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Information on EC 5.5.1.4 - inositol-3-phosphate synthase and Organism(s) Homo sapiens
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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
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nucleation
-
neuroblast
-
phytic
-
ice-nucleating
-
monophosphatase
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cloud
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halophytic
-
inositol-containing
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cyclitols
- phytate
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supercooled
- galactinol
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hexakisphosphate
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radiative
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2-kinase
- impase
- medicine
- pharmacology
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1L-myo-Inositol-1-phosphate synthase
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-
-
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D-Glucose 6-phosphate cycloaldolase
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-
-
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D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cyclase
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-
-
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D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cycloaldolase
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-
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D-Glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase
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-
-
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D-Glucose-6-phosphate,L-myo-inositol-1-phosphate cycloaldolase
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-
-
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Glucocycloaldolase
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-
-
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Glucose 6-phosphate cyclase
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-
-
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Glucose-6-phosphate inositol monophosphate cycloaldolase
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-
-
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Inositol 1-phosphate synthase
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-
-
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Inositol 1-phosphate synthetase
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-
-
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INPS1
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-
-
-
IPS
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-
-
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L-myo-Inositol 1-phosphate synthetase
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-
-
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L-myo-Inositol-1-phosphate synthase
MI-1-P synthase
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MIP synthase
MIPS
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-
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myo-Inositol-1-P synthase
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-
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Myo-inositol-1-phosphate synthase
Synthase, myo-inositol 1-phosphate
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-
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L-myo-Inositol-1-phosphate synthase
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-
-
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MIP synthase
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-
-
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Myo-inositol-1-phosphate synthase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
catalytic reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
9032-95-5
-
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
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
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-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
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rate-limiting step for de novo inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
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the enzyme is involved in phospholipid biosynthesis and is the key enzyme in regulation of the pathway catalyzing the rate limiting step, overview
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-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
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reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+
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-
?
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
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-
?
D-Glucose 6-phosphate
?
-
first step in de novo biosynthesis of myo-inositol
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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
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
?
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
?
-
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
K+
Na+
NH4+
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
5-methyl-4-phenyl-2-(1H-pyrrol-1-yl)thiophene-3-carboxylic acid
ZINC03844214
valnoctamide
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valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate, competitive
valrocemide
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valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate
Valproate
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noncompetitive, specific, only in vivo, e.g. in brain post mortem, no inhibition of the purified rcombinant enzyme in vitro
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). INO1_HUMAN
558
0
61068
Swiss-Prot
other Location (Reliability: 1)
J3QS51_HUMAN
233
0
25351
TrEMBL
other Location (Reliability: 2)
B3KSG0_HUMAN
408
0
44772
TrEMBL
other Location (Reliability: 2)
B7Z3K3_HUMAN
356
0
38822
TrEMBL
other Location (Reliability: 4)
A0A140VK73_HUMAN
558
0
61068
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the human enzyme can functionally complement the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, BioGel A purified fractions (final purification fraction), 5-7 days
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is purified 51fold using ammonium sulfate fractionation followed by successive chromatography through DEAE cellulose and BioGel A columns
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
anticonvulsants valnoctamide and valrocemide drastically reduce enzyme activity in crude brain homogenate
pharmacology
-
the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Adhikari, J.; Majumder, A.L.
L-Myo-inositol-1-phosphate synthase from mammalian brain: partial purification and characterisation of the fetal and adult enzyme
Indian J. Biochem. Biophys.
25
408-412
1988
Homo sapiens, Rattus norvegicus
Majumder, A.L.; Johnson, M.D.; Henry, S.A.
1L-myo-Inositol-1-phosphate synthase
Biochim. Biophys. Acta
1348
245-256
1997
Acer pseudoplatanus, Arabidopsis thaliana, Bos taurus, Brassica napus, Saccharomyces cerevisiae, Candida albicans, Streptomyces sp., Citrus x paradisi, Entamoeba histolytica, Euglena gracilis, Hevea brasiliensis, Homo sapiens, Lemna gibba, Lilium longiflorum, Mesembryanthemum crystallinum, Neurospora crassa, Vigna radiata, Phaseolus vulgaris, Pinus ponderosa, Rattus norvegicus, Spirodela polyrhiza, Arthrospira platensis
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
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
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
-
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
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
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