Information on EC 5.5.1.4 - inositol-3-phosphate synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
5.5.1.4
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RECOMMENDED NAME
GeneOntology No.
inositol-3-phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
D-glucose 6-phosphate = L-myo-inositol 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
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elimination/addition
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intramolecular
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1D-myo-inositol hexakisphosphate biosynthesis III (Spirodela polyrrhiza)
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1D-myo-inositol hexakisphosphate biosynthesis IV (Dictyostelium)
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di-myo-inositol phosphate biosynthesis
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mycothiol biosynthesis
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myo-inositol biosynthesis
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phosphatidylinositol biosynthesis I (bacteria)
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myo-inositol biosynthesis
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Streptomycin biosynthesis
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Inositol phosphate metabolism
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Metabolic pathways
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Biosynthesis of antibiotics
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-95-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
gene MIPS1
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Gleichenia glauca
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
isoform MIPS1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose 6-phosphate
5-deoxy-L-myo-inositol 1-phosphate
show the reaction diagram
D-2-Deoxy-2-fluoroglucose 6-phosphate
5-Deoxy-5-fluoro-myo-inositol 1-phosphate
show the reaction diagram
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
D-glucose 6-phosphate
1L-myo-inositol 1-phosphate
show the reaction diagram
D-glucose 6-phosphate
1L-myo-inositol-1-phosphate
show the reaction diagram
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-
-
-
?
D-Glucose 6-phosphate
?
show the reaction diagram
D-glucose 6-phosphate
D-myo-inositol 3-phosphate
show the reaction diagram
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
D-Mannose 6-phosphate
myo-Inositol 1-phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
D-glucose 6-phosphate
1L-myo-inositol 1-phosphate
show the reaction diagram
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first and rate-limiting step in biosynthesis of all inositol-conatining compounds
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?
D-glucose 6-phosphate
1L-myo-inositol-1-phosphate
show the reaction diagram
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?
D-Glucose 6-phosphate
?
show the reaction diagram
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
almost equally active as NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
Cu2+
inhibition
Hg2+
inhibition
NaCl
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
phosphate
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modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
1,5-Anhydro-D-glucitol 6-phosphate
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1-Deoxy-1-(phosphonomethyl)myo-2-inosose
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competitive
2-Deoxy-2-fluoroglucose 6-phosphate
2-deoxy-D-glucitol
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2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate
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binding structure, interaction with active site residues, overview
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2-Deoxy-D-glucitol 6-phosphate
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2-deoxy-D-glucose 6-phosphate
2-deoxy-glucitol-6-phosphate
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the inhibitor induces folding of the catalytic domain
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2-Deoxy-myo-inositol 1-phosphate
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competitive
choline
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slight inhibition
D-Allose 6-phosphate
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D-fructose 6-phosphate
D-galactose 6-phosphate
D-gluconate 6-phosphate
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D-glucose 6-phosphate
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the beta-anomer is preferred as substrate, the alpha-anomer is an inhibitor
D-mannitol 6-phosphate
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D-mannose 6-phosphate
D-sorbitol 6-phosphate
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dihydroxyacetone phosphate
-
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diphosphate
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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+
Endogeneous inhibitor from latex serum
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FeCl2
glucitol 6-phosphate
Inositol
lithium
mannitol
Mg2+
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inhibitory only at nonphysiological concentrations
myo-2-Inosose 1-phosphate
NaBH4
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partial inactivation in presence of NAD+. No inactivation in absence of NAD+
NH4HCO3
p-Substituted mercuribenzoate
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1 mM, 93% inhibition in presence of 1 mM NADH
PbCl2
pyridoxal 5'-phosphate
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sorbitol
Trinitrobenzene sulphonate
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valnoctamide
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valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate, competitive
Valproate
valrocemide
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valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
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stimulates
NaCl
leaf L-myo-inositol 1-phosphate concentration increases 40fold during the first 6 h of salt stress (exposure to 300 mM NaCl)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.15
2-deoxy-D-glucose 6-phosphate
pH 7, 37C, Vmax: 280 nM
0.12 - 4.47
D-glucose 6-phosphate
0.035 - 2.85
glucose 6-phosphate
0.0051 - 1.95
NAD+
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0817 - 9.6
D-glucose 6-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.233
D-glucose 6-phosphate
105
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00067
2-deoxy-D-glucitol
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pH 5.5
0.18
valnoctamide
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pH 7.6, 37C
0.21
Valproate
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brain, post mortem
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0003
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crude enzyme, in 50mM Bicine buffer (pH 8.5), at 60C
0.013
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purified recombinant refolded enzyme, with cofactor NADP+
0.015
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purified recombinant refolded enzyme, with cofactor NAD+
0.018
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purified native enzyme, with cofactor NADP+
0.02
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purified native enzyme, with cofactor NAD+
0.05
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value about, culture condition: 2 days, 30C
0.06
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value about, culture condition: 3 days, 30C
0.1
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value about, culture condition: 1 day, 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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8 - 8.5
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mutant bearing amino acids 174-210 of Porteresia coarctata enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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34% of maximal activity at pH 9.0, low activity below pH 5.0, inactive above pH 11.0
6.5 - 9.5
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pH 6.5: about 50% of maximal activity, pH 8.5: about 95% of maximal activity
7 - 7.5
optimal activity