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	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	-, 760719	
1.1.1.18	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	740059	
1.1.1.18	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	760767	
1.1.1.18	up	iolG expression is induced by myo-inositol, and less by scyllo-inositol	-, 712965	
1.1.1.18	Y233F	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	685170	
1.1.1.18	Y233R	site-directed mutagenesis, inactive mutant	685170	
1.1.1.18	Y235F	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	685170	
1.1.1.18	Y235R	site-directed mutagenesis, inactive mutant	685170