EC Number |
Protein Variants |
Reference |
---|
1.1.1.18 | 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 |
740059 |
1.1.1.18 | analysis |
specific determination of myo-inositol using a fluorophotometer to measure the fluorescence of NADH released by enzyme immobilized on porous glass |
656606 |
1.1.1.18 | D172N |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
685170 |
1.1.1.18 | 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 |
740059 |
1.1.1.18 | H176A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
685170 |
1.1.1.18 | K97V |
site-directed mutagenesis, inactive mutant |
711151 |
1.1.1.18 | more |
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 |
-, 760719 |
1.1.1.18 | more |
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 |
740059 |
1.1.1.18 | more |
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 |
760767 |
1.1.1.18 | up |
iolG expression is induced by myo-inositol, and less by scyllo-inositol |
-, 712965 |