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arabitol + NAD(P)+
? + NAD(P)H
-
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabitol + NAD+
?
-
-
-
?
D-arabitol + NAD+
? + NADH
D-fructose + NAD(P)+
? + NAD(P)H
-
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
D-fructose + NADPH + H+
D-mannitol + NADP+
D-fructose + polyethylenimine-NH-succinyl-NADH + H+
D-mannitol + polyethylenimine-NH-succinyl-NAD+
-
-
-
-
r
D-fructose 1-phosphate + NADH
?
D-glucitol + NAD+
?
4% of the activity with D-mannitol
-
-
?
D-glucitol + NAD+
? + NADH
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
D-mannitol + NAD+
D-fructose + NADH + H+
D-mannitol + NADP+
D-fructose + NADPH + H+
D-mannitol + polyethyleneglycol-NH-succinyl-aminoethyl-NAD+
D-fructose + polyethyleneglycol-NH-succinyl-aminoethyl-NADH
-
-
-
?
D-mannitol + polyethyleneglycol-NH-succinyl-NAD+
D-fructose + polyethyleneglycol-NH-succinyl-NADH
-
-
-
?
D-mannitol + polyethylenimin-NH-succinyl-NAD+
D-fructose + polyethylenimin-NH-succinyl-NADH
-
-
-
?
D-sorbitol + NAD+
?
-
-
-
-
r
D-tagatose + NAD(P)+
? + NAD(P)H
29% relative activity compared to D-fructose
-
-
?
D-tagatose + NAD+
?
29% relative activity on D-tagatose compared to 100% activity on D-fructose
-
-
?
D-xylose + NADH + H+
D-xylitol + NAD+
18% activity compared to D-fructose
-
-
r
D-xylulose + NAD(P)+
? + NAD(P)H
18% relative activity compared to D-fructose
-
-
?
D-xylulose + NAD+
?
18% relative activity on D-xylulose compared to 100% activity on D-fructose
-
-
?
D-xylulose + NADH + H+
D-arabinitol + NAD+
-
-
-
?
isomaltulose + NAD(P)+
? + NAD(P)H
-
-
-
-
?
L-sorbitol + NAD+
L-sorbose + NADH + H+
L-sorbose + NAD(P)+
? + NAD(P)H
5% relative activity compared to D-fructose
-
-
?
L-sorbose + NADH + H+
L-sorbitol + NAD+
meso-erythritol + NAD+
?
-
-
-
?
sorbitol + NAD(P)+
? + NAD(P)H
-
-
-
-
?
targatose + NADH + H+
? + NAD+
29% activity compared to D-fructose
-
-
r
additional information
?
-
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabitol + NAD+
? + NADH
-
-
-
?
D-arabitol + NAD+
? + NADH
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-mannitol production
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-mannitol production
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
Asn300 has an auxiliary role in stabilization of the transition state of hydride transfer and His303 contributes to substrate positioning, role of Lys295 in general base enzymic catalysis
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
the Thermotoga maritima MtDH pathway produces D-mannitol from glucose in two steps: first the xylose isomerase from Thermotoga neapolitana converts glucose to fructose, then MtDH converts D-fructose to D-mannitol
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
the Thermotoga maritima MtDH pathway produces D-mannitol from glucose in two steps: first the xylose isomerase from Thermotoga neapolitana converts glucose to fructose, then MtDH converts D-fructose to D-mannitol
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
the Thermotoga maritima MtDH pathway produces D-mannitol from glucose in two steps: first the xylose isomerase from Thermotoga neapolitana converts glucose to fructose, then MtDH converts D-fructose to D-mannitol
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
the Thermotoga maritima MtDH pathway produces D-mannitol from glucose in two steps: first the xylose isomerase from Thermotoga neapolitana converts glucose to fructose, then MtDH converts D-fructose to D-mannitol
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
the Thermotoga maritima MtDH pathway produces D-mannitol from glucose in two steps: first the xylose isomerase from Thermotoga neapolitana converts glucose to fructose, then MtDH converts D-fructose to D-mannitol
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
-
?
D-fructose + NADPH + H+
D-mannitol + NADP+
low activity
-
-
r
D-fructose + NADPH + H+
D-mannitol + NADP+
also active on fructose with NADPH
-
-
?
D-fructose + NADPH + H+
D-mannitol + NADP+
low activity
-
-
r
D-fructose + NADPH + H+
D-mannitol + NADP+
low activity
-
-
r
D-fructose + NADPH + H+
D-mannitol + NADP+
low activity
-
-
r
D-fructose + NADPH + H+
D-mannitol + NADP+
also active on fructose with NADPH
-
-
?
D-fructose + NADPH + H+
D-mannitol + NADP+
low activity
-
-
r
D-fructose 1-phosphate + NADH
?
-
-
-
?
D-fructose 1-phosphate + NADH
?
-
-
-
?
D-glucitol + NAD+
? + NADH
-
-
-
?
D-glucitol + NAD+
? + NADH
-
-
-
-
?
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
-
-
-
r
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
-
-
-
r
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
free energy profiles for the enzymatic reaction suggest that enzyme primarily acts in D-mannitol oxidation
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?, r
D-mannitol + NAD+
D-fructose + NADH + H+
Fomes pinicola
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
Lactobacillus gayonii
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
Lactobacillus gayonii
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
Lactobacillus pentoaceticus
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
Lactobacillus pentoaceticus
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
enzyme highly specific for D-mannitol and D-fructose
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
enzyme highly specific for D-mannitol and D-fructose
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
Nocardia erythropolis
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
the epsilon-NH2 group of Lys295 participates in an obligatory pH-dependent, pre-catalytic equilibrium which may control alcohol/alkoxide equilibration of the enzyme-bound D-mannitol and activates the C2 atom for subsequent catalytic oxidation by NAD+
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
wild-type enzyme
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
Sarcina aurantiaca
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
Sarcina marginata
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
100% activity
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
100% activity
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-mannitol + NADP+
D-fructose + NADPH + H+
M2DH is a much poorer enzyme when it employes NADP+ and NADPH as compared to NAD+ and NADH
-
-
r
D-mannitol + NADP+
D-fructose + NADPH + H+
32% of the activity with NAD+
-
-
?
L-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
r
L-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
L-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
L-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
L-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
L-sorbose + NADH + H+
L-sorbitol + NAD+
-
-
-
r
L-sorbose + NADH + H+
L-sorbitol + NAD+
5% relative activity on L-sorbose compared to 100% activity on D-fructose
-
-
?
L-sorbose + NADH + H+
L-sorbitol + NAD+
5% activity compared to D-fructose
-
-
r
L-sorbose + NADH + H+
L-sorbitol + NAD+
5% activity compared to D-fructose
-
-
r
L-sorbose + NADH + H+
L-sorbitol + NAD+
5% activity compared to D-fructose
-
-
r
L-sorbose + NADH + H+
L-sorbitol + NAD+
5% activity compared to D-fructose
-
-
r
L-sorbose + NADH + H+
L-sorbitol + NAD+
5% activity compared to D-fructose
-
-
r
additional information
?
-
a D-arabo configuration is required for a polyol substrate to become reactive. The C2 (R) configuration as in mannitol is preferred over the C2 (S) configuration as in D-sorbitol
-
-
?
additional information
?
-
-
slightly active with sorbitol, no activity with ribitol, arabinitol, or mesoerythritol
-
-
?
additional information
?
-
-
among the Escherichia coli strains, BL21 (DE3) plysS exhibits the maximum expression level of MDH (11mg/L)
-
-
?
additional information
?
-
no activity with glycerol, 1, 2-hexanediol, and 1,2,3-hexanetriol
-
-
?
additional information
?
-
-
no activity with glycerol, 1, 2-hexanediol, and 1,2,3-hexanetriol
-
-
?
additional information
?
-
-
no activity with NADP+ and NADPH
-
-
?
additional information
?
-
-
no activity with NADP+ and NADPH
-
-
?
additional information
?
-
mannitol can be produced directly from glucose in a two-step enzymatic process, using a Thermotoga neapolitana xylose isomerase mutant and TmMtDH at 60°C. No activity with glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
-
-
?
additional information
?
-
-
mannitol can be produced directly from glucose in a two-step enzymatic process, using a Thermotoga neapolitana xylose isomerase mutant and TmMtDH at 60°C. No activity with glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
-
-
?
additional information
?
-
TM0298 shows no detectable activity on glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
-
-
?
additional information
?
-
-
TM0298 shows no detectable activity on glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
-
-
?
additional information
?
-
No activity with glucose, arabinose, xylose, acetaldehyde, and 2-butanone
-
-
-
additional information
?
-
No activity with glucose, arabinose, xylose, acetaldehyde, and 2-butanone
-
-
-
additional information
?
-
No activity with glucose, arabinose, xylose, acetaldehyde, and 2-butanone
-
-
-
additional information
?
-
No activity with glucose, arabinose, xylose, acetaldehyde, and 2-butanone
-
-
-
additional information
?
-
mannitol can be produced directly from glucose in a two-step enzymatic process, using a Thermotoga neapolitana xylose isomerase mutant and TmMtDH at 60°C. No activity with glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
-
-
?
additional information
?
-
TM0298 shows no detectable activity on glucose, xylose, threonine, arabinose, acetaldehyde, 2-butanone, sorbitol, xylitol, ethanol, or 2-butanol
-
-
?
additional information
?
-
No activity with glucose, arabinose, xylose, acetaldehyde, and 2-butanone
-
-
-
additional information
?
-
-
the enzyme shows no activity with xylitol, inositol, sorbitol, rhamnose, mannose and xylose, and with NADPH and NADP+ as cofactors
-
-
?
additional information
?
-
-
no activity with sorbitol, xylitol, mannose, rhamnose, and xylose. The enzyme from Thermotoga neapolitana is dependent on NADH
-
-
-
additional information
?
-
-
the enzyme shows no activity with xylitol, inositol, sorbitol, rhamnose, mannose and xylose, and with NADPH and NADP+ as cofactors
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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58.5
D-sorbitol
-
recombinant protein
1.7
D-xylulose
pH 7.1, 25°C
680
L-sorbitol
pH 10.0, 25°C
0.1
polyethyleneglycol-NH-succinyl-aminoethyl-NADH
-
-
-
0.125
polyethyleneglycol-NH-succinyl-NADH
-
-
-
0.074
polyethylenimine-NH-succinyl-NADH
-
-
-
additional information
additional information
-
1.8 - 6.5
D-arabinitol
-
-
163
D-arabinitol
pH 10.0, 25°C
1.6
D-arabitol
-
recombinant protein
20.36
D-arabitol
mutant enzyme D230A, at pH 7.4 and 25°C
33.15
D-arabitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
55.85
D-arabitol
wild type enzyme, at pH 7.4 and 25°C
94.82
D-arabitol
mutant enzyme N300D, at pH 7.4 and 25°C
125.5
D-arabitol
mutant enzyme N191A, at pH 7.4 and 25°C
126.5
D-arabitol
mutant enzyme N300S, at pH 7.4 and 25°C
126.9
D-arabitol
mutant enzyme E133Q, at pH 7.4 and 25°C
132.1
D-arabitol
mutant enzyme N300A, at pH 7.4 and 25°C
134.1
D-arabitol
mutant enzyme E133A, at pH 7.4 and 25°C
144.5
D-arabitol
mutant enzyme R373A, at pH 7.4 and 25°C
145.1
D-arabitol
mutant enzyme H303A, at pH 7.4 and 25°C
176.9
D-arabitol
mutant enzyme K381A, at pH 7.4 and 25°C
0.037
D-fructose
pH 6.1, 60°C
0.048
D-fructose
pH 6.1, 80°C
0.24
D-fructose
wild-type, pH 7.1, 25°C
0.24
D-fructose
wild-type, pH 7.1, temperature not specified in the publication
0.44
D-fructose
-
in 50 mM glycine/NaOH buffer at pH 10.0
0.54
D-fructose
mutant N191D, pH 10.0, temperature not specified in the publication
0.6
D-fructose
pH 7.1, 25°C
1.1
D-fructose
mutant N191L, pH 7.1, 25°C
3.9
D-fructose
mutant N300D, pH 10.0, temperature not specified in the publication
6
D-fructose
mutant N191D, pH 7.1, temperature not specified in the publication
9
D-fructose
mutant N191A, pH 7.1, 25°C
16.3 - 79.2
D-fructose
-
-
16.3 - 79.2
D-fructose
-
-
16.3 - 79.2
D-fructose
-
-
16.3 - 79.2
D-fructose
-
-
16.3 - 79.2
D-fructose
-
-
16.3 - 79.2
D-fructose
-
-
20
D-fructose
mutant N191A/N300A, pH 7.1, 25°C
20
D-fructose
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
20
D-fructose
-
pH 6.5, 90°C
20
D-fructose
-
at pH 6.5 and 90°C
22
D-fructose
mutant N300D, pH 6.8, temperature not specified in the publication
24
D-fructose
-
25°C, pH 7.3
25
D-fructose
-
recombinant protein
44
D-fructose
pH 5.4, 30°C
50
D-fructose
at 60°C and pH 6.1
50
D-fructose
at 60°C, pH 6.1
50.97
D-fructose
at 80°C and pH 6.1
50.97
D-fructose
at 80°C, pH 6.1
60
D-fructose
at 25°C, in 100 mM Tris/HCl buffer, pH 7.1
0.29 - 21.8
D-mannitol
-
-
0.29 - 21.8
D-mannitol
-
-
0.29 - 21.8
D-mannitol
-
-
0.29 - 21.8
D-mannitol
-
-
0.29 - 21.8
D-mannitol
-
-
0.29 - 21.8
D-mannitol
-
-
0.29 - 21.8
D-mannitol
-
-
0.29 - 21.8
D-mannitol
-
-
0.3
D-mannitol
mutant N300D, pH 10.0, temperature not specified in the publication
0.32
D-mannitol
mutant N191D, pH 10.0, temperature not specified in the publication
0.4
D-mannitol
-
in 50 mM glycine/NaOH buffer at pH 10.0
0.4
D-mannitol
wild-type, pH 10.0, 25°C
0.6
D-mannitol
-
recombinant protein
0.9
D-mannitol
mutant N191L, pH 10.0, 25°C
1.2
D-mannitol
-
recombinant protein
4.56
D-mannitol
mutant enzyme N191A, at pH 7.4 and 25°C
5.51
D-mannitol
at 80°C and pH 8.3
5.51
D-mannitol
at 80°C, pH 8.3
5.98
D-mannitol
wild type enzyme, at pH 7.4 and 25°C
8.15
D-mannitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
8.7
D-mannitol
mutant N191A, pH 10.0, 25°C
9
D-mannitol
mutant N191D, pH 7.1, temperature not specified in the publication
9.1
D-mannitol
-
25°C, pH 9.0
12
D-mannitol
pH 8.6, 30°C
13
D-mannitol
pH 10.0, 25°C
13
D-mannitol
at 25°C, in 100 mM glycine/NaOH buffer pH 10.0
13.23
D-mannitol
at 60°C and pH 6.1
13.23
D-mannitol
at 60°C, pH 6.1
14.96
D-mannitol
mutant enzyme E133Q, at pH 7.4 and 25°C
15.4
D-mannitol
-
41°C, pH 9.0
17.49
D-mannitol
mutant enzyme R373A, at pH 7.4 and 25°C
18.21
D-mannitol
mutant enzyme E133A, at pH 7.4 and 25°C
20.42
D-mannitol
mutant enzyme N300D, at pH 7.4 and 25°C
21
D-mannitol
wild-type, pH 7.1, temperature not specified in the publication
23.89
D-mannitol
mutant enzyme K381A, at pH 7.4 and 25°C
42.74
D-mannitol
mutant enzyme D230A, at pH 7.4 and 25°C
49.95
D-mannitol
mutant enzyme N300S, at pH 7.4 and 25°C
68.94
D-mannitol
mutant enzyme N300A, at pH 7.4 and 25°C
93
D-mannitol
mutant N300D, pH 6.8, temperature not specified in the publication
93.85
D-mannitol
mutant enzyme H303A, at pH 7.4 and 25°C
1187
D-mannitol
mutant N191A/N300A, pH 10.0, 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme E133A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme E133Q, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme H303A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme N191A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme N300A, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, mutant enzyme N300S, at pH 7.4 and 25°C
1800
meso-erythritol
Km far above 1800 mM, wild type enzyme, at pH 7.4 and 25°C
0.001
NAD+
mutant N300D, pH 6.8, temperature not specified in the publication
0.054
NAD+
mutant N191D, pH 10.0, temperature not specified in the publication
0.055
NAD+
mutant N191L, pH 10.0, 25°C
0.074
NAD+
mutant N300D, pH 10.0, temperature not specified in the publication
0.093
NAD+
-
in 50 mM glycine/NaOH buffer at pH 10.0
0.093
NAD+
wild-type, pH 10.0, 25°C
0.14
NAD+
at 80°C and pH 8.3
0.14
NAD+
at 80°C, pH 8.3
0.15
NAD+
at 25°C, in 100 mM glycine/NaOH buffer pH 10.0
0.231
NAD+
mutant N191D, pH 7.1, temperature not specified in the publication
0.31
NAD+
mutant N191A, pH 10.0, 25°C
0.314
NAD+
mutant N191A/N300A, pH 10.0, 25°C
0.775
NAD+
wild-type, pH 7.1, temperature not specified in the publication
0.0033
NADH
mutant N191L, pH 7.1, 25°C
0.008
NADH
mutant N191D, pH 7.1, temperature not specified in the publication
0.009
NADH
mutant N300D, pH 10.0, temperature not specified in the publication
0.01
NADH
-
in 50 mM glycine/NaOH buffer at pH 10.0
0.011
NADH
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
0.016
NADH
mutant N191D, pH 10.0, temperature not specified in the publication
0.017
NADH
mutant N191A, pH 7.1, 25°C
0.019
NADH
at 25°C, in 100 mM Tris/HCl buffer, pH 7.1
0.02
NADH
mutant N300D, pH 6.8, temperature not specified in the publication
0.023
NADH
mutant N191A/N300A, pH 7.1, 25°C
0.037
NADH
at 60°C and pH 6.1
0.037
NADH
at 60°C, pH 6.1
0.048
NADH
at 80°C and pH 6.1
0.048
NADH
at 80°C, pH 6.1
0.067
NADH
wild-type, pH 7.1, 25°C
0.067
NADH
wild-type, pH 7.1, temperature not specified in the publication
0.15
NADH
-
recombinant protein
7.5
NADP+
at 80°C and pH 8.3
7.5
NADP+
at 80°C, pH 8.3
0.17
NADPH
at 80°C and pH 6.1
0.17
NADPH
at 80°C, pH 6.1
additional information
additional information
kinetic modeling
-
additional information
additional information
steady-state kinetic analysis, recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetic analysis, recombinant wild-type and mutant enzymes, overview
-
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0.99
D-arabinitol
pH 10.0, 25°C
0.000014 - 0.118
D-arabitol
0.000026 - 250
D-fructose
0.000015 - 100
D-mannitol
39
D-xylulose
pH 7.1, 25°C
0.088
L-sorbitol
pH 10.0, 25°C
1.1
L-sorbose
pH 7.1, 25°C
0.0000021 - 0.0018
meso-erythritol
0.000014
D-arabitol
mutant enzyme N300D, at pH 7.4 and 25°C
0.000051
D-arabitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.00014
D-arabitol
mutant enzyme D230A, at pH 7.4 and 25°C
0.00024
D-arabitol
mutant enzyme R373A, at pH 7.4 and 25°C
0.00035
D-arabitol
mutant enzyme N191A, at pH 7.4 and 25°C
0.00047
D-arabitol
mutant enzyme N300S, at pH 7.4 and 25°C
0.00069
D-arabitol
mutant enzyme N300A, at pH 7.4 and 25°C
0.002
D-arabitol
mutant enzyme H303A, at pH 7.4 and 25°C
0.00206
D-arabitol
mutant enzyme K381A, at pH 7.4 and 25°C
0.04332
D-arabitol
mutant enzyme E133Q, at pH 7.4 and 25°C
0.05448
D-arabitol
mutant enzyme E133A, at pH 7.4 and 25°C
0.118
D-arabitol
wild type enzyme, at pH 7.4 and 25°C
0.000026
D-fructose
mutant N191A/N300A, pH 7.1, 25°C
0.0074
D-fructose
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
0.041
D-fructose
mutant N300D, pH 6.8, temperature not specified in the publication
0.064
D-fructose
mutant N191A, pH 7.1, 25°C
0.205
D-fructose
mutant N300D, pH 10.0, temperature not specified in the publication
0.407
D-fructose
mutant N191L, pH 7.1, 25°C
0.45
D-fructose
mutant N191D, pH 7.1, temperature not specified in the publication
0.45
D-fructose
-
pH 6.5, 90°C
9
D-fructose
-
at pH 6.5 and 90°C
15
D-fructose
mutant N191D, pH 10.0, temperature not specified in the publication
140
D-fructose
pH 7.1, 25°C
250
D-fructose
wild-type, pH 7.1, 25°C
250
D-fructose
wild-type, pH 7.1, temperature not specified in the publication
0.000015
D-mannitol
mutant N300D, pH 6.8, temperature not specified in the publication
0.000034
D-mannitol
mutant N191A/N300A, pH 10.0, 25°C
0.00004
D-mannitol
mutant enzyme N300D, at pH 7.4 and 25°C
0.000061
D-mannitol
mutant N191D, pH 7.1, temperature not specified in the publication
0.00016
D-mannitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.00102
D-mannitol
mutant enzyme R373A, at pH 7.4 and 25°C
0.00192
D-mannitol
mutant enzyme N300S, at pH 7.4 and 25°C
0.00311
D-mannitol
mutant enzyme N300A, at pH 7.4 and 25°C
0.0034
D-mannitol
mutant N191D, pH 10.0, temperature not specified in the publication
0.00458
D-mannitol
mutant enzyme N191A, at pH 7.4 and 25°C
0.0049
D-mannitol
mutant N300D, pH 10.0, temperature not specified in the publication
0.00522
D-mannitol
mutant enzyme H303A, at pH 7.4 and 25°C
0.00775
D-mannitol
mutant enzyme K381A, at pH 7.4 and 25°C
0.00908
D-mannitol
mutant enzyme D230A, at pH 7.4 and 25°C
0.215
D-mannitol
mutant enzyme E133Q, at pH 7.4 and 25°C
0.219
D-mannitol
mutant enzyme E133A, at pH 7.4 and 25°C
0.319
D-mannitol
mutant N191A, pH 10.0, 25°C
0.598
D-mannitol
mutant N191L, pH 10.0, 25°C
0.734
D-mannitol
wild type enzyme, at pH 7.4 and 25°C
0.757
D-mannitol
wild-type, pH 7.1, temperature not specified in the publication
17
D-mannitol
pH 10.0, 25°C
100
D-mannitol
wild-type, pH 10.0, 25°C
0.0000021
meso-erythritol
mutant enzyme N191A, at pH 7.4 and 25°C
0.0000044
meso-erythritol
mutant enzyme N300S, at pH 7.4 and 25°C
0.0000065
meso-erythritol
mutant enzyme N300A, at pH 7.4 and 25°C
0.000029
meso-erythritol
mutant enzyme H303A, at pH 7.4 and 25°C
0.00088
meso-erythritol
mutant enzyme E133Q, at pH 7.4 and 25°C
0.00097
meso-erythritol
mutant enzyme E133A, at pH 7.4 and 25°C
0.0018
meso-erythritol
wild type enzyme, at pH 7.4 and 25°C
0.0024
NAD+
mutant N191D, pH 7.1, temperature not specified in the publication
0.02
NAD+
mutant N191D, pH 10.0, temperature not specified in the publication
0.02
NAD+
mutant N300D, pH 10.0, temperature not specified in the publication
0.127
NAD+
mutant N191A/N300A, pH 10.0, 25°C
1.4
NAD+
mutant N300D, pH 6.8, temperature not specified in the publication
8.968
NAD+
mutant N191A, pH 10.0, 25°C
9.964
NAD+
mutant N191L, pH 10.0, 25°C
20
NAD+
wild-type, pH 7.1, temperature not specified in the publication
400
NAD+
wild-type, pH 10.0, 25°C
0.019
NADH
mutant N191A/N300A, pH 7.1, 25°C
15
NADH
mutant N191D/N300D, pH 10.0, temperature not specified in the publication
32
NADH
mutant N191A, pH 7.1, 25°C
45
NADH
mutant N300D, pH 6.8, temperature not specified in the publication
89
NADH
mutant N300D, pH 10.0, temperature not specified in the publication
170
NADH
mutant N191L, pH 7.1, 25°C
340
NADH
mutant N191D, pH 7.1, temperature not specified in the publication
510
NADH
mutant N191D, pH 10.0, temperature not specified in the publication
910
NADH
wild-type, pH 7.1, 25°C
910
NADH
wild-type, pH 7.1, temperature not specified in the publication
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D230A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E133Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E292A
mutation partially disrupts the catalytic cycle. Role for residue Glu292 as a gate in a water chain mechanism of proton translocation. Removal of gatekeeper control in the E292A mutant results in a selective, up to 120fold slowing down of microscopicsteps immediately preceding catalytic oxidation of mannitol, consistent with the notion that formation of the productive enzyme-NAD-mannitol complex is promoted by a corresponding position change of Glu292
E68K
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is preferred by 10fold over NAD(H)
E68K/D69A
shows about a 10fold preference for NADP(H) over NAD(H), accompanied by a small decrease in catalytic efficiency for NAD(H)-dependent reactions as compared to wild-type enzyme
H303A/R373A/K381A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
K295M
-
2000000fold lower turnover number for D-mannitol oxidation at pH 10.0 than the wild-type enzyme
K381A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
N191A/N300A
the rate constants for the overall hydride transfer to and from C-2 of mannitol are selectively slowed, with additive effects in the double mutant
N191D
the internal equilibrium of enzyme-NADH-fructose and enzyme-NAD+-mannitol is altered 10000- to 100000fold from being balanced in the wild-type enzyme to favoring enzyme-NAD+-mannitol in the single site mutants, N191D and N300D. N191D and N300D appear to lose fructose binding affinity due to deprotonation of the respective Asp above apparent pK values of 5.3 0.1 and 6.3 0.2, respectively
N191D/N300D
mutant behaves as a slow fructose reductase at pH 5.2, lacking measurable activity for mannitol oxidation in the pH range 6.8-10
N191L
the rate constants for the overall hydride transfer to and from C-2 of mannitol are selectively slowed, between 540- and 2700fold. Partial disruption of the oxyanion hole in the single-site mutant causes an upshift, by about 1.2 pH units, in the kinetic pK of the catalytic acid-base Lys295 in the enzymeNAD+-mannitol complex
N300S
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R373A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D69A
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is equally utilized as NAD(H)
D69A
utilizes NAD(H) and NADP(H) with similar catalytic efficiencies. Uses NADP(H) almost as well as wild-type enzyme uses NAD(H)
H303A
-
mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 300fold below the wild-type value
H303A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
K295A
inactive
K295A
-
30000fold lower turnover number for D-mannitol oxidation at pH 10.0 than the wild-type enzyme
K295A
-
mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 400000fold below the wild-type value
N191A
the rate constants for the overall hydride transfer to and from C-2 of mannitol are selectively slowed, between 540- and 2700fold. Partial disruption of the oxyanion hole in the single-site mutant causes an upshift, by about 1.2 pH units, in the kinetic pK of the catalytic acid-base Lys295 in the enzymeNAD+-mannitol complex
N191A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
N300A
-
mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 1000fold below the wild-type value
N300A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
N300D
the internal equilibrium of enzyme-NADH-fructose and enzyme-NAD+-mannitol is altered 10000- to 100000fold from being balanced in the wild-type enzyme to favoring enzyme-NAD+-mannitol in the single site mutants, N191D and N300D. N191D and N300D appear to lose fructose binding affinity due to deprotonation of the respective Asp above apparent pK values of 5.3 0.1 and 6.3 0.2, respectively
N300D
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
additional information
D-mannitol production by resting state whole cell biotransformation of D-fructose by heterologous mannitol dehydrogenase gene from Leuconostoc pseudomesenteroides and the formate dehydrogenase gene, gene fdh from Mycobacterium vaccae N10, expression in Bacillus megaterium, development of an in vivo system, overview
additional information
-
D-mannitol production by resting state whole cell biotransformation of D-fructose by heterologous mannitol dehydrogenase gene from Leuconostoc pseudomesenteroides and the formate dehydrogenase gene, gene fdh from Mycobacterium vaccae N10, expression in Bacillus megaterium, development of an in vivo system, overview
-
additional information
application of a modular screening procedure that can identify the optimal operating policy of an enzymatic reactor, which minimizes the enzyme consumption, given the process kinetic model, and an imposed production capacity. Following an optimization procedure, the process effectiveness is evaluated in a systematic approach, by including simple batch reactor (BR), batch with intermittent addition of the key-enzyme following certain optimal policies (BRP). The enzymatic reduction of D-fructose to mannitol is used as a model system utilizing suspended MDH (mannitol dehydrogenase) and NADH (nicotinamide adenine dinucleotide) cofactor, with the in-situ continuous regeneration of the cofactor by the expense of formate degradation in the presence of suspended FDH (formate dehydrogenase). The NADH-dependent FDH and MDH typical activity in D-fructose reduction is of 1-2 U/ml in a batch reactor
additional information
-
application of a modular screening procedure that can identify the optimal operating policy of an enzymatic reactor, which minimizes the enzyme consumption, given the process kinetic model, and an imposed production capacity. Following an optimization procedure, the process effectiveness is evaluated in a systematic approach, by including simple batch reactor (BR), batch with intermittent addition of the key-enzyme following certain optimal policies (BRP). The enzymatic reduction of D-fructose to mannitol is used as a model system utilizing suspended MDH (mannitol dehydrogenase) and NADH (nicotinamide adenine dinucleotide) cofactor, with the in-situ continuous regeneration of the cofactor by the expense of formate degradation in the presence of suspended FDH (formate dehydrogenase). The NADH-dependent FDH and MDH typical activity in D-fructose reduction is of 1-2 U/ml in a batch reactor
-
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analysis
-
sensitive and specific photometric determination of mannitol in human serum
biotechnology
recombinant Escherichia coli expressing the enzyme from Leuconostoc pseudomesenteroides expressing strong catalytic activity of an NADH-dependent reduction of D-fructose to D-mannitol in cell extracts of the recombinant Escherichia coli strain can be utilized as an efficient biocatalyst for D-mannitol formation
industry
-
best strain for expression of MDH in both laboratory and industrial applications is Escherichia coli BL21 (DE3) plysS
industry
redox balancing between the intracellular NADP(H) and NAD(H) based on NAD(P)(H)-dependent interconversion of mannitol and fructose by M2DH may be a useful strategy of metabolic engineering
industry
the enzyme synthesizes D-mannitol is commonly known as a sweetener in food manufacturing such as juices, soft drinks, cakes, and sweet cookies, moreover, other processing including alternative sugar for diabetic patients, cosmetics, personal hygiene products, and laxative. D-mannitol is 50% as sweet as sucrose
industry
-
the enzyme synthesizes D-mannitol is commonly known as a sweetener in food manufacturing such as juices, soft drinks, cakes, and sweet cookies, moreover, other processing including alternative sugar for diabetic patients, cosmetics, personal hygiene products, and laxative. D-mannitol is 50% as sweet as sucrose
-
industry
-
the enzyme synthesizes D-mannitol is commonly known as a sweetener in food manufacturing such as juices, soft drinks, cakes, and sweet cookies, moreover, other processing including alternative sugar for diabetic patients, cosmetics, personal hygiene products, and laxative. D-mannitol is 50% as sweet as sucrose
-
industry
-
the enzyme synthesizes D-mannitol is commonly known as a sweetener in food manufacturing such as juices, soft drinks, cakes, and sweet cookies, moreover, other processing including alternative sugar for diabetic patients, cosmetics, personal hygiene products, and laxative. D-mannitol is 50% as sweet as sucrose
-
industry
-
the enzyme synthesizes D-mannitol is commonly known as a sweetener in food manufacturing such as juices, soft drinks, cakes, and sweet cookies, moreover, other processing including alternative sugar for diabetic patients, cosmetics, personal hygiene products, and laxative. D-mannitol is 50% as sweet as sucrose
-
nutrition
-
-
nutrition
-
cofactor regeneration system
synthesis
the recombinant enzyme expressed in Bacillus megaterium is useful in production of D-mannitol using a resting cell biotransformation approach
synthesis
-
an effective strategy for producing high yields of mannitol is developed. The combined strategies of aeration induction and redox modulation significantly increases the glucose consumption rate, intracellular NADH level and the specific activity of mannitol dehydrogenase (MDH), resulting in an increase in mannitol production from 64.6 to 88.1 g/l with the yield increased from 0.69 to 0.94 g/g
synthesis
mannitol is a natural hexitol with important applications in medicine and food industry. Development of a production method on an industrial scale, optimization and evaluation of production in a batch reactor (BR, or BRP operation) for a complex bi-enzymatic system with suspended enzymes and cofactor regeneration, method modeling, molecular calculations and simulations, detailed overview
synthesis
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga maritima involves production from glucose via Thermotoga neapolitana xylose isomerase (gene xylA, UniProt ID P45687) followed by the conversion of the formed D-fructose using Thermotoga maritima MtDH of enzymatic to chemical synthesis process, overview
synthesis
-
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga neapolitana is via D-fructose in a single step procedure. Comparison of enzymatic to chemical synthesis process, overview
synthesis
-
an effective strategy for producing high yields of mannitol is developed. The combined strategies of aeration induction and redox modulation significantly increases the glucose consumption rate, intracellular NADH level and the specific activity of mannitol dehydrogenase (MDH), resulting in an increase in mannitol production from 64.6 to 88.1 g/l with the yield increased from 0.69 to 0.94 g/g
-
synthesis
-
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga maritima involves production from glucose via Thermotoga neapolitana xylose isomerase (gene xylA, UniProt ID P45687) followed by the conversion of the formed D-fructose using Thermotoga maritima MtDH of enzymatic to chemical synthesis process, overview
-
synthesis
-
the recombinant enzyme expressed in Bacillus megaterium is useful in production of D-mannitol using a resting cell biotransformation approach
-
synthesis
-
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga maritima involves production from glucose via Thermotoga neapolitana xylose isomerase (gene xylA, UniProt ID P45687) followed by the conversion of the formed D-fructose using Thermotoga maritima MtDH of enzymatic to chemical synthesis process, overview
-
synthesis
-
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga maritima involves production from glucose via Thermotoga neapolitana xylose isomerase (gene xylA, UniProt ID P45687) followed by the conversion of the formed D-fructose using Thermotoga maritima MtDH of enzymatic to chemical synthesis process, overview
-
synthesis
-
the enzyme might be useful for enzymatic D-mannitol production in an industrial scale. The purified mannitol dehydrogenase have been reported to produce D-mannitol with no sorbitol formation at temperatures of 90-120°C. The pathway for D-mannitol production using MtDH isolated from Thermotoga maritima involves production from glucose via Thermotoga neapolitana xylose isomerase (gene xylA, UniProt ID P45687) followed by the conversion of the formed D-fructose using Thermotoga maritima MtDH of enzymatic to chemical synthesis process, overview
-
synthesis
-
mannitol is a natural hexitol with important applications in medicine and food industry. Development of a production method on an industrial scale, optimization and evaluation of production in a batch reactor (BR, or BRP operation) for a complex bi-enzymatic system with suspended enzymes and cofactor regeneration, method modeling, molecular calculations and simulations, detailed overview
-
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Leuconostoc mesenteroides
-
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Mannitol oxidation in two Micromonospora isolates and in representative species of other actinomycetes
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1977
Gluconobacter oxydans, Streptomyces lavendulae, Actinoplanes missouriensis, Levilactobacillus brevis, Mycolicibacterium smegmatis, Nocardia erythropolis, Sinorhizobium meliloti
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Some features of mannitol metabolism in Rhizobium japonicum
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Bradyrhizobium japonicum
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D-Mannitol dehydrogenase from Absidia glauca. Steady-state kinetic properties and the inhibitory role of mannitol 1-phosphate
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1977
Absidia glauca
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Ueng, S.T.H.; Hartanowicz, P.; Lewandowski, C.; Keller, J.; M.Holick, E.T.McGuinness
D-Mannitol dehydrogenase from Absidia glauca. Purification, metabolic role, and subunit interactions
Biochemistry
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1976
Absidia glauca
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Yamanaka, K.
D-Mannitol dehydrogenase from Leuconostoc mesenteroides
Methods Enzymol.
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138-142
1975
Leuconostoc mesenteroides, Levilactobacillus brevis, Lactobacillus gayonii, Lactobacillus pentoaceticus
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Yamanaka, K.; Sakai, S.
Production of polyol dehydrogenases in bacteria
Can. J. Microbiol.
14
391-396
1968
Leuconostoc mesenteroides, Levilactobacillus brevis, Lactobacillus gayonii, Lactobacillus pentoaceticus, Pseudomonas aeruginosa, Pseudomonas coronafaciens, Pseudomonas fluorescens, Sarcina aurantiaca, Sarcina marginata
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Sakai, S.; Yamanaka, K.
Crystalline D-mannitol:NAD oxidoreductase from Leuconostoc mesenteroides: Part II. substrate and coenzyme specificity
Agric. Biol. Chem.
32
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1968
Leuconostoc mesenteroides, no activity in Lactobacillus plantarum
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Sakai, S.; Yamanaka, K.
Crystalline D-mannitol:NAD+ oxidoreductase from Leuconostoc mesenteroides
Biochim. Biophys. Acta
151
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1968
Leuconostoc mesenteroides
brenda
Horecker, B.L.
Mannitol dehydrogenase (crystalline) from Lactobacillus brevis
Methods Enzymol.
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1966
Levilactobacillus brevis
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Martinez, G.; Barker, H.A.; Horecker, B.L.
A specific mannitol dehydrogenase from Lactobacillus brevis
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1963
Levilactobacillus brevis
-
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Schafer, A.; Stein, M.A.; Schneider, K.H.; Giffhorn, F.
Mannitol dehydrogenase from Rhodobacter sphaeroides Si4: subcloning, overexpression in Escherichia coli and characterization of the recombinant enzyme
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48
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1997
Cereibacter sphaeroides
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Slatner, M.; Nagl, G.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.
Enzymic synthesis of mannitol: reaction engineering for a recombinant mannitol dehydrogenase
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864
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1998
Pseudomonas fluorescens
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Slatner, M.; Nidetzky, B.; Kulbe, K.D.
Kinetic study of the catalytic mechanism of mannitol dehydrogenase from Pseudomonas fluorescens
Biochemistry
38
10489-10498
1999
Pseudomonas fluorescens
brenda
Brunker, P.; Altenbuchner, J.; Kulbe, K.D.; Mattes, R.
Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli
Biochim. Biophys. Acta
1351
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1997
Pseudomonas fluorescens
brenda
Aarnikunnas, J.; Ronnholm, K.; Palva, A.
The mannitol dehydrogenase gene (mdh) from Leuconostoc mesenteroides is distinct from other known bacterial mdh genes
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59
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2002
Leuconostoc mesenteroides (Q8KQG6), Leuconostoc mesenteroides ATCC -9135 (Q8KQG6)
brenda
Kaup, B.; Bringer-Meyer, S.; Sahm, H.
Metabolic engineering of Escherichia coli: construction of an efficient biocatalyst for D-mannitol formation in a whole-cell biotransformation
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64
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Leuconostoc pseudomesenteroides (Q83VI5)
brenda
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A zinc-containing mannitol-2-dehydrogenase from Leuconostoc pseudomesenteroides ATCC 12291: purification of the enzyme and cloning of the gene
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179
101-107
2003
Leuconostoc pseudomesenteroides (Q83VI5)
brenda
Klimacek, M.; Nidetzky, B.
A catalytic consensus motif for D-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens
Biochem. J.
367
13-18
2002
Pseudomonas fluorescens
brenda
Klimacek, M.; Kavanagh, K.L.; Wilson, D.K.; Nidetzky, B.
On the role of Bronsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase
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375
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2003
Pseudomonas fluorescens
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Kavanagh, K.L.; Klimacek, M.; Nidetzky, B.; Wilson, D.K.
Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase: evidence for a very divergent long-chain dehydrogenase family
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143-144
551-558
2003
Pseudomonas fluorescens
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Graefe, H.; Gutschow, B.; Gehring, H.; Dibbelt, L.
Sensitive and specific photometric determination of mannitol in human serum
Clin. Chem. Lab. Med.
41
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2003
Leuconostoc mesenteroides
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Purification and characterisation of mannitol dehydrogenase from Lactobacillus sanfranciscensis
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220
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2003
Fructilactobacillus sanfranciscensis
brenda
Kavanagh, K.L.; Klimacek, M.; Nidetzky, B.; Wilson, D.K.
Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism
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277
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2002
Pseudomonas fluorescens
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Cloning, expression, purification, and analysis of mannitol dehydrogenase gene mtlK from Lactobacillus brevis
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2005
Levilactobacillus brevis
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Enzymatic production of D-mannitol with the Leuconostoc pseudomesenteroides mannitol dehydrogenase coupled to a coenzyme regeneration system
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23
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2005
Leuconostoc pseudomesenteroides
-
brenda
Klimacek, M.; Nidetzky, B.
Examining the relative timing of hydrogen abstraction steps during NAD+-dependent oxidation of secondary alcohols catalyzed by long-chain D-mannitol dehydrogenase from Pseudomonas fluorescens using pH and kinetic isotope effects
Biochemistry
41
10158-10165
2002
Pseudomonas fluorescens
brenda
Parmentier, S.; Beauprez, J.; Arnaut, F.; Soetaert, W.; Vandamme, E.J.
Gluconobacter oxydans NAD-dependent, D-fructose reducing, polyol dehydrogenases activity: screening, medium optimisation and application for enzymatic polyol production
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27
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2005
Gluconobacter oxydans, Gluconobacter oxydans LMG 1489
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Saccharomyces cerevisiae
-
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Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase
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63
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2007
Thermotoga maritima
brenda
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2
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2007
Leuconostoc pseudomesenteroides (Q83VI5), Leuconostoc pseudomesenteroides ATCC 12291 (Q83VI5)
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Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
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Thermotoga maritima TM0298 is a highly thermostable mannitol dehydrogenase
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Limosilactobacillus reuteri (Q6ECH5), Thermotoga maritima (Q9WYD4), Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 (Q9WYD4)
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Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase
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Aspergillus fumigatus (Q4WQY4), Aspergillus fumigatus
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11
2001-2006
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Pseudomonas fluorescens
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Klimacek, M.; Nidetzky, B.
The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites
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425
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Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
brenda
Klimacek, M.; Nidetzky, B.
From alcohol dehydrogenase to a "one-way" carbonyl reductase by active-site redesign: a mechanistic study of mannitol 2-dehydrogenase from Pseudomonas fluorescens
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285
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2010
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
brenda
Krahulec, S.; Armao, G.C.; Klimacek, M.; Nidetzky, B.
Enzymes of mannitol metabolism in the human pathogenic fungus Aspergillus fumigatus--kinetic properties of mannitol-1-phosphate 5-dehydrogenase and mannitol 2-dehydrogenase, and their physiological implications
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278
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Aspergillus fumigatus (Q4WQY4)
brenda
Klimacek, M.; Brunsteiner, M.; Nidetzky, B.
Dynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent
J. Biol. Chem.
287
6655-6667
2012
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
brenda
Koko, M.; Hassanin, H.; Letsididi, R.; Zhang, T.; Mu, W.
Characterization of a thermostable mannitol dehydrogenase from hyperthermophilic Thermotoga neapolitana DSM 4359 with potential application in mannitol production
J. Mol. Catal. B
134
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2016
Thermotoga neapolitana, Thermotoga neapolitana DSM 4359
-
brenda
Jang, M.; Park, J.; Kim, M.; Lee, S.; Kang, J.; Kim, T.
Molecular cloning and gene expression of Sinorhizobium meliloti mannitol dehydrogenase in Escherichia coli, and its enzymatic characterization
Korean J. Microbiol. Biotechnol.
41
153-159
2013
Sinorhizobium meliloti, Sinorhizobium meliloti KCTC 2353
-
brenda
Shao, Z.; Zhang, P.; Li, Q.; Wang, X.; Duan, D.
Characterization of mannitol-2-dehydrogenase in Saccharina japonica: evidence for a new polyol-specific long-chain dehydrogenases/reductase
PLoS ONE
9
e97935
2014
Saccharina japonica (R9UHL6), Saccharina japonica
brenda
Lucas, J.; Siegel, J.
Erratum: Quantitative functional characterization of conserved molecular interactions in the active site of mannitol 2-dehydrogenase
Protein Sci.
24
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2015
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens
brenda
Koko, M.Y.F.; Mu, W.; Hassanin, H.A.M.; Zhang, S.; Lu, H.; Mohammed, J.K.; Hussain, M.; Baokun, Q.; Yang, L.
Archaeal hyperthermostable mannitol dehydrogenases A promising industrial enzymes for d-mannitol synthesis
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2020
Thermotoga maritima (Q9WYD4), Thermotoga maritima ATCC 43589 (Q9WYD4), Thermotoga maritima DSM 3109 (Q9WYD4), Thermotoga maritima JCM 10099 (Q9WYD4), Thermotoga maritima NBRC 100826 (Q9WYD4), Thermotoga neapolitana
brenda
Zhang, M.; Gu, L.; Cheng, C.; Zhu, J.; Wu, H.; Ma, J.; Dong, W.; Kong, X.; Jiang, M.; Ouyang, P.
High-yield production of mannitol by Leuconostoc pseudomesenteroides CTCC G123 from chicory-derived inulin hydrolysate
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44
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2017
Leuconostoc pseudomesenteroides, Leuconostoc pseudomesenteroides CTCC G123
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Huang, X.; Chen, X.; He, Y.; Yu, X.; Li, S.; Gao, N.; Niu, L.; Mao, Y.; Wang, Y.; Wu, X.; Wu, W.; Wu, J.; Zhou, D.; Zhan, X.; Chen, C.
Mitochondrial complex I bridges a connection between regulation of carbon flexibility and gastrointestinal commensalism in the human fungal pathogen Candida albicans
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13
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2017
Candida albicans
brenda
Crisan, M.; Maria, G.
Modular simulation to determine the optimal operating policy of a batch reactor for the enzymatic fructose reduction to mannitol with the in situ continuous enzymatic regeneration of the NAD cofactor
Rev. Chim.
68
2196-2203
2017
Pseudomonas fluorescens (O08355), Pseudomonas fluorescens DSM 50106 (O08355)
-
brenda