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Information on EC 5.5.1.4 - inositol-3-phosphate synthase
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5.5.1.4 inositol-3-phosphate synthaseIUBMB Comments
Requires NAD+, which dehydrogenates the -CHOH- group to -CO- at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1. Finally, the enzyme-bound NADH reconverts C-5 into the -CHOH- form.
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Word Map
- 5.5.1.4
-
nucleation
-
neuroblast
-
phytic
-
ice-nucleating
-
monophosphatase
-
cloud
-
halophytic
-
inositol-containing
-
cyclitols
- phytate
-
supercooled
- galactinol
-
hexakisphosphate
-
radiative
-
2-kinase
- impase
- medicine
- pharmacology
- biotechnology
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
inps, myo-inositol-1-phosphate synthase, mips1, inositol-1-phosphate synthase, mip synthase, pip synthase, myo-inositol 1-phosphate synthase, inositol-3-phosphate synthase, l-myo-inositol-1-phosphate synthase, sll1981, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1D-myo-inositol 3-phosphate synthase
1L-myo-Inositol-1-phosphate synthase
D-Glucose 6-phosphate cycloaldolase
-
-
-
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D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cyclase
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D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cycloaldolase
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D-Glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase
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D-Glucose-6-phosphate,L-myo-inositol-1-phosphate cycloaldolase
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D-myo-inositol-3-phosphate synthase
Glucocycloaldolase
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Glucose 6-phosphate cyclase
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Glucose-6-phosphate inositol monophosphate cycloaldolase
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INO-1
INO1
Ino1p
Inositol 1-phosphate synthase
Inositol 1-phosphate synthetase
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-
-
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inositol 3-phosphate synthase
inositol-3-phosphate synthase
INPS1
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IP synthase
IPS
L-myo-inositol 1-phosphate synthase
L-myo-Inositol 1-phosphate synthetase
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L-myo-Inositol-1-phosphate synthase
MI-1-P synthase
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MIP synthase
MIPS
MIPS1
myo-D-inositol 3-phosphate synthase
myo-inositol 1-phosphate synthase
myo-inositol phosphate synthase
myo-Inositol-1-P synthase
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Myo-inositol-1-phosphate synthase
RINO1 protein
Synthase, myo-inositol 1-phosphate
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1L-myo-Inositol-1-phosphate synthase
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Inositol 1-phosphate synthase
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IPS
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L-myo-Inositol-1-phosphate synthase
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MIP synthase
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MIPS
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Myo-inositol-1-phosphate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
reaction proceeds with stereospecific loss of the pro-6R and incorporation of the pro-6S hydrogen into the product. The ring closure thus occurs in a retention mode at C-6 of the substrate
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
reaction proceeds with stereospecific loss of the pro-6R and incorporation of the pro-6S hydrogen into the product. The ring closure thus occurs in a retention mode at C-6 of the substrate
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
RNA amounts are upregulated at least 5fold during salinity stress
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
reaction sequence: 1. Oxidation by NAD+ of C-5 of D-glucose 6-phosphate to give 5-oxo-D-glucose 6-phosphate, 2. aldol condensation between C-6 and C-1 of this molecule to give 1L-myo-inosose-2 1-phosphate, 3. reduction by the NADH first formed to give 1L-myo-inositol 1-phosphate. The NADH and oxidized intermediates are tightly bound
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
formation of 5-keto-D-glucose 6-phosphate as an enzyme-bound intermediate in the conversion of D-glucose 6-phosphate into 1L-myo-inositol 1-phosphate
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
pro-S specificity of the first step, the reversible oxidation of glucose 6-phosphate to 5-ketoglucose 6-phosphate and in the second oxidation-reduction step, the reduction of myo-inosose-2 1-phosphate to myo-inositol 1-phosphate
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
ordered sequential mechanism with NAD+ adding first
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
reaction sequence: 1. oxidation by NAD+ of C-5 of D-glucose 6-phosphate to give 5-oxo-D-glucose 6-phosphate, 2. aldol condensation between C-6 and C-1 of this molecule to give 1L-myoinosose-2 1-phosphate, 3. reduction by the NADH first formed to give 1L-myoinositol 1-phosphate. The NADH and oxidized intermediates are tightly bound
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
it is possible that the enzyme has an aldol step in the enzymatic pathway which is of neither classical aldolase type
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
it is possible that the enzyme has an aldol step in the enzymatic pathway which is of neither classical aldolase type
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
it is possible that the enzyme has an aldol step in the enzymatic pathway which is of neither classical aldolase type
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
mechanism, the phosphate-bearing carbon-atom in D-glucose 6-phosphate is the same atom which bears the phosphate in L-myo-inositol-1-phosphate
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
no upregulation of transcription by salinity stress
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
catalytic reaction mechanism
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
catalytic reaction mechanism involving K369, K412, K373, and K489
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
catalytic reaction mechanism, induced-fit active site formation by substrate binding
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
catalytic reaction mechanism, induced-fit active site formation by substrate binding
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D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
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D-glucose 6-phosphate = L-myo-inositol 1-phosphate
reaction mechanism involves 3 reaction steps: 1. oxidation by NAD+, 2. condensation to a cyclic molecule, 3. reduction by NADH
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D-glucose 6-phosphate = L-myo-inositol 1-phosphate
reaction mechanism, active site residues are T228, G229, T230, D261, K274, K278-K373, K306, D332, and K367, mechanism of phosphate and metal binding in the active site, overview
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D-glucose 6-phosphate = L-myo-inositol 1-phosphate
substrate binding and metal-dependent reaction mechanism, overview, active site residues are D225, K274, K278, K306, D332, and K367
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D-glucose 6-phosphate = L-myo-inositol 1-phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
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elimination/addition
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intramolecular
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-3-phosphate lyase (isomerizing)
Requires NAD+, which dehydrogenates the -CHOH- group to -CO- at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1. Finally, the enzyme-bound NADH reconverts C-5 into the -CHOH- form.
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CAS REGISTRY NUMBER
COMMENTARY
9032-95-5
-
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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
CDP-2,3-di-O-phytanyl-sn-glycerol + 1D-myo-inositol 1-phosphate
archaetidylinositol phosphate + CMP
-
-
-
-
?
2-deoxy-D-glucose 6-phosphate
5-deoxy-L-myo-inositol 1-phosphate
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at 11.5% of the activity relative to D-glucose 6-phosphate
-
-
?
D-2-Deoxy-2-fluoroglucose 6-phosphate
5-Deoxy-5-fluoro-myo-inositol 1-phosphate
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-
-
?
D-2-Deoxy-2-fluoroglucose 6-phosphate
5-Deoxy-5-fluoro-myo-inositol 1-phosphate
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at 0.2% of the activity relative to D-glucose 6-phosphate
-
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
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key enzyme in inositol biosynthesis, rate-limiting step
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?
D-glucose 6-phosphate
1D-inositol 3-phosphate
-
key enzyme in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
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the enzyme catalyzes critical steps in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
-
the enzyme catalyzes the first and rate-limiting step in biosynthesis of inositol-containg compounds
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
class II aldolase
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?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
rate-limiting step for de novo inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+
-
-
?
D-glucose 6-phosphate
1L-myo-inositol 1-phosphate
-
-
-
-
?
D-glucose 6-phosphate
1L-myo-inositol 1-phosphate
-
first and rate-limiting step in biosynthesis of all inositol-conatining compounds
-
-
?
D-glucose 6-phosphate
1L-myo-inositol 1-phosphate
-
determination of the catalytic reaction mechanism
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-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
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the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
key enzyme in myo-inositol biosynthetic pathway
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
first step in de novo biosynthesis of myo-inositol
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the key enzyme in the biosynthesis of myo-inositol, and the derivatives of myo-inositol like phytic acid and the inositol phosphatides
-
-
?
D-Glucose 6-phosphate
?
-
functional role of the myo-inositol oxidation pathway during in vivo conversion of glucose into galactosyluronic residues of pectin in germinating lilly pollen
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-glucose 6-phosphate
D-myo-inositol 3-phosphate
-
assay at pH 7.5, 37°C
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
reaction mechanism involves 3 reaction steps: 1. oxidation by NAD+, 2. condensation to a cyclic molecule, 3. reduction by NADH
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
absolute specificity for
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
key enzyme in phytate biosynthesis, a phosphate-rich storage molecule
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
reaction mechanism involves 3 reaction steps: 1. oxidation by NAD+, 2. condensation to a cyclic molecule, 3. reduction by NADH
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
no reversibility of the overall reaction is found
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
at least 5-fold preference for the beta-anomer
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
absolute specificity for
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
absolute specificity for
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
first and rate-limiting step in inositol biosynthesis followed by L-myo-inositol 1-phosphate dephosphorylation catalyzed by a Mg2+-dependent inositol 1-phosphatase, EC 3.1.3.25
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
important in myo-inositol level regulation
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
absolute specificity for
-
?
D-Mannose 6-phosphate
myo-Inositol 1-phosphate
-
at 11.5% of the activity relative to D-glucose 6-phosphate
-
-
?
additional information
?
-
-
development of a continuous spectrophotometric method for measuring MIPS activity using a coupled assay that allows the rapid characterization of MIPS in a multiwell plate format, method validation, overview
-
-
?
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
?
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
?
additional information
?
-
-
after removal of tightly bound NAD+ the enzyme catalyzes the reduction of 5-keto-D-glucitol 6-phosphate and 5-keto-D-glucose 6-phosphate by NADH to give glucitol 6-phosphate and glucose 6-phosphate respectively
-
-
?
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
?
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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-glucose 6-phosphate
1L-myo-inositol 1-phosphate
-
first and rate-limiting step in biosynthesis of all inositol-conatining compounds
-
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
-
key enzyme in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
-
the enzyme catalyzes critical steps in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
-
the enzyme catalyzes the first and rate-limiting step in biosynthesis of inositol-containg compounds
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
rate-limiting step for de novo inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
-
the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
key enzyme in myo-inositol biosynthetic pathway
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
first step in de novo biosynthesis of myo-inositol
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the key enzyme in the biosynthesis of myo-inositol, and the derivatives of myo-inositol like phytic acid and the inositol phosphatides
-
-
?
D-Glucose 6-phosphate
?
-
functional role of the myo-inositol oxidation pathway during in vivo conversion of glucose into galactosyluronic residues of pectin in germinating lilly pollen
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
key enzyme in phytate biosynthesis, a phosphate-rich storage molecule
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
first and rate-limiting step in inositol biosynthesis followed by L-myo-inositol 1-phosphate dephosphorylation catalyzed by a Mg2+-dependent inositol 1-phosphatase, EC 3.1.3.25
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
-
important in myo-inositol level regulation
-
-
?
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
?
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
?
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
different proportions of an NAD+-independent activity can be obtained depending on the conditions of extraction and dialysis
NAD+
-
the first partial reaction is the oxidation by NAD+ of C-5 of D-glucose 6-phosphate to give 5-oxo-D-glucose 6-phosphate
NAD+
Km: 0.153 mM for the native enzyme, Km: 0.166 mM, recombinant enzyme
NAD+
Km value of wild-type 0.166 mM, Km value of mutant lacking amino acids 174-210 0.451 mM
NAD+
Km value of wild-type 0.188 mM, Km value of mutant bearing amino acids 174-210 of Porteresia coarctata enzyme 0.451 mM
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
Co2+
-
absolute requirement for a divalent metal ion, Zn2+ or Mn2+ are the best activators, followed by Co2+
K+
Mg2+
Mn2+
Na+
NaCl
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
NH4+
phosphate
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
Zn2+
additional information
Mn2+
-
Km: 0.00077 mM, absolute requirement for a divalent metal ion, Zn2+ or Mn2+ are the best activators, followed by Co2+
Zn2+
-
Km: 0.0011 mM, absolute requirement for a divalent metal ion, Zn2+ or Mn2+ are the best activators, followed by Co2+
Zn2+
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
Zn2+
-
enzyme contains Zn2+. The nicotinamide moiety of the NAD+ cofactor is in the syn conformation about the N-glycosidic bond and is held there by coordination with the Zn2+ ion. N233, D235 and D310 provide ligands to a water molecule that coordinates the zinc ion
additional information
-
the activity of MIPS is moderately enhanced by the addition Mg2+ and is not enhanced by other divalent metal ions, such as Zn2+ and Mn2+
additional information
-
the native enzyme probably contains a bound divalent cation, Mg2+, Mn2+, or Zn2+, which is absolutely required for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2S,3S,6R)-3,4-dimethyl-6-(2-methylprop-1-en-1-yl)cyclohex-4-ene-1,2-dicarboxylic acid
ZINC04023366
(2S)-2-[(5R)-2,5,6-trimethylcyclohepta-1,6-dien-1-yl]pentanedioic acid
ZINC72320447
2,2,5,7-tetramethyl-1-oxo-2,3-dihydro-1H-indene-4-carboxylic acid
ZINC00137063
2-(2-methyl-1H-pyrrol-1-yl)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxylic acid
ZINC03844222
2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate
-
binding structure, interaction with active site residues, overview
2-deoxy-glucitol-6-phosphate
-
the inhibitor induces folding of the catalytic domain
5-methyl-4-phenyl-2-(1H-pyrrol-1-yl)thiophene-3-carboxylic acid
ZINC03844214
D-glucose 6-phosphate
-
the beta-anomer is preferred as substrate, the alpha-anomer is an inhibitor
diphosphate
-
inhibition occurs only in the presence of NH4+. Inhibition is pH-dependent. The inhibition of enzyme activity by diphosphate, at pH 7.7, is reversed in decreasing order of effectiveness by Mn2+, Fe3+, Mg2+, Co2+, Cu2+, Ca2+, Ba2+ and Zn2+
NaBH4
-
partial inactivation in presence of NAD+. No inactivation in absence of NAD+
p-Substituted mercuribenzoate
-
1 mM, 93% inhibition in presence of 1 mM NADH
phosphate
the enzyme activity is almost completely abolished at 125 mM
sodium hexametaphosphate
the enzyme activity is almost completely abolished at 20 mM
valnoctamide
-
valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate, competitive
valrocemide
-
valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate
Inositol
-
feedback/product inhibition by inhibition of INO1 gene transcription, acts as a metabolic sensor
Li+
-
14 mM, 50% inhibition in absence of NH4+. Only 10% inhibition in presence of 14 mM NH4+
Valproate
-
noncompetitive, specific, only in vivo, e.g. in brain post mortem, no inhibition of the purified rcombinant enzyme in vitro
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
leaf L-myo-inositol 1-phosphate concentration increases 40fold during the first 6 h of salt stress (exposure to 300 mM NaCl)
NH4+
-
10-14 mM NH4Cl, 5fold stimulation. Other NH4+ salts are strong inhibitors
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
The Inositol-3-Phosphate Synthase Biosynthetic Enzyme Has Distinct Catalytic and Metabolic Roles.
Brain Neoplasms
Earmuff restricts progenitor cell potential by attenuating the competence to respond to self-renewal factors.
Brain Neoplasms
klumpfuss distinguishes stem cells from progenitor cells during asymmetric neuroblast division.
Breast Neoplasms
Delivery as nanoparticles reduces imatinib mesylate-induced cardiotoxicity and improves anticancer activity.
Carcinoma
Improving drug accumulation and photothermal efficacy in tumor depending on size of ICG loaded lipid-polymer nanoparticles.
Cardiotoxicity
Delivery as nanoparticles reduces imatinib mesylate-induced cardiotoxicity and improves anticancer activity.
Dehydration
Ectopic expression of the ABA-inducible dehydration-responsive chickpea L-myo-inositol 1-phosphate synthase 2 (CaMIPS2) in Arabidopsis enhances tolerance to salinity and dehydration stress.
Dehydration
Importance of inositols and their derivatives in cowpea under root dehydration: An omics perspective.
Glioma
Distributions of intravenous injected iodine nanoparticles in orthotopic u87 human glioma xenografts over time and tumor therapy.
Glioma
Myo-inositol concentration in MR spectroscopy for differentiating high grade glioma from primary central nervous system lymphoma.
Infections
Minimum detectable level of Salmonellae using a binomial-based bacterial ice nucleation detection assay (BIND).
Infertility, Male
Disruption of INOS, a Gene Encoding myo-Inositol Phosphate Synthase, Causes Male Sterility in Drosophila melanogaster.
Leishmaniasis
In-silico studies on Myo inositol-1-phosphate synthase of Leishmania donovani in search of anti-leishmaniasis.
Lung Neoplasms
Antibody Conjugated PLGA Nanoparticles for Targeted Delivery of Paclitaxel Palmitate: Efficacy and Biofate in a Lung Cancer Mouse Model.
Lymphogranuloma Venereum
Candidate vaginal microbicides with activity against Chlamydia trachomatis and Neisseriagonorrhoeae.
Microcephaly
Retinoic acid controls early neurogenesis in the developing mouse cerebral cortex.
Neoplasms
Antibody Conjugated PLGA Nanoparticles for Targeted Delivery of Paclitaxel Palmitate: Efficacy and Biofate in a Lung Cancer Mouse Model.
Neoplasms
Distributions of intravenous injected iodine nanoparticles in orthotopic u87 human glioma xenografts over time and tumor therapy.
Neoplasms
Improving drug accumulation and photothermal efficacy in tumor depending on size of ICG loaded lipid-polymer nanoparticles.
Neoplasms
INPS: predicting the impact of non-synonymous variations on protein stability from sequence.
Neoplasms
Iodine nanoparticle radiotherapy of human breast cancer growing in the brains of athymic mice.
Neoplasms
Musashi2 promotes the progression of pancreatic cancer through a novel ISYNA1-p21/ZEB-1 pathway.
Trypanosomiasis, African
Screening the MayBridge Rule of 3 Fragment Library for Compounds That Interact with the Trypanosoma brucei myo-Inositol-3-Phosphate Synthase and/or Show Trypanocidal Activity.
Tuberculosis
Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis.
Tuberculosis
Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1-phosphate synthase enzyme.
Tuberculosis
Studies of inositol 1-phosphate analogues as inhibitors of the phosphatidylinositol phosphate synthase in mycobacteria.
Tuberculosis
[Organization of the 1st 9 international courses on the "Epidemiology and Control of Tuberculosis" for physicians treating tuberculosis, held at the Istituto "C. Forlanini" of the INPS of Rome]
Tuberculosis
[Report of the scientific and didactic activity of the tuberculosis clinic of the University of Rome, and the Carlo Forlanini sanatorium and study center of the INPS in the year 1965]
Tuberculosis
[SCIENTIFIC AND DIDACTIC ACTIVITIES OF THE TUBERCULOSIS CLINIC, THE CENTER OF STUDIES AND THE OSPEDALE "CARLO FORLANINI" OF THE INPS DURING THE YEAR 1964.]
Tuberculosis, Pulmonary
[Observation on "1st admittance" cases of pulmonary tuberculosis in the Ospedale Sanitoriale INPS di Rovigo. (Clinico-statistical investigation related to the last 2-year period)]
Tuberculosis, Pulmonary
[The incidence of pulmonary tuberculosis in childhood (0-12 years) in the records of the Ospedale Sanatoriale INPS of Cagliari.]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.67 - 0.72
D-glucose 6-phosphate
-
pH 7.5, 30°C, dependent on the assay method, presence or absence of Mg2+
3.19
D-glucose 6-phosphate
mutant bearing amino acids 174-210 of Porteresia coarctata enzyme, 37°C
1.95
glucose 6-phosphate
-
cytosolic enzyme from streptomycin-bleached cells, and chloroplastidic enzyme
additional information
additional information
-
dissociation constants
-
additional information
additional information
-
kinetics, effects of different divalent metal ions, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0817
D-glucose 6-phosphate
-
pH 7.5, 30°C, periodate assay method, in absence of 1 mM Mg2+
0.102
D-glucose 6-phosphate
-
pH 7.5, 30°C, periodate assay method, in presence of 1 mM Mg2+
0.107
D-glucose 6-phosphate
-
pH 7.5, 30°C, IMP-coupled assay method, in presence of 1 mM Mg2+
0.3
D-glucose 6-phosphate
-
pH 7.5, 30°C, IMP-coupled assay method, in presence of 10 mM Mg2+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
D-glucose 6-phosphate
-
pH 7.5, 30°C, periodate assay method, in absence of 1 mM Mg2+
0.14
D-glucose 6-phosphate
-
pH 7.5, 30°C, periodate assay method, in presence of 1 mM Mg2+
0.157
D-glucose 6-phosphate
-
pH 7.5, 30°C, IMP-coupled assay method, in presence of 1 mM Mg2+
0.233
D-glucose 6-phosphate
-
pH 7.5, 30°C, IMP-coupled assay method, in presence of 10 mM Mg2+
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0003
-
crude enzyme, in 50mM Bicine buffer (pH 8.5), at 60°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
7.6
7.7
7.8
8 - 8.5
mutant bearing amino acids 174-210 of Porteresia coarctata enzyme
8.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
34% of maximal activity at pH 9.0, low activity below pH 5.0, inactive above pH 11.0
6.5 - 9.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 95% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
35 - 37
37
40
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
increasing activity from 20°C to 40 °C, rapid loss of 60% activity at 50°C, inactive at 60°C
76 - 100
-
76°C: about 40% of maximal activity, 100°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression is upregulated under cold and heat stress
SwissProt
brenda
gene mips1; three MIPS genes mips1, mips2, and mips3
UniProt
brenda
gene mips2; three MIPS genes mips1, mips2, and mips3
UniProt
brenda
gene mips3; three MIPS genes mips1, mips2, and mips3
UniProt
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
salt-resistant enzyme, direct correlation between increased sythesis of inositol under salinity stress by the enzyme and salt tolerance
-
-
brenda
two enzyme forms: MW 33000 and MW 56000. Its expression is temporally and spatially regulated
-
-
brenda
-
-
-
brenda
strain PCC6803, bifunctional inositol-3-phosphate synthase/acetolactate synthase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
transcript levels increase in unfertilized ovaries and significant amounts are present during the recovery period
brenda
additional information
-
grown in a fermenter in an inositol-deficient medium
brenda
-
highly expressed in developing seed embryos and in the aleurone layer
brenda
constitutive accumulation of its transcript is seen in flower and developing silique tissues
brenda
isoenzyme AtMIPS2-1 is largely heat inducible at the various growth stages such as seedling, flower, developing silique and mature siliques
brenda
isoenzyme OsMIPS1-3: OsMIPS1-3 shows a more or less constitutive expression in different abiotic stresses in shoots, roots, panicle stages, and various developing seed stages
brenda
isoenzyme OsMIPS1-1: expression is largely responsive to abiotic stress in the root tissue, its expression is induced by drought, NaCl, cold, abscisic acid, brassinosteroid and salicylic acid
brenda
isoenzyme OsMIPS1-2: low expression expression comparable to splice varian OsMIPS1
brenda
isoenzyme OsMIPS1-3: OsMIPS1-3 shows a more or less constitutive expression in different abiotic stresses in shoots, roots, panicle stages, and various developing seed stages
brenda
isoenzyme TaMIPS1 shows constitutive expression in both roots as well as shoots
brenda
is induced by abiotic stresses in 2-week-old seedlings
brenda
isoenzyme AtMIPS2-1 is largely heat inducible at the various growth stages such as seedling, flower, developing silique and mature siliques
brenda
-
seed-specific expression of isoform GmMIPS-1 in the outer integumentary layer during early seed development. Enzyme is associated with oxalate crystal idioblasts
brenda
isoenzyme OsMIPS1-1: expression during seed development comparable to splice variant OsMIPS1: Seed of 20 DAP stage has the highest expression followed by 10 and 30 DAP stages
brenda
isoenzyme OsMIPS1-2: expression during seed development comparable to splice variant OsMIPS1: Seed of 20 DAP stage has the highest expression followed by 10 and 30 DAP stages
brenda
isoenzyme OsMIPS1-3: OsMIPS1-3: expression during seed development comparable to splice variant OsMIPS1: Seed of 20 DAP stage has the highest expression followed by 10 and 30 DAP stages
brenda
isoenzyme OsMIPS1: expression largely seed-specific: Seed of 20 DAP stage has the highest expression followed by 10 and 30 DAP stages
brenda
presence of gene transcripts, peak at 9 days after pollination
brenda
transcript is expressed during different developing seed stages upon heat stress
brenda
AtMIPS3 is stress inducible in the shoot by heat stress, mannitol, ABA, cold and NaCl
brenda
isoenzyme OsMIPS1-2: low expression expression comparable to splice varian OsMIPS1
brenda
isoenzyme OsMIPS1-3: OsMIPS1-3 shows a more or less constitutive expression in different abiotic stresses in shoots, roots, panicle stages, and various developing seed stages
brenda
isoenzyme TaMIPS1 shows constitutive expression in both roots as well as shoots
brenda
constitutive accumulation of its transcript is seen in flower and developing silique tissues
brenda
isoenzyme AtMIPS2-1 is largely heat inducible at the various growth stages such as seedling, flower, developing silique and mature siliques
brenda
additional information
-
isoform MIPS1 is expressed in most cell types and developmental stages while isoforms MIPS2 and MIPS3 are mainly restricted to vascular or related tissues
brenda
additional information
MIPS tissue expression analysis, overview
brenda
additional information
almost no expression in skeletal muscle
brenda
additional information
-
the enzyme activity is maximal during the logarithmic stage of growth and is decreased in the stationary phase
brenda
additional information
expression analysis in wild-type and ipa 1-1 mutant leaves
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
MW 33000 enzyme form, thylakoid membrane of fractionated leaf chloroplasts
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
loss in MIPS1 results in smaller plants with curly leaves and spontaneous production of lesions
malfunction
-
the inositol 3-phosphate synthase-deficient mutant is not virulent in mice and loses viability in macrophages
malfunction
-
the inositol 3-phosphate synthase-deficient mutant is not virulent in mice and loses viability in macrophages
malfunction
-
the inositol 3-phosphate synthase-deficient mutant is not virulent in mice and loses viability in macrophages
malfunction
-
the inositol 3-phosphate synthase-deficient mutant is not virulent in mice and loses viability in macrophages
malfunction
-
the inositol 3-phosphate synthase-deficient mutant is virulent in mice as the wild type
malfunction
endomembrane function in embryo cells is impaired in the mips1mips3 double mutant. Mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant phenotypes, overview
malfunction
null mips1 mutants are defective in embryogenesis, cotyledon venation patterning, root growth, and root cap development. The mutant roots are also agravitropic and have reduced basipetal auxin transport. mips1 mutants have significantly reduced levels of major phosphatidylinositols and exhibit much slower rates of endocytosis, as well as altered PIN2 trafficking, phenotype, detailed overview
malfunction
-
overexpression in Arabidopsis provides significantly improved tolerance to salt stress during germination and seedling growth and development. Transgenics retain more chlorophyll and carotenoid by protecting the photosystem II. The low level of stress-induced cellular damage in the transgenics is clearly evident by lower accumulation of proline in comparison to wild-tpye
malfunction
-
seed-specific silencing of MIPS in transgenic rice plants leads to substantial reduction in levels of phytic acid along with an increase in phosphate content. Low phytate seeds have an undesirable diminution in levels of myo-inositol and ascorbate possibly leading to sensitiveness of seeds to abscisic acid during germination
malfunction
transgenic expression of CaMIPS2 in Arabidopsis enhances tolerance to salinity and dehydration stress
malfunction
transgenic expression of isoenzyme CaMIPS1 in Arabidopsis improves tolerance to salinity and dehydration stress but not as strong as transgenic expression of isoenzyme CaMIPS2
malfunction
enzyme loss causes a pleiotropic phenotype, triggers inositol depletion and results in an inositol auxotrophy
malfunction
-
null mips1 mutants are defective in embryogenesis, cotyledon venation patterning, root growth, and root cap development. The mutant roots are also agravitropic and have reduced basipetal auxin transport. mips1 mutants have significantly reduced levels of major phosphatidylinositols and exhibit much slower rates of endocytosis, as well as altered PIN2 trafficking, phenotype, detailed overview
-
metabolism
MIPS catalyzes the rate-limiting step in de novo synthesis of myo-inositol
metabolism
myo-inositol-1-phosphate synthase is a conserved enzyme that catalyzes the first committed and rate-limiting step in inositol biosynthesis
metabolism
-
the reaction catalyzed by MIPS is the first step in the biosynthesis of inositol and inositol-containing molecules that serve important roles in both eukaryotes and prokaryotes
metabolism
-
myo-inositol-1-phosphate synthase is a conserved enzyme that catalyzes the first committed and rate-limiting step in inositol biosynthesis
-
physiological function
isoform gammac negatively modulates alpha isoform activity, possibly by competing for NAD+, when the gammac isoform is preincubated with NAD+, prior to incubation with the alpha isoform, the decrease is quite pronounced with enzyme activity falling to about 63% at the end of 1 h and to about 40% at the end of 3 h
physiological function
-
isoform MIPS1, but not MIPS2 or MIPS3, is required for seed development, for physiological responses to salt and abscisic acid, and to suppress cell death
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
-
MIPS is a pivotal biosynthetic enzyme in the myo-inositol pathway, including the synthesis of phytic acid
physiological function
MIPS plays an important role in the defensive mechanisms of Ricinus communis against drought stress
physiological function
MIPS1 is required for multiple developmental processes. It is critical for maintaining phosphatidylinositol levels and affects pattern formation in plants likely through regulation of auxin distribution. MIPS1 is required for embryo development and vascular patterning
physiological function
isoenzyme CaMIPS1 and CaMIPS2 are successfully complemented and shown to repair the defect of seedling growth and altered seed phenotype of Atmips1 mutant
physiological function
-
expression of myo-inositol 3-phosphate synthase confers salt tolerance in rice
physiological function
-
MIPS1 is required for multiple developmental processes. It is critical for maintaining phosphatidylinositol levels and affects pattern formation in plants likely through regulation of auxin distribution. MIPS1 is required for embryo development and vascular patterning
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
165000
179000
180000
210000
-
testis, gel filtration, PAGE, ultracentrifugal equilibrium sedimentation
260000
50000
56300
56500
59000
60000
60100
-
x * 65000, MALDI-TOF, x * 60100, calculated for acetolactate synthase large subunit which is identical to enzyme
61000
62000
65000
67000
68000
65000
-
x * 65000, MALDI-TOF, x * 60100, calculated for acetolactate synthase large subunit which is identical to enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
tetramer
trimer
additional information
?
-
two enzyme forms: MW 33000 and MW 56000 determined by SDS-PAGE. Its expression is temporally and spatially regulated
?
-
x * 65000, MALDI-TOF, x * 60100, calculated for acetolactate synthase large subunit which is identical to enzyme
additional information
-
the protomer contains 2 domains, a Rossman fold with a C-terminal extension D1a, and a domain involving tetramerization D1b
additional information
-
structure of the enzyme-NAD+-2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex
additional information
-
the protomer contains 3 domains, a catalytic domain, a central domain, and an NAD+ binding domain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, protein solution containing 8 mg/ml or 16 mg/ml protein, 50 mM Tris, pH 7.5, 1 mM EDTA, versus HEPES, pH 7.5, 2% v/v PEG 400, 2.0 M ammonium sulfate, and 30% w/v PEG 1500 in equal volumes, 2-3 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
-
hanging-drop vapour-diffusion method, crystal structure of native and selenomethionine-bound enzyme at 1.95 resolution, bound to the cofactor NAD+
-
hanging-drop vapour-diffusion method, selenomethionine-substituted enzyme, 2.65 A crystal structure of recombinant enzyme
-
purified apo-enzyme and in complex with NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate, complexing by soaking of apo-enzyme crystals in 5% PEG 8000, 0.1 M NaAc, pH 5.5, 1 mM NAD+, and 13.5 mM 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate for 24 h, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
structure of the 1L-myo-inositol 1-phosphate synthase/NAD+/2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex
-
structure of the enzyme both completely devoid of NAD+ and completely occupied with NAD+, structure at 1.7 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D225A
-
site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
D332A
-
site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps
K274A
-
site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
K278A
-
site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
K306A
-
site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps
K367A
-
site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
L257A
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
N255A
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows reduced activity
K369A
K412A
K489A
additional information
K369A
-
site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
K412A
-
site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
K489A
-
site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
additional information
construction of transgenic plants expressing GFP-tagged MIPS using Agrobacterium tumefaciens GV3101 transfection method, overview
additional information
single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
-
single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
-
construction of transgenic plants expressing GFP-tagged MIPS using Agrobacterium tumefaciens GV3101 transfection method, overview
-
additional information
-
the human enzyme can functionally complement the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain
additional information
-
significant reduction of enzyme expression by use of phosphorothioate-modified antisense oligodeoxyribonucleotides. Treatment results in reduced level of mycothiol and the proliferation of Mycobacterium tuberculosis, enhanced susceptibility to antibiotics isoniazid, vancomycin and rifampin and decreased tolerance to H2O2
additional information
A 37-amino acid stretch between W174 and S210 is the salt-tolerance determinant domain of enzyme. Deletion of this stretch results in loss of salt tolerance, introduction of stretch into Brassica juncea or Oryza sativa enzyme provides salt tolerance properties
additional information
-
A 37-amino acid stretch between W174 and S210 is the salt-tolerance determinant domain of enzyme. Deletion of this stretch results in loss of salt tolerance, introduction of stretch into Brassica juncea or Oryza sativa enzyme provides salt tolerance properties
additional information
-
functional introgression of enzyme gene confers salt-tolerance to several organisms such as Escherichia coli, Schizosaccharomyces pombe, Oryza sativa and Brassica juncea albeit to varialbe extent. Direct correlation between increased synthesis of inositol under salinity stress by the enzyme and salt tolerance
additional information
a 37-amino acid stretch between W174 and S210 is the salt-tolerance determinant domain of Porteresia coarctata enzyme. Introduction of this stretch into Oryza sativa enzyme provides salt tolerance properties
additional information
-
the enzyme-deficient ino1 mutant strain can be functionally complemented by expression of the human enzyme
additional information
-
the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain FY250 can be functionally complemented by expression of sll1722
additional information
-
enzyme gene can complement inositol auxotroph Saccharomyces cerevisiae strain FY250 and the natural inositol auxotroph Schizosaccharomyces pombe
additional information
maize mutant ipa 1-1 produces kernels containing low phytic acid, reducd by 66% compared to the wild-type maize kernels probably due to a mutation in the gene encoding the enzyme, i.e. gene MIPS, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
98
-
loss of 50% activity after about 40 min in 50 mM Tris-HCl, pH 8.0
additional information
additional information
-
addition of NAD+ increases thermotolerance of both cytosolic and chloroplast enzyme isoforms
additional information
-
the lower thermal stability of the fetal enzyme increases in presence of added NAD+, 0.8 mM, whereas the higher thermal stability of the adult brain enzyme declines when NAD+ is specifically removed from the enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% v/v glycerol, 2 mM PMSF, and 1 mM E-64 stabilize the native and the recombinant enzyme
-
the lower thermal stability of the fetal brain enzyme increases in presence of added NAD+, 0.8 mM, whereas the higher thermal stability of the adult brain enzyme declines when NAD+ is specifically removed from the enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, BioGel A purified fractions (final purification fraction), 5-7 days
-20°C, purified recombinant enzyme, 20% v/v glycerol, completely stable for several weeks
-
0°C, 70% loss of activity after 18 h, enzyme in crude extract. Stabilization by (NH4)2SO4 and dimethyl sulfoxide in 20% solution
-
4°C, very stable in 0.1 M Tris-acetate buffer, pH 7.8, 14% loss of activity after 7 days and 51% loss of activity after 1 month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate saturation, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
DEAE-Sephacel column chromatography and Superose 12 gel filtration
enzyme is purified 51fold using ammonium sulfate fractionation followed by successive chromatography through DEAE cellulose and BioGel A columns
from the reproductive pinnules by low-speed centrifugation, streptomycin sulfate precipitation, ammonium sulafte fractionation, DEAE ion exchange chromatography, and gel filtration
Gleichenia glauca
-
partial
partially purified by ammonium sulfate fractionation (50-70%)
-
recombinant enzyme
recombinant His-tagged INOS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant, solubilized and refolded enzyme from Escherichia coli strain BL21(DE3) and native enzyme by ion exchange chromatography and gel filtration
-
Superose12 gel filtration and DEAE Sephace gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression of His-tagged INOS in Escherichia coli strain BL21(DE3)
-
enzyme is encoded by sll1722, an unassigned open reading frame, phylogenetic analysis, subcloning and overexpression in Escherichia coli strains DH5alpha and BL21(DE3) in inclusion bodies
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and Mycobacterium smegmatis strain mc24517
-
expression in Escherichia coli
gene INO1, DNA sequence analysis, expression is regulated by inositol and Opi1p, phylogenetic analysis
-
gene ISYNA1 is upregulated by E2F1 acting on the minimal promoter, which can be suppressed by retinoblastoma protein, E2F1 functional binding motif determination at -117 overlapping an Sp1 motif, upregulation probably by interaction with several other low-affinity E2F1 binding motifs
-
gene MIPS, DNA and amino acid sequence determination and analysis, sequence comparisons, semi-quantitative RT-PCR expression analysis in different tissues
isoform gammac is expressed in Escherichia coli Rosetta (DE3) pLysS cells
MIPS genes mips1, mips2, and mips3, phylogenetic analysis, the three Arabidopsis thaliana MIPS genes show dynamic expression patterns during Arabidopsis embryo development. They all functionally rescue the yeast ino1 mutant, which is defective in yeast MIPS gene INO1
overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AtMIPS2-1 is largely heat inducible at the various growth stages such as seedling, flower, developing silique and mature siliques
AtMIPS3 is stress inducible in the shoot by heat stress, mannitol, ABA, cold and NaCl
CaMIPS2 is an early dehydration-responsive gene and is also rapidly induced by exogenous ABA application
expression highest at the young fruit stage
isoenzyme OsMIPS1-1: expression is largely responsive to abiotic stress in the root tissue, its expression is induced by drought, NaCl, cold, ABA, BR and SA
isoenzyme OsMIPS2: expression is considerably high in the unfertilized flower and during panicle development
isoenzyme TaMIPS2 is highly inducible by heat stress in both root and shoot tissues of wheat seedlings at different time points
MIPS expression is increased in leaves, stems, and roots after drought stress
seawater acclimation results in a 2.5fold increase in mRNA expression
seawater acclimation results in large (6-32fold) increases in mRNA expression
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization and recvery of about 90% of the recombinant enzyme from inclusion bodies by 8 M urea, refolding in 20 mM Tris-HCl, pH 7.6, 0.5 M NaCl, and 10 mM 2-mercaptoethanol
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
the enzyme is a possible target for genetic modification of maize plants to get low phytic acid containing variants
medicine
pharmacology
synthesis
medicine
-
anticonvulsants valnoctamide and valrocemide drastically reduce enzyme activity in crude brain homogenate
medicine
the common inositol-reversible effects of mood stabilizers lithium, valproate and carbamazepine on neurons are independent of enzyme and of sodium-dependent myo-inositol transporters
pharmacology
-
the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs
pharmacology
-
the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs
synthesis
production of myo-inositol from glucose by a novel trienzymatic cascade of polyphosphate glucokinase, inositol 1-phosphate synthase and inositol monophosphatase. myo-Inositol (inositol) is important in the cosmetics, pharmaceutical and functional food industries. The conversion ratio from glucose to inositol reaches 90%, which is promising for the enzymatic synthesis of inositol without ATP supplementation
synthesis
-
production of myo-inositol from glucose by a novel trienzymatic cascade of polyphosphate glucokinase, inositol 1-phosphate synthase and inositol monophosphatase. myo-Inositol (inositol) is important in the cosmetics, pharmaceutical and functional food industries. The conversion ratio from glucose to inositol reaches 90%, which is promising for the enzymatic synthesis of inositol without ATP supplementation
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishitani, M.; Majumder, A.L.; Bornhouser, A.; Michalowski, C.B.; Jensen, R.G.; Bohnert, H.J.
Coordinate transcriptional induction of myo-inositol metabolism during environmental stress
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537-548
1996
Arabidopsis thaliana, Mesembryanthemum crystallinum
brenda
Sherman, W.R.; Stewart, M.A.; Zinbo, M.
Mass spectrometric study on the mechanism of D-glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase
J. Biol. Chem.
244
5703-5708
1969
Bos taurus
brenda
Rasheed, A.; Corina, D.L.; Barnett, J.E.G.
Partial reactions of D-glucose 6-phosphate-1L-myoinositol 1-phosphate cyclase from rat testis
Biochem. J.
126
15P
1972
Rattus norvegicus
brenda
Brunner A.L.; Pina, M.Z.; Chagoya de Sanchez, V.; Pina, E.
Effect of (NH4)2SO4 and glycerol on the preservation of the "NAD+-independent" activity of D-glucose-6-phosphate,L-myo-inositol-1-phosphate cycloaldolase from Neurospora crassa
Arch. Biochem. Biophys.
150
32-37
1972
Neurospora crassa
brenda
Barnett, J.E.G.; Rasheed, A.; Corina, D.L.
Partial reactions of D-glucose 6-phosphate-1L-myoinositol 1-phosphate cyclase
Biochem. J.
131
21-30
1973
Rattus norvegicus
brenda
Pittner, F.; Fried, W.; Hoffman-Ostenhof, O.
Studies on the biosynthesis of cyclitols, XXX. Purification of myo-inositol-1-phosphate synthase of rat testes to homogeneity by affinity chromatography on NAD-Sepharose
Hoppe-Seyler's Z. Physiol. Chem.
355
222-224
1974
Rattus norvegicus
brenda
Barnett, J.E.G.; Rasheed, A.; Corina, D.L.
Inhibitors of inositol cyclase (D-glucose 6-phosphate-1L-myoinositol 1-phosphate cycloaldolase) from rat testis
Biochem. Soc. Trans.
1
1267-1269
1973
Rattus norvegicus
brenda
Naccarato, W.F.; Ray, R.E.; Wells, W.W.
Biosynthesis of myo-inositol in rat mammary gland. Isolation and properties of the enzymes
Arch. Biochem. Biophys.
164
194-201
1974
Rattus norvegicus
brenda
Pina, M.Z.; Brunner, A.; Chagoya de Sanchez, V.; Pina, E.
The regulation of myo-inositol-1-phosphate-synthase activity from Neurospora crassa by pyrophosphate and some cations
Biochim. Biophys. Acta
384
501-507
1975
Neurospora crassa
brenda
Ogunyemi, E.O.; Pittner, F.; Hoffmann-Ostenhof, O.
Studies on the biosynthesis of cyclitols, XXXVI. Purification of myo-inositol-1-phosphate synthase of duckweed, Lemna gibba to homogeneity by affinity chromatography on NAD-Sepharose. Molecular and catalytic properties of the enzyme
Hoppe-Seyler's Z. Physiol. Chem.
359
613-616
1978
Lemna gibba
brenda
Mauck, L.A.; Wong, Y.H.; Sherman, W.R.
L-myo-Inositol-1-phosphate synthase from bovine testis: purification to homogeneity and partial characterization
Biochemistry
19
3623-3629
1980
Bos taurus
brenda
Maeda, T.; Eisenberg jr., F.
Purification, structure, and catalytic properties of L-myo-inositol-1-phosphate synthase from rat testis
J. Biol. Chem.
255
8458-8464
1980
Rattus norvegicus
brenda
Donahue, T.F.; Henry, S.A.
myo-Inositol-1-phosphate synthase. Characteristics of the enzyme and identification of its structural gene in yeast
J. Biol. Chem.
256
7077-7085
1981
Saccharomyces cerevisiae
brenda
Sherman, W.R.; Loewus, M.W.; Pina, M.Z.; Wong, Y.H.H.
Studies on myo-inositol-1-phosphate synthase from Lilium longiflorum pollen, Neurospora crassa and bovine testis. Further evidence that a classical aldolase step is not utilized
Biochim. Biophys. Acta
660
299-305
1981
Bos taurus, Lilium longiflorum, Neurospora crassa
brenda
Escamilla, J.E.; Contreras, M.; Martinez, A.; Zentella-Pina, M.
L-Myoinositol-1-phosphate synthase from Neurospora crassa: purification to homogeneity and partial characterization
Arch. Biochem. Biophys.
218
275-285
1982
Neurospora crassa
brenda
Wong, Y.H.H.; Mauck, L.A.; Sherman, W.R.
L-myo-Inositol-1-phosphate synthase from bovine testis
Methods Enzymol.
90
309-314
1982
Bos taurus
brenda
Adhikari, J.; Majumder, A.L.
Differences in the thermal stability of the fetal and adult brain myo-inositol-1-phosphate synthase
FEBS Lett.
163
46-49
1983
Rattus norvegicus
brenda
Loewus, M.W.; Bedgar, D.L.; Loewus, F.A.
1L-myo-Inositol 1-phosphate synthase from pollen of Lilium longiflorum
J. Biol. Chem.
259
7644-7647
1984
Lilium longiflorum
brenda
Wong, Y.H.H.; Sherman, W.R.
Anomeric and other substrate specificity studies with myo-inositol-1-P synthase
J. Biol. Chem.
260
11083-11090
1985
Bos taurus
brenda
Loewus, M.W.; Tupy, J.; Loewus, F.A.
1L-myo-Inositol-1-phosphate synthase in serum from Hevea latex
Plant Sci.
44
29-32
1986
Hevea brasiliensis
-
brenda
Eisenberg jr., F.; Parthasarathy, R.
Measurement of biosynthesis of myo-inositol from glucose 6-phosphate
Methods Enzymol.
141
127-143
1987
Rattus norvegicus
brenda
Johnson, M.D.
The Arabidopsis thaliana myo-inositol 1-phosphate synthase (EC 5.5.1.4)
Plant Physiol.
105
1023-1024
1994
Arabidopsis thaliana
brenda
Migaud, M.E.; Frost, J.W.
Elaboration of a general strategy for inhibition of myo-inositol 1-phosphate synthase: active site interactions of analogues possessing oxidized reaction centers
J. Am. Chem. Soc.
118
495-501
1996
Saccharomyces cerevisiae
-
brenda
Migaud, M.E.; Frost, J.W.
Inhibition of myo-inositol-1-phosphate synthase by a reaction coordinate intermediate
J. Am. Chem. Soc.
117
5154-5155
1995
Homo sapiens
-
brenda
Sipos, L.; Szabo, G.
Myo-inositol-1-phosphate synthase in different Streptomyces griseus variants
FEMS Microbiol. Lett.
65
339-344
1989
Streptomyces sp.
brenda
Feth, F.; Wagner, R.; Baydoun, H.; Wray, V.; Wagner, K.G.
Medium scale production of L-myo-inositol 1-phosphate
Biotechnol. Appl. Biochem.
12
364-369
1990
Saccharomyces cerevisiae
brenda
Ogunyemi, E.O.
Purification and characterisation of myo-inositol-1-phosphate synthase of the yeast Candida utilis
Biokemistri
4
97-102
1994
Cyberlindnera jadinii
-
brenda
Adhikari, J.; Majumder, A.L.
L-Myo-inositol-1-phosphate synthase from mammalian brain: partial purification and characterisation of the fetal and adult enzyme
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25
408-412
1988
Homo sapiens, Rattus norvegicus
brenda
RayChaudhuri, A.; Hait, N.C.; das Gupta, S.; Bhaduri, T.J.; Deb, R.; Majumder, A.L.
L-myo-Inositol 1-phosphate synthase from plant sources
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115
727-736
1997
Saccharomyces cerevisiae, Euglena gracilis, Oryza sativa, Vigna radiata, Arthrospira platensis
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1L-myo-Inositol-1-phosphate synthase
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1348
245-256
1997
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brenda
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Biosynthesis of inositol in yeast. Primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus
J. Biol. Chem.
264
1274-1283
1989
Saccharomyces cerevisiae
brenda
Dean Johnson, M.; Wang, X.
Differentially expressed forms of 1-L-myo-inositol-1-phosphate synthase (EC 5.5.1.4) in Phaseolus vulgaris
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271
17215-17218
1996
Phaseolus vulgaris
brenda
Byun, S.M.; Jenness, R.
Stereospecificity of L-myo-inositol-1-phosphate synthase for nicotinamide adenine dinucleotide
Biochemistry
20
5174-5177
1981
Rattus norvegicus
brenda
Loewus, M.W.; Loewus, F.A.
The C-5 hydrogen isotope-effect in myo-inositol 1-phosphate synthase as evidence for the myo-inositol oxidation-pathway
Carbohydr. Res.
82
333-342
1980
Lilium longiflorum
brenda
Pittner, F.; Hoffmann-Ostenhof, O.
Preparation of homogeneous crystals of myo-inositol 1-phosphate synthase from rat testicles - further data on the chemical and catalytic properties of the enzyme (studies on the biosynthesis cyclitols, XXXIX)
Mol. Cell. Biochem.
28
23-26
1979
Rattus norvegicus
brenda
Gumber, S.C.; Loewus, M.W.; Loewus, F.A.
myo-Inositol-1-phosphate synthase from pine pollen: sulfhydryl involvement at the active site
Arch. Biochem. Biophys.
231
372-377
1984
Pinus ponderosa
brenda
Loewus, M.W.; Loewus, F.A.; Brillinger, G.U.; Otsuka, H.; Floss, H.G.
Stereochemistry, of the myo-inositol-1-phosphate synthase reaction
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255
11710-11712
1980
Bos taurus, Lilium longiflorum
brenda
Norman, R.A.; McAlister, M.S.; Murray-Rust, J.; Movahedzadeh, F.; Stoker, N.G.; McDonald, N.Q.
Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis
Structure
10
393-402
2002
Mycobacterium tuberculosis
brenda
Jin, X.; Geiger, J.H.
Structures of NAD(+)- and NADH-bound 1-l-myo-inositol 1-phosphate synthase
Acta Crystallogr. Sect. D
59
1154-1164
2003
Saccharomyces cerevisiae
brenda
Stein, A.J.; Geiger, J.H.
Structural studies of MIP synthase
Acta Crystallogr. Sect. D
D56
348-350
2000
Saccharomyces cerevisiae
-
brenda
Chen, L.; Zhou, C.; Yang, H.; Roberts, M.F.
Inositol-1-phosphate synthase from Archaeoglobus fulgidus is a class II aldolase
Biochemistry
39
12415-12423
2000
Archaeoglobus fulgidus
brenda
Jin, X.; Foley, K.M.; Geiger, J.H.
The structure of the 1L-myo-inositol 1-phosphate synthase/NAD+ /2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme's mechanism
J. Biol. Chem.
279
13889-13895
2004
Saccharomyces cerevisiae
brenda
Ju, S.; Shaltiel, G.; Shamir, A.; Agam, G.; Greenberg, M.L.
Human 1D-myo-inositol 3-phosphate synthase is functional in yeast
J. Biol. Chem.
279
21759-21765
2004
Homo sapiens
brenda
Majee, M.; Maitra, S.; Ghosh Dastidar, K.; Pattnaik, S.; Chatterjee, A.; Hait, N.C.; Das, K.P.; Majumder, A.L.
A novel salt-tolerant L-myo-inositol 1-phosphate synthase from Porteresia coarctata (Roxb.)Tateoka, a halophytic wild rice Molecular cloning, bacterial overexpression, characterization and functional introgression into tobacco conferring salt-tolerance phenotype
J. Biol. Chem.
279
28539-28552
2004
Oryza sativa (O64437), Oryza sativa, Oryza coarctata (Q7XZE6), Oryza coarctata
brenda
Kniewel, R.; Buglino, J.A.; Shen, V.; Chadha, T.; Beckwith, A.; Lima, C.D.
Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase
J. Struct. Funct. Genomics
2
129-134
2002
Saccharomyces cerevisiae
brenda
Seelan, R.S.; Parthasarathy, L.K.; Parthasarathy, R.N.
E2F1 regulation of the human myo-inositol 1-phosphate synthase (ISYNA1) gene promoter
Arch. Biochem. Biophys.
431
95-106
2004
Homo sapiens
brenda
Stieglitz, K.A.; Yang, H.; Roberts, M.F.; Stec, B.
Reaching for mechanistic consensus across life kingdoms: structure and insights into catalysis of the myo-inositol-1-phosphate synthase (mIPS) from Archaeoglobus fulgidus
Biochemistry
44
213-224
2005
Archaeoglobus fulgidus
brenda
Chettri, D.R.; Choudhuri, M.; Mukherjee, A.K.; Adhikari, J.
L-myo-inositol-1-phosphate synthase: partial purification and characterization from Gleichenia glauca
Biol. Plant.
49
59-63
2005
Gleichenia glauca
-
brenda
Ju, S.; Greenberg, M.L.
1D-myo-inositol 3-phosphate synthase: conservation, regulation, and putative target of mood stabilizers
Clin. Neurosci. Res.
4
181-187
2004
Saccharomyces cerevisiae, Homo sapiens, Mycobacterium tuberculosis
-
brenda
Shukla, S.; VanToai, T.T.; Pratt, R.C.
Expression and nucleotide sequence of an INS (3) P1 synthase gene associated with low-phytate kernels in maize (Zea mays L.)
J. Agric. Food Chem.
52
4565-4570
2004
Zea mays (Q9FPK7), Zea mays
brenda
Neelon, K.; Wang, Y.; Stec, B.; Roberts, M.F.
Probing the mechanism of the Archaeoglobus fulgidus inositol-1-phosphate synthase
J. Biol. Chem.
280
11475-11482
2005
Archaeoglobus fulgidus
brenda
Park, S.H.; Kim, J.I.
Characterization of recombinant Drosophila melanogaster myo-inositol-1-phosphate synthase expressed in Escherichia coli
J. Microbiol.
42
20-24
2004
Drosophila melanogaster
brenda
Chhetri, D.R.; Chiu, P.F.
Identification and characterization of L-myo-inositol-1-phosphate synthase from Taxus baccata L
J. Phytol. Res.
17
141-146
2004
Taxus baccata
-
brenda
Oren Benaroya, R.; Zamski, E.; Tel-Or, E.
L-myo-inositol 1-phosphate synthase in the aquatic fern Azolla filiculoides
Plant Physiol. Biochem.
42
97-102
2004
Azolla filiculoides
brenda
Chatterjee, A.; Majee, M.; Ghosh, S.; Majumder, A.L.
sll1722, an unassigned open reading frame of Synechocystis PCC 6803, codes for L-myo-inositol 1-phosphate synthase
Planta
218
989-998
2004
Synechocystis sp.
brenda
Chatterjee, A.; Dastidar, K.G.; Maitra, S.; Das-Chatterjee, A.; Dihazi, H.; Eschrich, K.; Majumder, A.L.
sll1981, an acetolactate synthase homologue of Synechocystis sp. PCC6803, functions as L-myo-inositol 1-phosphate synthase
Planta
224
367-379
2006
Synechocystis sp.
brenda
Abreu, E.F.; Aragao, F.J.
Isolation and characterization of a myo-inositol-1-phosphate synthase gene from yellow passion fruit (Passiflora edulis f. flavicarpa) expressed during seed development and environmental stress
Ann. Bot.
99
285-292
2007
Passiflora edulis f. flavicarpa (Q1HG62), Passiflora edulis f. flavicarpa
brenda
Das-Chatterjee, A.; Goswami, L.; Maitra, S.; Dastidar, K.G.; Ray, S.; Majumder, A.L.
Introgression of a novel salt-tolerant L-myo-inositol 1-phosphate synthase from Porteresia coarctata (Roxb.) Tateoka (PcINO1) confers salt tolerance to evolutionary diverse organisms
FEBS Lett.
580
3980-3988
2006
Oryza coarctata
brenda
Li, Y.; Chen, Z.; Li, X.; Zhang, H.; Huang, Q.; Zhang, Y.; Xu, S.
Inositol-1-phosphate synthetase mRNA as a new target for antisense inhibition of Mycobacterium tuberculosis
J. Biotechnol.
128
726-734
2007
Mycobacterium tuberculosis
brenda
Chiera, J.; Grabau, E.
Localization of myo-inositol phosphate synthase (GmMIPS-1) during the early stages of soybean seed development
J. Exp. Bot.
58
2261-2268
2007
Glycine max
brenda
Di Daniel, E.; Cheng, L.; Maycox, P.R.; Mudge, A.W.
The common inositol-reversible effect of mood stabilizers on neurons does not involve GSK3 inhibition, myo-inositol-1-phosphate synthase or the sodium-dependent myo-inositol transporters
Mol. Cell. Neurosci.
32
27-36
2006
Rattus norvegicus (Q6AYK3)
brenda
Galit, S.; Shirley, M.; Ora, K.; Belmaker, R.H.; Galila, A.
Effects of valproate derivatives on human brain myo-inositol-1-phosphate (MIP) synthase activity and amphetamine-induced rearing
Pharmacol. Rep.
59
402-407
2007
Homo sapiens
brenda
Ghosh Dastidar, K.; Maitra, S.; Goswami, L.; Roy, D.; Das, K.P.; Majumder, A.L.
An insight into the molecular basis of salt tolerance of L-myo-inositol 1-P synthase (PcINO1) from Porteresia coarctata (Roxb.) Tateoka, a halophytic wild rice
Plant Physiol.
140
1279-1296
2006
Oryza coarctata (Q7XZE6), Oryza coarctata, Oryza sativa (O64437)
brenda
Chhetri, D.R.; Adhikari, J.; Mukherjee, A.K.
NAD+ mediated differential thermotolerance between chloroplastic and cytosolic L-myo-inositol-1-phosphate synthase from Diplopterygium glaucum (Thunb.) Nakai
Prep. Biochem. Biotechnol.
36
307-319
2006
Diplopterygium glaucum
brenda
Baisakh, N.; Subudhi, P.K.; Varadwaj, P.
Primary responses to salt stress in a halophyte, smooth cordgrass (Spartina alterniflora Loisel.)
Funct. Integr. Genomics
8
287-300
2008
Sporobolus alterniflorus
brenda
Lehner, A.; Chopera, D.R.; Peters, S.W.; Keller, F.; Mundree, S.G.; Thomson, J.A.; Farrant, J.M.
Protection mechanisms in the resurrection plant Xerophyta viscosa: cloning, expression, characterisation and role of XvINO1, a gene coding for a myo-inositol 1-phosphate synthase [Erratum: 2008, v. 35, no. 2, p. 171.]
Funct. Plant Biol.
35
26-39
2008
Xerophyta viscosa (A4UMS1)
brenda
Mitsuhashi, N.; Kondo, M.; Nakaune, S.; Ohnishi, M.; Hayashi, M.; Hara-Nishimura, I.; Richardson, A.; Fukaki, H.; Nishimura, M.; Mimura, T.
Localization of myo-inositol-1-phosphate synthase to the endosperm in developing seeds of Arabidopsis
J. Exp. Bot.
59
3069-3076
2008
Arabidopsis thaliana
brenda
Kuwano, M.; Mimura, T.; Takaiwa, F.; Yoshida, K.T.
Generation of stable low phytic acid transgenic rice through antisense repression of the 1D-myo-inositol 3-phosphate synthase gene (RINO1) using the 18-kDa oleosin promoter
Plant Biotechnol. J.
7
96-105
2009
Oryza sativa
brenda
Kaur, H.; Shukla, R.K.; Yadav, G.; Chattopadhyay, D.; Majee, M.
Two divergent genes encoding L-myo-inositol 1-phosphate synthase1 (CaMIPS1) and 2 (CaMIPS2) are differentially expressed in chickpea
Plant Cell Environ.
31
1701-1716
2008
Cicer arietinum (B6SBM1), Cicer arietinum (B6SBM2), Cicer arietinum
brenda
Moon, T.S.; Yoon, S.H.; Lanza, A.M.; Roy-Mayhew, J.D.; Prather, K.L.
Production of glucaric acid from a synthetic pathway in recombinant Escherichia coli
Appl. Environ. Microbiol.
75
589-595
2009
Saccharomyces cerevisiae
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (P42801), Arabidopsis thaliana (Q38862), Arabidopsis thaliana (Q9LX12)
brenda
Abid, G.; Silue, S.; Muhovski, Y.; Jacquemin, J.M.; Toussaint, A.; Baudoin, J.P.
Role of myo-inositol phosphate synthase and sucrose synthase genes in plant seed development
Gene
439
1-10
2009
Arabidopsis thaliana, Archaeoglobus fulgidus, Brassica napus, Citrus x paradisi, Euglena gracilis, Glycine max, Hordeum vulgare, Mesembryanthemum crystallinum, Nicotiana tabacum, Oryza sativa, Perilla frutescens, Vigna radiata, Phaseolus vulgaris, Pisum sativum, Sesamum indicum, Solanum tuberosum, Zea mays
brenda
Morii, H.; Kiyonari, S.; Ishino, Y.; Koga, Y.
A novel biosynthetic pathway of archaetidyl-myo-inositol via archaetidyl-myo-inositol phosphate from CDP-archaeol and D-glucose 6-phosphate in methanoarchaeon Methanothermobacter thermautotrophicus cells
J. Biol. Chem.
284
30766-30774
2009
Methanothermobacter thermautotrophicus
brenda
Seelan, R.S.; Lakshmanan, J.; Casanova, M.F.; Parthasarathy, R.N.
Identification of myo-inositol-3-phosphate synthase isoforms: characterization, expression, and putative role of a 16-kDa gammac isoform
J. Biol. Chem.
284
9443-9457
2009
Rattus norvegicus (Q6AYK3)
brenda
Reynolds, T.B.
Strategies for acquiring the phospholipid metabolite inositol in pathogenic bacteria, fungi and protozoa: making it and taking it
Microbiology
155
1386-1396
2009
Saccharomyces cerevisiae, Candida albicans, Cryptococcus neoformans, Leishmania mexicana, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Trypanosoma brucei
brenda
Bethea, E.K.; Carver, B.J.; Montedonico, A.E.; Reynolds, T.B.
The inositol regulon controls viability in Candida glabrata
Microbiology
156
452-462
2010
[Candida] glabrata
brenda
Donahue, J.L.; Alford, S.R.; Torabinejad, J.; Kerwin, R.E.; Nourbakhsh, A.; Ray, W.K.; Hernick, M.; Huang, X.; Lyons, B.M.; Hein, P.P.; Gillaspy, G.E.
The Arabidopsis thaliana myo-inositol 1-phosphate synthase1 gene is required for myo-inositol synthesis and suppression of cell death
Plant Cell
22
888-903
2010
Arabidopsis thaliana
brenda
Wongkaew, A.; Nakasathien, S.; Srinives, P.
Isolation and characterization of D-myo-inositol-3-phosphate synthase from mungbean (Vigna radiata)
Plant Mol. Biol. Rep.
28
122-127
2009
Vigna radiata (A8WEL5)
-
brenda
Ray, S.; Patra, B.; Das-Chatterjee, A.; Ganguli, A.; Majumder, A.L.
Identification and organization of chloroplastic and cytosolic L-myo-inositol 1-phosphate synthase coding gene(s) in Oryza sativa: comparison with the wild halophytic rice, Porteresia coarctata
Planta
231
1211-1227
2010
Oryza coarctata (B6V6K8), Oryza coarctata (B6V6K9), Oryza coarctata, Oryza sativa (O64437), Oryza sativa
brenda
Huang, X.; Hernick, M.
A limitation of the continuous spectrophotometric assay for the measurement of myo-inositol-1-phosphate synthase activity
Anal. Biochem.
417
228-232
2011
Arabidopsis thaliana
brenda
Chen, H.; Xiong, L.
myo-Inositol-1-phosphate synthase is required for polar auxin transport and organ development
J. Biol. Chem.
285
24238-24247
2010
Arabidopsis thaliana (C4PW05), Arabidopsis thaliana Columbia-0 (C4PW05)
brenda
Luo, Y.; Qin, G.; Zhang, J.; Liang, Y.; Song, Y.; Zhao, M.; Tsuge, T.; Aoyama, T.; Liu, J.; Gu, H.; Qu, L.J.
D-myo-Inositol-3-phosphate affects phosphatidylinositol-mediated endomembrane function in Arabidopsis and is essential for auxin-regulated embryogenesis
Plant Cell
23
1352-1372
2011
Arabidopsis thaliana (F4IIN3), Arabidopsis thaliana (P42801), Arabidopsis thaliana (Q9LX12), Arabidopsis thaliana
brenda
Wei, W.; Dai, X.; Wang, Y.; Chuan, Y.; Gou, C.; Chen, F.
Cloning and expression analysis of 1 l-myo-inositol-1-phosphate synthase gene from Ricinus communis L.
Z. Naturforsch. C
65
501-507
2010
Ricinus communis (C7B9C0), Ricinus communis
brenda
Chhetri, D.R.; Gupta, S.; Mukherjee, A.K.; Adhikari, J.
L-myo-inositol-1-phosphate synthase expressed in developing organ: isolation and characterisation of the enzyme from human fetal liver
Appl. Biochem. Biotechnol.
167
2269-2282
2012
Homo sapiens (Q9NPH2), Homo sapiens
brenda
Khurana, N.; Chauhan, H.; Khurana, P.
Expression analysis of a heat-inducible, myo-inositol-1-phosphate synthase (MIPS) gene from wheat and the alternatively spliced variants of rice and Arabidopsis
Plant Cell Rep.
31
237-251
2012
Arabidopsis thaliana, Arabidopsis thaliana (Q38862), Arabidopsis thaliana (Q9LX12), Oryza sativa, Oryza sativa (O64437), Triticum aestivum (G8HMZ0), Triticum aestivum (Q9S7U0), Triticum aestivum
brenda
Joshi, R.; Ramanarao, M.V.; Baisakh, N.
Arabidopsis plants constitutively overexpressing a myo-inositol 1-phosphate synthase gene (SaINO1) from the halophyte smooth cordgrass exhibits enhanced level of tolerance to salt stress
Plant Physiol. Biochem.
65
61-66
2013
Arabidopsis thaliana
brenda
Cui, M.; Liang, D.; Wu, S.; Ma, F.; Lei, Y.
Isolation and developmental expression analysis of L-myo-inositol-1-phosphate synthase in four Actinidia species
Plant Physiol. Biochem.
73
351-358
2013
Actinidia rufa, Actinidia deliciosa (K4MTP0), Actinidia deliciosa, Actinidia eriantha (V5TCU6), Actinidia eriantha, Actinidia arguta (V5TDM6), Actinidia arguta
brenda
Kaur, H.; Verma, P.; Petla, B.P.; Rao, V.; Saxena, S.C.; Majee, M.
Ectopic expression of the ABA-inducible dehydration-responsive chickpea L-myo-inositol 1-phosphate synthase 2 (CaMIPS2) in Arabidopsis enhances tolerance to salinity and dehydration stress
Planta
237
321-335
2013
Cicer arietinum (B6SBM1), Cicer arietinum (B6SBM2), Cicer arietinum
brenda
Ali, N.; Paul, S.; Gayen, D.; Sarkar, S.N.; Datta, S.K.; Datta, K.
RNAi mediated down regulation of myo-inositol-3-phosphate synthase to generate low phytate rice
Rice (N.Y.)
6
12
2013
Oryza sativa
brenda
Kalujnaia, S.; Hazon, N.; Cramb, G.
Myo-inositol phosphate synthase expression in the European eel (Anguilla anguilla) and Nile tilapia (Oreochromis niloticus) effect of seawater acclimation
Am. J. Physiol. Regul. Integr. Comp. Physiol.
311
R287-R298
2016
Anguilla anguilla (A0A143Y3U8), Anguilla anguilla, Oreochromis niloticus (I3IXX3), Oreochromis niloticus
brenda
Morii, H.; Ogawa, M.; Fukuda, K.; Taniguchi, H.
Ubiquitous distribution of phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase in Bacteria and Archaea, which contain inositol phospholipid
Biochem. Biophys. Res. Commun.
443
86-90
2014
Aeropyrum pernix
brenda
Hazra, A.; Nandy Datta, P.
Myo-inositol 1-phosphate synthase - The chosen path of evolution
Biotechnologia
97
95-108
2016
Aspergillus nidulans, Avicennia marina, Bacillus cereus, Chlamydomonas reinhardtii, Chondrus crispus, Fusarium oxysporum, Glycine max, Physcomitrium patens, Oryza coarctata, Setaria italica, Ostreococcus tauri, Selaginella moellendorffii, Metarhizium robertsii, Colletotrichum higginsianum, Sphaerulina musiva, Oscillatoria acuminata
-
brenda
Lu, Y.; Wang, L.; Teng, F.; Zhang, J.; Hu, M.; Tao, Y.
Production of myo-inositol from glucose by a novel trienzymatic cascade of polyphosphate glucokinase, inositol 1-phosphate synthase and inositol monophosphatase
Enzyme Microb. Technol.
112
1-5
2018
Trypanosoma brucei, Trypanosoma brucei (Q38AQ2), Trypanosoma brucei TREU927, Trypanosoma brucei TREU927 (Q38AQ2)
brenda
Azam, S.S.; Sarfaraz, S.; Abro, A.
Comparative modeling and virtual screening for the identification of novel inhibitors for myo-inositol-1-phosphate synthase
Mol. Biol. Rep.
41
5039-5052
2014
Homo sapiens (Q9NPH2), Homo sapiens
brenda
Frej, A.D.; Clark, J.; Le Roy, C.I.; Lilla, S.; Thomason, P.A.; Otto, G.P.; Churchill, G.; Insall, R.H.; Claus, S.P.; Hawkins, P.; Stephens, L.; Williams, R.S.
The inositol-3-phosphate synthase biosynthetic enzyme has distinct catalytic and metabolic roles
Mol. Cell. Biol.
36
1464-1479
2016
Dictyostelium discoideum (Q54N49), Dictyostelium discoideum
brenda
Kusuda, H.; Koga, W.; Kusano, M.; Oikawa, A.; Saito, K.; Hirai, M.Y.; Yoshida, K.T.
Ectopic expression of myo-inositol 3-phosphate synthase induces a wide range of metabolic changes and confers salt tolerance in rice
Plant Sci.
232
49-56
2015
Oryza sativa
brenda
Basak, P.; Maitra-Majee, S.; Das, J.K.; Mukherjee, A.; Ghosh Dastidar, S.; Pal Choudhury, P.; Lahiri Majumder, A.
An evolutionary analysis identifies a conserved pentapeptide stretch containing the two essential lysine residues for rice L-myo-inositol 1-phosphate synthase catalytic activity
PLoS ONE
12
e0185351
2017
Oryza sativa (Q8S5N2), Oryza sativa
brenda
Huang, X.; Hernick, M.
Recombinant expression of a functional myo-inositol-1-phosphate synthase (MIPS) in Mycobacterium smegmatis
Protein J.
34
380-390
2015
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
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