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Information on EC 5.5.1.4 - inositol-3-phosphate synthase and Organism(s) Rattus norvegicus and UniProt Accession Q6AYK3
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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: Rattus norvegicus
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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D-Glucose 6-phosphate cycloaldolase
-
-
-
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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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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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Inositol 1-phosphate synthetase
-
-
-
-
INPS1
-
-
-
-
IPS
-
-
-
-
L-myo-Inositol 1-phosphate synthetase
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-
-
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L-myo-Inositol-1-phosphate synthase
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-
-
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MI-1-P synthase
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-
-
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MIP synthase
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-
-
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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
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-
-
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Synthase, myo-inositol 1-phosphate
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
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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
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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
D-Glucose 6-phosphate
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
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-
?
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
-
-
?
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
?
-
the enzyme catalyzes the first committed step in the production of all inositol containing compounds, including phospholipids
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Na+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaBH4
-
partial inactivation in presence of NAD+. No inactivation in absence of NAD+
p-Substituted mercuribenzoate
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1 mM, 93% inhibition in presence of 1 mM NADH
Li+
-
14 mM, 50% inhibition in absence of NH4+. Only 10% inhibition in presence of 14 mM NH4+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
7.7
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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_RAT
557
0
60884
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
210000
-
testis, gel filtration, PAGE, ultracentrifugal equilibrium sedimentation
68000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
trimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate saturation, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform gammac is expressed in Escherichia coli Rosetta (DE3) pLysS cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
Eisenberg jr., F.; Parthasarathy, R.
Measurement of biosynthesis of myo-inositol from glucose 6-phosphate
Methods Enzymol.
141
127-143
1987
Rattus norvegicus
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
Byun, S.M.; Jenness, R.
Stereospecificity of L-myo-inositol-1-phosphate synthase for nicotinamide adenine dinucleotide
Biochemistry
20
5174-5177
1981
Rattus norvegicus
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
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)
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