1.1.1.18: inositol 2-dehydrogenase
This is an abbreviated version!
For detailed information about inositol 2-dehydrogenase, go to the full flat file.
Reaction
Synonyms
BsIDH, cg0204, GK1898, IDH, inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase, inositol dehydrogenase, iolG, iolG1, iolG2, LcIDH1, LcIDH2, MI dehydrogenase, More, myo-inositol 2-dehydrogenase, myo-inositol dehydrogenase, myo-inositol:NAD2 oxidoreductase
ECTree
1.1.1.18 inositol 2-dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.1.1.18 - inositol 2-dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A12K/D35S/V36R
site-directed mutagenesis, the triple mutant has a value of 570000 M/s in reaction with NADP+, higher than that of the wild-type IDH with NAD+. The binding of the coenzyme in the mutant is altered such that although the nicotinamide ring maintains the required position for catalysis, the coenzyme has twisted by nearly 90°, so the adenine moiety no longer binds to a hydrophobic cleft in the Rossmann fold as in the wild-type enzyme
D172N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D35S/V36R
site-directed mutagenesis, the double mutant prefers NADP+ to NAD+ by a factor of 5. The mutant is an excellent catalyst with a second-order rate constant with respect to NADP of 370000 M/s
H176A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
up
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iolG expression is induced by myo-inositol, and less by scyllo-inositol
Y233F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y235F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
up
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iolG expression is induced by myo-inositol, and less by scyllo-inositol
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analysis
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specific determination of myo-inositol using a fluorophotometer to measure the fluorescence of NADH released by enzyme immobilized on porous glass
additional information
additional information
convertion of NAD+-specific inositol dehydrogenase to an efficient NADP+-selective catalyst to enhance understanding of coenzyme selectivity and to create an enzyme capable of recycling NADP+ in biocatalytic processes
additional information
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convertion of NAD+-specific inositol dehydrogenase to an efficient NADP+-selective catalyst to enhance understanding of coenzyme selectivity and to create an enzyme capable of recycling NADP+ in biocatalytic processes
additional information
construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
additional information
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construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
additional information
-
construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
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additional information
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construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
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additional information
-
construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
-
additional information
-
construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
-
additional information
-
construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
-
additional information
-
construction of Corynebacterium glutamicum DELTAiolR strain. Loss of the transcriptional regulator IolR in an evolved strain variant, termed WMB2evo, drastically increases the growth rate in D-xylose containing media. The myo-inositol/proton symporter IolT1, whose gene is under control of IolR, contributes to D-xylose uptake, ultimately leading to the observed improved growth phenotype. Batch and fed-batch processes for production of D-xylonate with C. glutamicum DELTAiolR, overview. The endogenous myo-inositol dehydrogenase IolG is mainly responsible for the oxidation of D-xylose in Corynebacterium glutamicum. D-Xylonate production with Corynebacterium glutamicum DELTAiolR is characterized by a high volumetric productivity and maximum product yield under batch and fed-batch process conditions applying defined D-xylose/D-glucose mixtures and hydrolyzed bagasse, respectively
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additional information
thermophilic myo-inositol 2-dehydrogenase (IDH) and scyllo-inositol 2-dehydrogenase (SIDH, EC 1.1.1.370) from Geobacillus kaustophilus are co-expressed in Escherichia coli strain BL21(DE3). The Escherichia coli cells containing the two enzymes are permeabilized by heat treatment (heat treatment at 70°C for 20 min for cell permeabilization) as whole-cell catalysts to convert myo-inositol (MI) to scyllo-inositol (SI). After condition optimizations about permeabilized temperature, reaction temperature, and initial MI concentration, about 82 g/l of SI is produced from 250 g/l of MI within 24 h without any cofactor supplementation. The whole-cell catalytic pathway for SI synthesis is initiated by oxidation of MI to scyllo-inosose catalyzed by cofactor NAD+-dependent IDH. Scyllo-inosose is subsequently reduced to SI by SIDH in the presence of NADH. Recycling of NAD+/NADH is achieved in the whole pathway. The specific activity of SIDH is lower than that of IDH, so SIDH is the rate-limiting step in the two-step cascade reaction. The optimal pH of SIDH is 7.0 and IDH does not become the rate-limited enzyme at pH 7.0. The optimal reaction temperature for SI production is set at 60°C, instabilty and loss of activity at 75°C and above. Method development, overview
