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
5.5.1.4
-
RECOMMENDED NAME
GeneOntology No.
inositol-3-phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
-
-
-
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
no upregulation of transcription by salinity stress
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
RNA amounts are upregulated at least 5fold during salinity stress
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
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
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
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; 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
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
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
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
it is possible that the enzyme has an aldol step in the enzymatic pathway which is of neither classical aldolase type
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
ordered sequential mechanism with NAD+ adding first
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
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
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
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
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
catalytic reaction mechanism involving K369, K412, K373, and K489
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
catalytic reaction mechanism
-
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
show the reaction diagram
catalytic reaction mechanism, induced-fit active site formation by substrate binding
-
D-glucose 6-phosphate = L-myo-inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-glucose 6-phosphate = L-myo-inositol 1-phosphate
show the reaction diagram
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
-
D-glucose 6-phosphate = L-myo-inositol 1-phosphate
show the reaction diagram
substrate binding and metal-dependent reaction mechanism, overview, active site residues are D225, K274, K278, K306, D332, and K367
-
D-glucose 6-phosphate = L-myo-inositol 1-phosphate
show the reaction diagram
reaction mechanism involves 3 reaction steps: 1. oxidation by NAD+, 2. condensation to a cyclic molecule, 3. reduction by NADH
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cyclization
-
-
-
-
elimination/addition
-
-
intramolecular
-
PATHWAY
KEGG Link
MetaCyc Link
1D-myo-inositol hexakisphosphate biosynthesis III (Spirodela polyrrhiza)
-
1D-myo-inositol hexakisphosphate biosynthesis IV (Dictyostelium)
-
Biosynthesis of secondary metabolites
-
di-myo-inositol phosphate biosynthesis
-
Inositol phosphate metabolism
-
L-1-phosphatidyl-inositol biosynthesis (Mycobacteria)
-
Metabolic pathways
-
mycothiol biosynthesis
-
myo-inositol biosynthesis
-
Streptomycin biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1D-myo-inositol 3-phosphate synthase
-
-
1D-myo-inositol 3-phosphate synthase
-
-
1D-myo-inositol 3-phosphate synthase
-
-
1L-myo-Inositol-1-phosphate synthase
-
-
-
-
1L-myo-Inositol-1-phosphate synthase
-
-
D-Glucose 6-phosphate cycloaldolase
-
-
-
-
D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cyclase
-
-
-
-
D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cycloaldolase
-
-
-
-
D-Glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase
-
-
-
-
D-Glucose-6-phosphate,L-myo-inositol-1-phosphate cycloaldolase
-
-
-
-
D-myo-inositol-3-phosphate synthase
F4IIN3, P42801, Q9LX12
-
D-myo-inositol-3-phosphate synthase
A8WEL5
-
Glucocycloaldolase
-
-
-
-
Glucose 6-phosphate cyclase
-
-
-
-
Glucose-6-phosphate inositol monophosphate cycloaldolase
-
-
-
-
INO-1
B6V6K8
-
INO-1
O64437
-
INO-2
B6V6K9
-
INO1
A4UMS1
isozyme
Inositol 1-phosphate synthase
-
-
-
-
Inositol 1-phosphate synthase
-
-
Inositol 1-phosphate synthetase
-
-
-
-
inositol phosphate synthase
P42801, Q38862, Q9LX12
-
inositol-1-phosphate synthase
-
-
inositol-3-phosphate synthase
-
-
INPS1
-
-
-
-
INS (3) P1 synthase
-
-
IP synthase
-
-
IP synthase
-
-
IPS
-
-
-
-
L-myo-inositol 1-phosphate synthase
-
-
L-myo-inositol 1-phosphate synthase
-
-
L-myo-inositol 1-phosphate synthase
B6SBM1, B6SBM2
-
L-myo-inositol 1-phosphate synthase
B6V6K8, B6V6K9
-
L-myo-inositol 1-phosphate synthase
O64437
-
L-myo-inositol 1-phosphate synthase
-
-
L-myo-Inositol 1-phosphate synthetase
-
-
-
-
L-myo-Inositol-1-phosphate synthase
-
-
-
-
L-myo-Inositol-1-phosphate synthase
Gleichenia glauca
-
-
L-myo-Inositol-1-phosphate synthase
C7B9C0
-
L-myo-Inositol-1-phosphate synthase
-
-
MI-1-P synthase
-
-
-
-
MIP synthase
-
-
-
-
MIP synthase
-
-
MIPS
-
-
-
-
MIPS
F4IIN3, P42801, Q9LX12
-
MIPS
B6V6K8, B6V6K9
-
MIPS
-
-
MIPS
O64437
-
MIPS
C7B9C0
-
MIPS
A4UMS1
-
MIPS1
B6SBM1
isoyzme
MIPS1
A8WEL5
-
MIPS2
B6SBM2
isozyme
myo-inositol 1-phosphate synthase
-
-
myo-inositol 1-phosphate synthase
-
-
myo-inositol phosphate synthase
-
-
myo-Inositol-1-P synthase
-
-
-
-
Myo-inositol-1-phosphate synthase
-
-
-
-
Myo-inositol-1-phosphate synthase
-
-
Myo-inositol-1-phosphate synthase
C4PW05
-
Myo-inositol-1-phosphate synthase
Arabidopsis thaliana Columbia-0
C4PW05
-
-
Myo-inositol-1-phosphate synthase
-
-
Myo-inositol-1-phosphate synthase
-
-
Myo-inositol-1-phosphate synthase
-
-
Myo-inositol-1-phosphate synthase
A4UMS1
-
myo-inositol-3-phosphate synthase
-
-
PcINO1
-
-
PINO1 protein
Q7XZE6
-
RINO1 protein
-
-
RINO1 protein
O64437
-
sll1981
Synechocystis sp. PCC6803
-
-
-
Synthase, myo-inositol 1-phosphate
-
-
-
-
yMIP synthase
-
-
[Ins(3)P1] synthase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9032-95-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
gene MIPS1
UniProt
Manually annotated by BRENDA team
gene mips1; three MIPS genes mips1, mips2, and mips3
UniProt
Manually annotated by BRENDA team
gene mips2; three MIPS genes mips1, mips2, and mips3
UniProt
Manually annotated by BRENDA team
gene mips3; three MIPS genes mips1, mips2, and mips3
UniProt
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
gene MIPS1
UniProt
Manually annotated by BRENDA team
aquatic fern
-
-
Manually annotated by BRENDA team
isozyme MIPS1; cultivar BGD72
UniProt
Manually annotated by BRENDA team
isozyme MIPS2; cultivar BGD72
UniProt
Manually annotated by BRENDA team
chloroplast and cytosolic isoforms
-
-
Manually annotated by BRENDA team
Gleichenia glauca
-
-
-
Manually annotated by BRENDA team
gene ISYNA1
-
-
Manually annotated by BRENDA team
isoform INO1-1
UniProt
Manually annotated by BRENDA team
isoform INO1-2
UniProt
Manually annotated by BRENDA team
Roxb. Tateoka
SwissProt
Manually annotated by BRENDA team
salt-resistant enzyme, direct correlation between increased sythesis of inositol under salinity stress by the enzyme and salt tolerance
-
-
Manually annotated by BRENDA team
expression is upregulated under cold and heat stress
SwissProt
Manually annotated by BRENDA team
two enzyme forms: MW 33000 and MW 56000. Its expression is temporally and spatially regulated
-
-
Manually annotated by BRENDA team
Rattus norvegicus
-
-
Manually annotated by BRENDA team
Streptomyces griseus; streptomycin producing and streptomycin non-producing strains
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
strain PCC6803, bifunctional inositol-3-phosphate synthase/acetolactate synthase
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
strain PCC6803, bifunctional inositol-3-phosphate synthase/acetolactate synthase
-
-
Manually annotated by BRENDA team
variant KPS1
UniProt
Manually annotated by BRENDA team
isoform MIPS1
UniProt
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the inositol 3-phosphate synthase-deficient mutant is virulent in mice as the wild type
malfunction
-
the inositol 3-phosphate synthase-deficient mutant is not virulent in mice and loses viability in macrophages
malfunction
-
loss in MIPS1 results in smaller plants with curly leaves and spontaneous production of lesions
malfunction
C4PW05
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
F4IIN3, P42801, Q9LX12
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; 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; 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
Arabidopsis thaliana Columbia-0
-
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
-
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
C4PW05
myo-inositol-1-phosphate synthase is a conserved enzyme that catalyzes the first committed and rate-limiting step in inositol biosynthesis
metabolism
F4IIN3, P42801, Q9LX12
MIPS catalyzes the rate-limiting step in de novo synthesis of myo-inositol; MIPS catalyzes the rate-limiting step in de novo synthesis of myo-inositol; MIPS catalyzes the rate-limiting step in de novo synthesis of myo-inositol
metabolism
Arabidopsis thaliana Columbia-0
-
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
C4PW05
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
C7B9C0, -
MIPS plays an important role in the defensive mechanisms of Ricinus communis against drought stress
physiological function
Arabidopsis thaliana Columbia-0
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
2-deoxy-D-glucose 6-phosphate
5-deoxy-L-myo-inositol 1-phosphate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
D-2-Deoxy-2-fluoroglucose 6-phosphate
5-Deoxy-5-fluoro-myo-inositol 1-phosphate
show the reaction diagram
-
at 0.2% of the activity relative to D-glucose 6-phosphate
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
Gleichenia glauca
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
B6SBM1, B6SBM2, -
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
A4UMS1
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
B6V6K8, B6V6K9
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
ir
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
no reversibility of the overall reaction is found
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
absolute specificity for
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
at least 5-fold preference for the beta-anomer
-
-
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
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
show the reaction diagram
-
first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
important in myo-inositol level regulation
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
key enzyme in phytate biosynthesis, a phosphate-rich storage molecule
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
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
show the reaction diagram
-
reaction mechanism involves 3 reaction steps: 1. oxidation by NAD+, 2. condensation to a cyclic molecule, 3. reduction by NADH
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
Q9FPK7, -
-
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
Q7XZE6
-
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-, Q7XZE6
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
O64437
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
class II aldolase
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
rate-limiting step for de novo inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
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
show the reaction diagram
-
reaction includes 3 partial reactions with enzyme-bound intermediates, dependent on NAD+
-
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
-
key enzyme in inositol biosynthesis, rate-limiting step
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
-
key enzyme in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
-
the enzyme catalyzes critical steps in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
-
the enzyme catalyzes the first and rate-limiting step in biosynthesis of inositol-containg compounds
-
?
D-Glucose 6-phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
first step in de novo biosynthesis of myo-inositol
-
-
-
D-Glucose 6-phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
key enzyme in myo-inositol biosynthetic pathway
-
-
-
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
-
first and rate-limiting step in biosynthesis of all inositol-conatining compounds, determination of the catalytic reaction mechanism
-
-
?
D-glucose 6-phosphate
D-myo-inositol 3-phosphate
show the reaction diagram
A8WEL5
-
-
-
?
D-glucose 6-phosphate
D-myo-inositol 3-phosphate
show the reaction diagram
-
assay at pH 7.5, 37C
-
-
?
D-glucose 6-phosphate
1L-myo-inositol-1-phosphate
show the reaction diagram
-
-
-
-
?
D-Mannose 6-phosphate
myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
-
D-Mannose 6-phosphate
myo-Inositol 1-phosphate
show the reaction diagram
-
at 11.5% of the activity relative to D-glucose 6-phosphate
-
-
-
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
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
-
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
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
show the reaction diagram
-
first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
important in myo-inositol level regulation
-
-
?
D-Glucose 6-phosphate
L-myo-Inositol 1-phosphate
show the reaction diagram
-
key enzyme in phytate biosynthesis, a phosphate-rich storage molecule
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
Q9FPK7, -
-
-
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
rate-limiting step for de novo inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
show the reaction diagram
-
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-inositol 3-phosphate
show the reaction diagram
-
key enzyme in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
-
the enzyme catalyzes critical steps in inositol biosynthesis
-
?
D-glucose 6-phosphate
1D-inositol 3-phosphate
show the reaction diagram
-
the enzyme catalyzes the first and rate-limiting step in biosynthesis of inositol-containg compounds
-
?
D-Glucose 6-phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
first step in de novo biosynthesis of myo-inositol
-
-
-
D-Glucose 6-phosphate
?
show the reaction diagram
-
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
?
show the reaction diagram
-
key enzyme in myo-inositol biosynthetic pathway
-
-
-
D-glucose 6-phosphate
1L-myo-inositol 1-phosphate
show the reaction diagram
-
first and rate-limiting step in biosynthesis of all inositol-conatining compounds
-
-
?
D-glucose 6-phosphate
1L-myo-inositol-1-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
inositol phosphates are involved in several signal transduction pathways
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
Km: 0.05 mM; 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+
-
absolute requirement for NAD+; different proportions of an NAD+-independent activity can be obtained depending on the conditions of extraction and dialysis
NAD+
-
Km: 0.05 mM; tightly bound
NAD+
-
absolute requirement for NAD+
NAD+
-
bound to the enzyme
NAD+
-
required
NAD+
-
cofactor, Km: 0.008 mM
NAD+
-
cofactor, Km: 0.011 mM
NAD+
-
required, Km: 0.0024
NAD+
-
tightly bound
NAD+
-
complete activity without addition of NAD+
NAD+
-
the enzyme is specific for the pro-S-hydrogen at C-4 of NAD+
NAD+
-
the enzyme contains close to 2 mol NAD+ per mol of enzyme
NAD+
-
required
NAD+
Q7XZE6
Km: 0.153 mM for the native enzyme, Km: 0.166 mM, recombinant enzyme
NAD+
-
Km: 0.14 mM for the native enzyme, Km: 0.188 mM, recombinant enzyme
NAD+
-
binding domain structure, interacts with S149 and Asp261
NAD+
Gleichenia glauca
-
dependent on, only basal activity in absence of exogenous NAD+
NAD+
-
dependent on
NAD+
-
slightly preferred cofactor compared to NADP+
NAD+
-
Km value 0.285 mM
NAD+
Q7XZE6
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
NAD+
B6SBM1, B6SBM2, -
;
NAD+
B6V6K8, B6V6K9
;
NADH
-
dependent on
NADP+
-
almost equally active as NAD+
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
10 mM, 2fold stimulation
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+
-
14 mM, slight stimulation
K+
-
50 mM, 2fold stimulation
K+
-
stimulates 2fold and with added K+, 2.5fold
K+
-
slight stimulation
K+
-
optimal stimulation at 50 mM
K+
-
stimulates 2fold and with added K+, 2.5fold
K+
-
5 mM KCl stimulates 25-35%
K+
-
stimulation of chloroplastic and cytosolic enzyme up to 2.5 mM
K+
-
10 mM, 5fold stimulation
Mg2+
-
required
Mg2+
-
slight activation
Mg2+
-
KM: 0.0242 mM, activates
Mg2+
-
1-10 mM, 2-3fold stimulation
Mg2+
-
activates
Mg2+
-
activates
Mn2+
-
activation
Mn2+
-
Km: 0.00077 mM, absolute requirement for a divalent metal ion, Zn2+ or Mn2+ are the best activators, followed by Co2+
Mn2+
-
1-10 mM, 2-3fold stimulation
Na+
-
slight stimulation
Na+
-
slight stimulation
Na+
-
10 mM, 2fold stimulation
Na+
-
activates
NaCl
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
NH4+
Gleichenia glauca
-
activates
NH4+
-
strong activation
phosphate
-
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
Zn2+
-
Km: 0.0011 mM, absolute requirement for a divalent metal ion, Zn2+ or Mn2+ are the best activators, followed by Co2+
Zn2+
-
activates
Zn2+
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
Mn2+
-
activates
additional information
-
the native enzyme probably contains a bound divalent cation, Mg2+, Mn2+, or Zn2+, which is absolutely required for activity
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+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,5-Anhydro-D-glucitol 6-phosphate
-
-
1-Deoxy-1-(phosphonomethyl)myo-2-inosose
-
competitive
2-Deoxy-2-fluoroglucose 6-phosphate
-
-
2-Deoxy-2-fluoroglucose 6-phosphate
-
competitive
2-deoxy-D-glucitol
-
-
2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate
-
binding structure, interaction with active site residues, overview
-
2-Deoxy-D-glucitol 6-phosphate
-
-
2-deoxy-D-glucose 6-phosphate
-
-
2-deoxy-D-glucose 6-phosphate
-
-
2-deoxy-D-glucose 6-phosphate
-
-
2-deoxy-D-glucose 6-phosphate
-
-
2-deoxy-D-glucose 6-phosphate
-
competitive
2-deoxy-D-glucose 6-phosphate
-
-
2-deoxy-glucitol-6-phosphate
-
the inhibitor induces folding of the catalytic domain
-
2-Deoxy-myo-inositol 1-phosphate
-
competitive
choline
-
slight inhibition
Cu2+
Gleichenia glauca
-
-
Cu2+
-
strong inhibition
D-Allose 6-phosphate
-
-
D-fructose 6-phosphate
-
-
D-galactose 6-phosphate
-
-
D-gluconate 6-phosphate
-
-
D-glucose 6-phosphate
-
the beta-anomer is preferred as substrate, the alpha-anomer is an inhibitor
D-mannitol 6-phosphate
-
-
D-mannose 6-phosphate
-
-
D-mannose 6-phosphate
-
-
D-mannose 6-phosphate
-
competitive
D-sorbitol 6-phosphate
-
-
dihydroxyacetone phosphate
-
-
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+
EDTA
-
reactivation by Mn2+
EDTA
-
no inhibition
EDTA
-
inhibition
EDTA
-
no inhibition
EDTA
-
reactivation by some divalent cations
EDTA
-
0.002 mM, 50% inhibition
Endogeneous inhibitor from latex serum
-
-
-
Hg2+
Gleichenia glauca
-
-
Hg2+
-
strong inhibition
Inositol
-
feedback/product inhibition by inhibition of INO1 gene transcription, acts as a metabolic sensor
K+
-
concentration-dependent inhibition up to 5 mM
K+
-
5 mM, 10-15% inhibition
K+
-
concentration-dependent inhibition up to 5 mM
Li+
-
14 mM, 50% inhibition in absence of NH4+. Only 10% inhibition in presence of 14 mM NH4+
Mg2+
-
inhibitory only at nonphysiological concentrations
Mn2+
-
inhibitory only at nonphysiological concentrations
Mn2+
-
slight inhibition
myo-2-Inosose 1-phosphate
-
competitive
myo-2-Inosose 1-phosphate
-
competitive
Na+
-
153 mM, 78% inhibition
Na+
-
1 mM and above; chloroplastic and cytosolic enzyme
Na+
-
1 mM and above; chloroplastic enzyme
Na+
-
slight inhibition
NaBH4
-
partial inactivation in presence of NAD+. No inactivation in absence of NAD+
NEM
-
protection by D-glucose 6-phosphate in presence of NAD+
p-Substituted mercuribenzoate
-
1 mM, 93% inhibition in presence of 1 mM NADH
PCMB
-
protection by D-glucose 6-phosphate in presence of NAD+
pyridoxal 5'-phosphate
-
-
Trinitrobenzene sulphonate
-
-
valnoctamide
-
valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate, competitive
Valproate
-
slight inhibition
Valproate
-
noncompetitive, specific, only in vivo, e.g. in brain post mortem, no inhibition of the purified rcombinant enzyme in vitro
valrocemide
-
valproate derivative with anticonvulsant effect. Drastic inhibition of enzyme at 1 mM in crude brain homogenate
Zn2+
-
1 mM, 5fold decrease in activity
Zn2+
Gleichenia glauca
-
-
Zn2+
-
strong inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ethanol
-
stimulates
NaCl
A4UMS1
leaf L-myo-inositol 1-phosphate concentration increases 40fold during the first 6 h of salt stress (exposure to 300 mM NaCl)
NH4+
-
14 mM, 40% stimulation
NH4+
-
50 mM, 2fold stimulation
NH4+
-
stimulates
NH4+
-
21.5fold stimulation
NH4+
-
optimal stimulation at 10 mM (NH4)2SO4
NH4+
-
stimulates
NH4+
-
between 2.5fold and 3fold stimulation in presence of 12 mM NH4Cl; stimulates
NH4+
-
10-14 mM NH4Cl, 5fold stimulation. Other NH4+ salts are strong inhibitors
NH4+
-
10-14 mM NH4Cl, 5fold stimulation. Other NH4+ salts are strong inhibitors
NH4+
-
stimulates
NH4+
-
5 mM, 5fold increase in activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.12
-
D-glucose 6-phosphate
-
90C, pH 7.5
0.24
-
D-glucose 6-phosphate
-
with addition of 5% ethanol plus 50 mM KCl
0.26
-
D-glucose 6-phosphate
-
with addition of 20 mM NH4Cl
0.26
-
D-glucose 6-phosphate
-
NAD+, chloroplastic enzyme
0.67
0.72
D-glucose 6-phosphate
-
pH 7.5, 30C, dependent on the assay method, presence or absence of Mg2+
0.8
-
D-glucose 6-phosphate
-
pH 7.6, 37C
0.9
-
D-glucose 6-phosphate
-
with addition of 5% ethanol
0.922
-
D-glucose 6-phosphate
Gleichenia glauca
-
pH 7.5
0.97
-
D-glucose 6-phosphate
-
pH 7.5, recombinant refolded enzyme
1.05
-
D-glucose 6-phosphate
-
pH 7.0-7.5, 30C
1.18
-
D-glucose 6-phosphate
-
-
1.19
-
D-glucose 6-phosphate
-
pH 7.5, native enzyme
1.2
-
D-glucose 6-phosphate
-
-
1.8
-
D-glucose 6-phosphate
Q7XZE6
native enzyme
1.9
-
D-glucose 6-phosphate
-
-
1.97
-
D-glucose 6-phosphate
-
native enzyme
2.5
-
D-glucose 6-phosphate
Q7XZE6
recombinant enzyme
2.5
-
D-glucose 6-phosphate
Q7XZE6
wild-type
2.63
-
D-glucose 6-phosphate
B6SBM1, B6SBM2, -
isozyme MIPS1
2.7
-
D-glucose 6-phosphate
-
-
2.7
-
D-glucose 6-phosphate
B6SBM1, B6SBM2, -
isozyme MIPS2
2.83
-
D-glucose 6-phosphate
Q7XZE6
mutant lacking amino acids 174-210
3
-
D-glucose 6-phosphate
-
recombinant enzyme
3
-
D-glucose 6-phosphate
-
wild-type, 37C
3.19
-
D-glucose 6-phosphate
-
mutant bearing amino acids 174-210 of Porteresia coarctata enzyme, 37C
3.4
-
D-glucose 6-phosphate
-
presence of 0.6 mM valnoctamide, pH 7.6, 37C
3.5
-
D-glucose 6-phosphate
-
pH 7.5, 37C, 7.5, recombinant enzyme
3.89
-
D-glucose 6-phosphate
-
-
4.4
-
D-glucose 6-phosphate
-
-
4.47
-
D-glucose 6-phosphate
-
-
0.035
-
glucose 6-phosphate
-
-
0.06
-
glucose 6-phosphate
-
-
0.33
-
glucose 6-phosphate
-
-
0.5
-
glucose 6-phosphate
-
-
0.52
-
glucose 6-phosphate
-
-
0.57
-
glucose 6-phosphate
-
-
1.95
-
glucose 6-phosphate
-
cytosolic enzyme from streptomycin-bleached cells, and chloroplastidic enzyme
1.97
-
glucose 6-phosphate
-
cytosolic enzyme
2.14
-
glucose 6-phosphate
-
chloroplastic enzyme
2.17
-
glucose 6-phosphate
-
cytosolic enzyme
2.25
-
glucose 6-phosphate
-
cytosolic enzyme from green cells
2.51
-
glucose 6-phosphate
-
cytosolic enzyme from dark-grown cells
0.0051
-
NAD+
-
90C, pH 7.5
0.008
-
NAD+
-
-
0.08
-
NAD+
-
chloroplastic enzyme
0.11
-
NAD+
-
cytosolic enzyme
0.12
-
NAD+
-
chloroplastic enzyme
0.14
-
NAD+
-
cytosolic enzyme
0.16
-
NAD+
-
cytosolic enzyme from green cells
0.19
-
NAD+
-
cytosolic enzyme from dark-grown cells
0.2
-
NAD+
-
cytosolic enzyme from streptomycin-bleached cells
0.42
-
NAD+
-
pH 7.5, 37C, 7.5, recombinant enzyme
0.9
-
NAD+
Gleichenia glauca
-
pH 7.5
1.67
-
NAD+
-
pH 7.5, recombinant refolded enzyme
1.95
-
NAD+
-
pH 7.5, native enzyme
2.85
-
glucose 6-phosphate
-
chloroplastic enzyme
additional information
-
additional information
-
dissociation constants
-
additional information
-
additional information
-
Vmax is 2.95 mM
-
additional information
-
additional information
-
kinetics, effects of different divalent metal ions, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0817
-
D-glucose 6-phosphate
-
pH 7.5, 30C, periodate assay method, in absence of 1 mM Mg2+
0.102
-
D-glucose 6-phosphate
-
pH 7.5, 30C, periodate assay method, in presence of 1 mM Mg2+
0.107
-
D-glucose 6-phosphate
-
pH 7.5, 30C, IMP-coupled assay method, in presence of 1 mM Mg2+
0.3
-
D-glucose 6-phosphate
-
pH 7.5, 30C, IMP-coupled assay method, in presence of 10 mM Mg2+
9.6
-
D-glucose 6-phosphate
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.12
-
D-glucose 6-phosphate
-
pH 7.5, 30C, periodate assay method, in absence of 1 mM Mg2+
9206
0.14
-
D-glucose 6-phosphate
-
pH 7.5, 30C, periodate assay method, in presence of 1 mM Mg2+
9206
0.157
-
D-glucose 6-phosphate
-
pH 7.5, 30C, IMP-coupled assay method, in presence of 1 mM Mg2+
9206
0.233
-
D-glucose 6-phosphate
-
pH 7.5, 30C, IMP-coupled assay method, in presence of 10 mM Mg2+
9206
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00067
-
2-deoxy-D-glucitol
-
pH 5.5
0.18
-
valnoctamide
-
pH 7.6, 37C
0.21
-
Valproate
-
brain, post mortem
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0003
-
-
crude enzyme, in 50mM Bicine buffer (pH 8.5), at 60C
0.013
-
-
purified recombinant refolded enzyme, with cofactor NADP+
0.015
-
-
purified recombinant refolded enzyme, with cofactor NAD+
0.018
-
-
purified native enzyme, with cofactor NADP+
0.02
-
-
purified native enzyme, with cofactor NAD+
0.05
-
-
value about, culture condition: 2 days, 30C
0.06
-
-
value about, culture condition: 3 days, 30C
0.1
-
-
value about, culture condition: 1 day, 30C
0.216
-
-
-
0.26
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
-
-
7.2
-
-
chloroplastic enzyme
7.2
-
-
mammary gland
7.2
-
-
chloroplastic enzyme
7.3
7.8
-
-
7.5
-
-
cytosolic enzyme
7.5
-
-
-
7.5
-
-
brain
7.5
-
Q7XZE6
native enzyme
7.5
-
-
recombinant enzyme
7.5
-
Gleichenia glauca
-
-
7.5
-
-
assay at
7.5
-
-
recombinant enzyme
7.5
-
-
wild-type
7.5
-
B6SBM1, B6SBM2, -
;
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
cytosolic and chloroplastic enzyme
7.6
-
-
chloroplastic enzyme
7.6
-
-
chloroplastic enzyme
7.7
-
-
testis
7.7
-
-
assay at
7.8
-
-
cytosolic enzyme
8
8.5
-
mutant bearing amino acids 174-210 of Porteresia coarctata enzyme
8
-
-
at 37C
8
-
Q7XZE6
recombinant enzyme
8
-
Q7XZE6
-
8.2
-
-
cytosolic enzyme
8.2
-
-
native enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
Q9FPK7, -
assay at
30
-
-
assay at
35
-
Q7XZE6
native enzyme
35
-
-
native enzyme
35
-
B6SBM1, B6SBM2, -
;
37
-
-
-
37
-
Q7XZE6
recombinant enzyme
37
-
-
recombinant enzyme
37
-
Q7XZE6
-
37
-
-
-
40
-
-
recombinant enzyme
90
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
50
-
increasing activity from 20C to 40 C, rapid loss of 60% activity at 50C, inactive at 60C
76
100
-
76C: about 40% of maximal activity, 100C: about 50% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.08
-
A4UMS1
calculated from amino acid sequence
7.5
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
fetal and adult
Manually annotated by BRENDA team
-
moderately high expression
Manually annotated by BRENDA team
-
highest expression of isoform MIPS1
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
-
-
-
Manually annotated by BRENDA team
-
grown in a fermenter in an inositol-deficient medium
Manually annotated by BRENDA team
-
cotyledonary phase , MW 56000 enzyme form; globular stage; MW 33000 enzyme form
Manually annotated by BRENDA team
-
highly expressed in developing seed embryos and in the aleurone layer
Manually annotated by BRENDA team
B6SBM1, B6SBM2, -
;
Manually annotated by BRENDA team
-
highest expression of isoform MIPS1
Manually annotated by BRENDA team
C4PW05
high expression level
Manually annotated by BRENDA team
-
dorsal root ganglia
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
isoform gammac predominates in intestine
Manually annotated by BRENDA team
Q9FPK7, -
-
Manually annotated by BRENDA team
-
moderately high expression
Manually annotated by BRENDA team
-
young needle
Manually annotated by BRENDA team
B6SBM1, B6SBM2, -
;
Manually annotated by BRENDA team
-
highest expression of isoform MIPS1
Manually annotated by BRENDA team
A8WEL5
lower levels of expression in young leaves
Manually annotated by BRENDA team
B6V6K8, B6V6K9
;
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
-
-
-
Manually annotated by BRENDA team
-
moderately high expression
Manually annotated by BRENDA team
-
moderately high expression
Manually annotated by BRENDA team
Gleichenia glauca
-
reproductive pinnule
Manually annotated by BRENDA team
-
mature, MW 33000 enzyme form; young, MW 56000 enzyme form
Manually annotated by BRENDA team
B6SBM1, B6SBM2, -
;
Manually annotated by BRENDA team
-
highest expression of isoform MIPS3
Manually annotated by BRENDA team
A8WEL5
strong expression
Manually annotated by BRENDA team
C4PW05
epidermal and cortical cells
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
-
epidermal and cortical cells
-
Manually annotated by BRENDA team
F4IIN3, P42801, Q9LX12
-
Manually annotated by BRENDA team
-, Q1HG62
presence of gene transcripts, peak at 9 days after pollination
Manually annotated by BRENDA team
-
seed-specific expression of isoform GmMIPS-1 in the outer integumentary layer during early seed development. Enzyme is associated with oxalate crystal idioblasts
Manually annotated by BRENDA team
B6SBM1, B6SBM2, -
-
Manually annotated by BRENDA team
-
highest expression of isoform MIPS2
Manually annotated by BRENDA team
A8WEL5
strong expression in developing seeds during embryogenesis
Manually annotated by BRENDA team
-
green cotyledons, MW 33000 enzyme form
Manually annotated by BRENDA team
-
highest expression of isoform MIPS1
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
-
-
-
Manually annotated by BRENDA team
B6SBM1, B6SBM2, -
;
Manually annotated by BRENDA team
-
highest expression of isoform MIPS1
Manually annotated by BRENDA team
-
low expression, isoform alpha predominates in spleen
Manually annotated by BRENDA team
A8WEL5
strong expression
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
-
-
-
Manually annotated by BRENDA team
-
isoform alpha predominates in testis
Manually annotated by BRENDA team
additional information
-
the enzyme activity is maximal during the logarithmic stage of growth and is decreased in the stationary phase
Manually annotated by BRENDA team
additional information
Q9FPK7, -
expression analysis in wild-type and ipa 1-1 mutant leaves
Manually annotated by BRENDA team
additional information
B6SBM1, B6SBM2, -
isozyme MIPS1 is not expressed in seeds
Manually annotated by BRENDA team
additional information
-
almost no expression in skeletal muscle
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
C4PW05
MIPS tissue expression analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
MW 33000 enzyme form, thylakoid membrane of fractionated leaf chloroplasts
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
-
-
-
Manually annotated by BRENDA team
-
high thermotolerance
Manually annotated by BRENDA team
C4PW05
associated, isozyme MIPS1
Manually annotated by BRENDA team
F4IIN3, P42801, Q9LX12
-
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia-0
-
associated, isozyme MIPS1
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16000
-
-
gammac isoform, SDS-PAGE
56300
-
-
isoform MIPS2, calculated from amino acid sequence
56400
-
-
isoform MIPS3, calculated from amino acid sequence
56500
-
-
isoform MIPS1, calculated from amino acid sequence
56500
-
A8WEL5
calculated from amino acid sequence
56690
-
A4UMS1
calculated from amino acid sequence
60000
-
B6V6K8, B6V6K9
SDS-PAGE; SDS-PAGE
60000
-
-
SDS-PAGE
68000
-
-
fully spliced alpha isoform, SDS-PAGE
105000
-
-
gel filtration
135000
-
-
gel filtration
150000
-
-
-
155000
-
-
-
157000
-
-
gel filtration
159000
-
-
gel filtration
165000
-
-
gel filtration
165000
-
-
gel filtration
168000
-
-
gel filtration
179000
-
-
cytosolic enzyme, gel filtration
179000
-
-
cytosolic enzyme, gel filtration
180000
-
Q7XZE6
native and recombinant enzyme, gel filtration
180000
-
-
native and recombinant enzyme, gel filtration
180000
-
-
about, recombinant enzyme form 2, gel filtration
200000
-
-
about, recombinant enzyme form 1, gel filtration
200300
-
-
cytosolic enzyme, gel filtration
209000
-
-
equilibrium centrifugation
210000
-
-
testis, gel filtration, PAGE, ultracentrifugal equilibrium sedimentation
215000
-
-
gel filtration
216000
-
-
gel filtration
218000
-
-
testis
240000
-
-
gel filtration
248000
-
-
chloroplastic enzyme, gel filtration
253000
-
-
chloroplastic enzyme, gel filtration
266000
-
-
chloroplastic enzyme, gel filtration
271000
-
-
approximately, recombinant enzyme, gel filtration
290000
-
-
mammary gland, gel filtration
345000
-
-
gel filtration, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 62000, SDS-PAGE
?
-
x * 61000, SDS-PAGE
?
-
x * 46249, calculation from nucleotide sequence
?
-
x * 57781,calculation from nucleotide sequence
?
-
x * 56337, calculation from nucleotide sequence
?
-
x * 56685, calculation from nucleotide sequence
?
-
x * 56761, calculation from nucleotide sequence
?
-
x * 56529, calculation from nucleotide sequence
?
-
x * 56388, calculation from nucleotide sequence
?
-
x * 62842, calculation from nucleotide sequence
?
-
two enzyme forms: MW 33000 and MW 56000 determined by SDS-PAGE. Its expression is temporally and spatially regulated
?
Q7XZE6
x * 60000, native and recombinant enzyme, SDS-PAGE
?
-
x * 60000, native and recombinant enzyme, SDS-PAGE
?
-
x * 65000, MALDI-TOF, x * 60100, calculated for acetolactate synthase large subunit which is identical to enzyme
?
Synechocystis sp. PCC6803
-
x * 65000, MALDI-TOF, x * 60100, calculated for acetolactate synthase large subunit which is identical to enzyme
-
hexamer
-
6 * 59000, SDS-PAGE
tetramer
-
2 * 35000 + 2 * 72000, SDS-PAGE
tetramer
-
4 * 67000, chloroplastic enzyme, SDS-PAGE
tetramer
-
4 * 61000, chloroplastic enzyme, SDS-PAGE
tetramer
-
4 * 59000, chloroplastic enzyme, SDS-PAGE
tetramer
-
4 * 54500
tetramer
-
4 * 62000, chloroplastic enzyme
tetramer
-
4 * 65000
tetramer
-
4 * 68000, testis
tetramer
-
4 * 62000
tetramer
-
4 * 58000
tetramer
-
4 * 44100, SDS-PAGE
tetramer
-
homotetramer formed by dimerization of dimers
tetramer
-
4 * 62000, SDS-PAGE
tetramer
-
x * 50000 + x * 65000, recombinant enzyme form 1, SDS-PAGE; x * 50000 + x * 65000, recombinant enzyme form 2, SDS-PAGE
trimer
-
3 * 68000, SDS-PAGE
trimer
-
3 * 59000, cytosolic enzyme, SDS-PAGE
trimer
-
3 * 67000, cytosolic enzyme, SDS-PAGE
trimer
-
3 * 61000, cytosolic enzyme, SDS-PAGE
trimer
-
3 * 45000, SDS-PAGE in presence of 2-mercaptoethanol
trimer
-
3 * 61000
trimer
-
-
homotrimer
-
x-ray crystallography
additional information
-
structure of the enzyme-NAD+-2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex
additional information
-
structure analysis
additional information
-
the protomer contains 2 domains, a Rossman fold with a C-terminal extension D1a, and a domain involving tetramerization D1b
additional information
-
the protomer contains 3 domains, a catalytic domain, a central domain, and an NAD+ binding domain
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 vapor-diffusion method
-
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
-
20 min, stable up to
50
-
-
rapid loss of 60% activity
60
-
-
20 min, approximately 60% loss of activity
60
-
-
complete loss of activity after 5 min
98
-
-
loss of 50% activity after about 40 min in 50 mM Tris-HCl, pH 8.0
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
additional information
-
-
addition of NAD+ increases thermotolerance of both cytosolic and chloroplast enzyme isoforms
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5 mM D-glucose 6-phosphate with 1 mM NAD+ stabilizes the enzyme
-
20% v/v glycerol, 2 mM PMSF, and 1 mM E-64 stabilize the native and the recombinant enzyme
-
salt-tolerant enzyme
Q7XZE6
optimal concentration of dithiothreitol for stability is 0.5 mM
-
rapid loss of activity on freezing and thawing
-
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 ACCESSION NO.
LITERATURE
4C, 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
-
-20C, purified recombinant enzyme, 20% v/v glycerol, completely stable for several weeks
-
-20C, partially purified enzyme is stable for at least 6 months
-
-20C, partially purified enzyme is stable for several months
-
4C, -20C or -70C, stable
-
0C, 70% loss of activity after 18 h, enzyme in crude extract. Stabilization by (NH4)2SO4 and dimethyl sulfoxide in 20% solution
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HiTrap chelating column chromatography
-
recombinant enzyme
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
-
DEAE-Sephacel column chromatography and Superose 12 gel filtration; DEAE-Sephacel column chromatography and Superose 12 gel filtration
B6SBM1, B6SBM2, -
recombinant His-tagged INOS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
from the reproductive pinnules by low-speed centrifugation, streptomycin sulfate precipitation, ammonium sulafte fractionation, DEAE ion exchange chromatography, and gel filtration
Gleichenia glauca
-
partial
-
recombinant enzyme
-
partially purified by ammonium sulfate fractionation (50-70%)
-
Superose12 gel filtration and DEAE Sephace gel filtration; Superose12 gel filtration and DEAE Sephace gel filtration
B6V6K8, B6V6K9
Superose12 gel filtration and DEAE Sephace gel filtration
-
partial
-
affinity chromatography
-
ammonium sulfate saturation, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
-
recombinant, solubilized and refolded enzyme from Escherichia coli strain BL21(DE3) and native enzyme by ion exchange chromatography and gel filtration
-
about 85fold from young needles
-
Ni-NTA resin chromatography
A4UMS1
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
P42801, Q38862, Q9LX12
gene MIPS
C4PW05
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; 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; 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
F4IIN3, P42801, Q9LX12
overexpression in Escherichia coli
-
overexpression in Escherichia coli strain BL21(DE3)
-
expressed in Schizosaccharomyces pombe; expressed in Schizosaccharomyces pombe
B6SBM1, B6SBM2, -
DNA sequence determination and analysis, expression of His-tagged INOS in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
gene INO1, DNA sequence analysis, expression in Saccharomyces cerevisiae
-
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
-
isoform gammac is expressed in Escherichia coli Rosetta (DE3) pLysS cells
-
gene MIPS, DNA and amino acid sequence determination and analysis, sequence comparisons, semi-quantitative RT-PCR expression analysis in different tissues
C7B9C0, -
expression in Escherichia coli
-
gene INO1, DNA sequence analysis, expression is regulated by inositol and Opi1p, phylogenetic analysis
-
overexpression in Escherichia coli
-
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)pLysS cells
A4UMS1
cloning of gene MIPS encoding the enzyme, DNA sequence determination
Q9FPK7, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Opi1p is a transcriptional repressor INO1
-
MIPS expression is increased in leaves, stems, and roots after drought stress
C7B9C0, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
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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
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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
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site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps
K367A
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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
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site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
K369A
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mutation results in complete loss of activity; site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
K412A
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mutation results in complete loss of activity; site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
additional information
C4PW05
construction of transgenic plants expressing GFP-tagged MIPS using Agrobacterium tumefaciens GV3101 transfection method, overview
additional information
F4IIN3, P42801, Q9LX12
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; 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; 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
Arabidopsis thaliana Columbia-0
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construction of transgenic plants expressing GFP-tagged MIPS using Agrobacterium tumefaciens GV3101 transfection method, overview
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N255A
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site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows reduced activity
additional information
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the human enzyme can functionally complement the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain
additional information
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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
-
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
Q7XZE6
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
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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
K489A
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mutation results in complete loss of activity; site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
additional information
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the enzyme-deficient ino1 mutant strain can be functionally complemented by expression of the human enzyme
additional information
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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
Synechocystis sp. PCC6803
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enzyme gene can complement inositol auxotroph Saccharomyces cerevisiae strain FY250 and the natural inositol auxotroph Schizosaccharomyces pombe
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additional information
Q9FPK7, -
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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anticonvulsants valnoctamide and valrocemide drastically reduce enzyme activity in crude brain homogenate
pharmacology
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the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs
medicine
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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
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the enzyme is a target for mood stabilizing drugs, and anti-bipolar drugs
biotechnology
Q9FPK7, -
the enzyme is a possible target for genetic modification of maize plants to get low phytic acid containing variants