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(1S,2S,3R,4S,5S)-5-(allyloxy)cyclohexane-1,2,3,4-tetrol + NAD+
?
Substrates: -
Products: -
?
(1S,2S,3R,4S,5S)-5-(benzyloxy)cyclohexane-1,2,3,4-tetrol + NAD+
?
Substrates: -
Products: -
?
(1S,2S,3R,4S,5S)-5-methoxycyclohexane-1,2,3,4-tetrol + NAD+
?
Substrates: -
Products: -
?
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoic acid + NAD+
?
Substrates: -
Products: -
?
4-methylbenzenesulfonyl-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-((1S)-10-camphor-sulfonyl)-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-((4-methyloxycarbonyl)-benzyl)-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-(4-carboxybenzyl)-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-(trans-cinnamoyl)-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-allyl-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-alpha-D-glucopyranosyl-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-benzyl-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-methyl-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-[(2-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
4-O-[(3-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
alpha-D-glucopyranose + NAD+
D-gluconate + NADH
-
Substrates: 4fold lower activity compared to myo-inositol as substrate, does not act with the beta-anomer
Products: -
?
alpha-D-glucopyranosyl-(1,6)-myo-inositol + NAD+
?
-
Substrates: -
Products: -
?
D-2,3-diketo-4-deoxy-epi-inositol + NADH
ketodeoxyinositol + NAD+
-
Substrates: -
Products: -
?
D-chiro-inositol + NAD+
? + NADH
-
Substrates: 19% of the activity with myo-inositol
Products: -
?
D-glucose + NAD+
D-gluconate + NADH
epi-inositol + NAD+
? + NADH
-
Substrates: 4% of the activity with myo-inositol
Products: -
?
epi-inositol + NAD+
epi-inosose + NADH
-
Substrates: 5% of the activity compared to myo-inositol as substrate, conversion of epi-inosose 5% of the activity compared to scyllo-inosose as substrate
Products: -
r
melibiose + NAD+
?
Substrates: -
Products: -
?
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate + NAD+
?
Substrates: -
Products: -
?
myo-inositol + 2,6-dichlorophenolindophenol
2,4,6/3,5-pentahydroxycyclohexanone + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
r
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
myo-inositol + NAD+
scyllo-inosose + NADH
myo-inositol + NAD+
scyllo-inosose + NADH + H+
scyllo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: 5% of the activity compared to myo-inositol as substrate
Products: -
?
[(4-methylphenyl)methyl]-myo-inositol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
additional information
?
-
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
-
Substrates: -
Products: -
r
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
-
Substrates: -
Products: -
r
D-glucose + NAD+
D-gluconate + NADH
-
Substrates: -
Products: -
?
D-glucose + NAD+
D-gluconate + NADH
Substrates: 9% of the activity compared to myo-inositol as substrate
Products: -
?
D-xylose + NAD+
? + NADH
-
Substrates: very low activity
Products: -
?
D-xylose + NAD+
? + NADH
Substrates: 7% of the activity compared to myo-inositol as substrate
Products: -
?
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
-
Substrates: -
Products: -
r
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
-
Substrates: -
Products: -
r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: should be classified as A-type enzyme
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: involved in nitrogen fixation and nodulation of soybean
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: involved in nitrogen fixation and nodulation of soybean
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: involved in rhizopine utilization
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: i.e. scyllo-inosose
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: i.e. scyllo-inosose
?
myo-inositol + NAD+
scyllo-inosose + NADH
Substrates: -
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: first enzyme in the catabolic pathway of myo-inositol
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: oxidation of the axial hydroxyl group of myo-inositol
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: 75 times lower activity compared to the reverse reaction
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: -
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
Substrates: -
Products: -
?
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
Substrates: -
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH + H+
Substrates: -
Products: -
?
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
Substrates: the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
Products: -
?
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
Substrates: -
Products: -
r
pinitol + NADH + H+
?
-
Substrates: i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
Products: -
?
pinitol + NADH + H+
?
-
Substrates: i.e. 3-O-methyl-D-chiro-inositol
Products: -
?
pinitol + NADH + H+
?
-
Substrates: i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
Products: -
?
pinitol + NADH + H+
?
-
Substrates: i.e. 3-O-methyl-D-chiro-inositol
Products: -
?
additional information
?
-
Substrates: a nonpolar cavity adjacent to the active site, allows racemic protected inositol derivatives such as 4-O-benzyl-myo-inositol to be recognized with very high stereoselectivity. Trace activity with (1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl dihydrogen phosphate
Products: -
?
additional information
?
-
-
Substrates: a nonpolar cavity adjacent to the active site, allows racemic protected inositol derivatives such as 4-O-benzyl-myo-inositol to be recognized with very high stereoselectivity. Trace activity with (1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl dihydrogen phosphate
Products: -
?
additional information
?
-
Substrates: substrate specificity and substrate binding structure, molecular modeling, overview
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and substrate binding structure, molecular modeling, overview
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose
Products: -
?
additional information
?
-
-
Substrates: scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
Products: -
?
additional information
?
-
-
Substrates: structure-function analysis, overview
Products: -
?
additional information
?
-
-
Substrates: scyllo-inositol is no substrate for the enzyme, thus IolG does not act as a scyllo-inositol dehydrogenase
Products: -
?
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1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
D-2,3-diketo-4-deoxy-epi-inositol + NADH
ketodeoxyinositol + NAD+
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
myo-inositol + NAD+
scyllo-inosose + NADH
myo-inositol + NAD+
scyllo-inosose + NADH + H+
additional information
?
-
-
Substrates: the enzyme shows a broad substrate spectrum while remaining highly stereoselective. BsIDH is able to oxidize the mono-saccharides alpha-D-glucose and alpha-D-xylose but not beta-D-glucose, D-mannose and D-galactose
Products: -
?
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
-
Substrates: -
Products: -
r
1-oxo-D-chiro-inositol + NADH + H+
D-chiro-inositol + NAD+
-
Substrates: -
Products: -
r
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
-
Substrates: -
Products: -
r
myo-inositol + NAD+
2,3,4,5,6-pentahydroxycyclohexanone + NADH + H+
-
Substrates: -
Products: -
r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: should be classified as A-type enzyme
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: involved in nitrogen fixation and nodulation of soybean
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: involved in nitrogen fixation and nodulation of soybean
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
Substrates: involved in rhizopine utilization
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: i.e. scyllo-inosose
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
r
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
?
myo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: i.e. scyllo-inosose
?
myo-inositol + NAD+
scyllo-inosose + NADH
Substrates: -
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: first enzyme in the catabolic pathway of myo-inositol
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: 75 times lower activity compared to the reverse reaction
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: -
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH
-
Substrates: -
Products: -
?
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
Substrates: -
Products: -
r
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
Substrates: the NAD+-dependent enzyme catalyses the oxidation of the axial hydroxyl group of myo-inositol to form scyllo-inosose
Products: -
?
myo-inositol + NAD+
scyllo-inosose + NADH + H+
-
Substrates: -
Products: -
r
pinitol + NADH + H+
?
-
Substrates: i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
Products: -
?
pinitol + NADH + H+
?
-
Substrates: i.e. 3-O-methyl-D-chiro-inositol. Bacillus subtilis can utilize pinitol as the sole carbon source via the same myo-inositol catabolic pathway
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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7
(1S,2S,3R,4S,5S)-5-(allyloxy)cyclohexane-1,2,3,4-tetrol
25°C, pH 9.0
4
(1S,2S,3R,4S,5S)-5-(benzyloxy)cyclohexane-1,2,3,4-tetrol
25°C, pH 9.0
8
(1S,2S,3R,4S,5S)-5-methoxycyclohexane-1,2,3,4-tetrol
25°C, pH 9.0
44
4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoic acid
25°C, pH 9.0
9
alpha-D-glucopyranosyl-(1,6)-myo-inositol
-
-
57
melibiose
25°C, pH 9.0
3
methyl 4-([[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxycyclohexyl]oxy]methyl)benzoate
25°C, pH 9.0
4
myo-inositol
pH 9.0, 25°C, recombinant mutant Y233F
4.4
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
18
myo-inositol
25°C, pH 9.0
28
myo-inositol
pH 9.0, 25°C, recombinant mutant D179N
39
myo-inositol
pH 9.0, 25°C, recombinant mutant Y235F
65
myo-inositol
pH 9.0, 25°C, recombinant mutant D172N
118
myo-inositol
pH 9.0, 25°C, recombinant mutant H176A
0.07
NAD+
pH 9.0, 25°C, recombinant mutant Y233F
0.08
NAD+
pH 9.0, 25°C, recombinant wild-type enzyme
0.11
NAD+
pH 9.0, 25°C, recombinant mutant Y235F
0.3
NAD+
pH 9.0, 25°C, recombinant mutant H176A
0.4
NAD+
pH 9.0, 25°C, recombinant mutant D179N
1.1
NAD+
pH 9.0, 25°C, recombinant mutant D172N
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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
K97V
-
site-directed mutagenesis, inactive mutant
up
-
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
Y233R
site-directed mutagenesis, inactive mutant
Y235F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y235R
site-directed mutagenesis, inactive mutant
up
-
iolG expression is induced by myo-inositol, and less by scyllo-inositol
-
analysis
-
specific determination of myo-inositol using a fluorophotometer to measure the fluorescence of NADH released by enzyme immobilized on porous glass
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
-
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
-
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
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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
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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
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