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sensitive to proteinase K treatment
-
activity is lost within a week, when the enzyme is frozen or kept at 4C without glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-30C, 25 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol, 2 mM MgCl2, 0.25 mM ammonium sulfate, 50% glycerol, half-life: 300 d
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gel filtration and SDS-PAGE, recombinant protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Arabidopsis thaliana cultivar Columbia
-
expressed in Glycine max
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21DE3 PLys(S) strain, pET15b vector
-