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Synonyms
D-mannitol dehydrogenase, M2DH, mannitol 2-dehydrogenase, mannitol dehydrogenase, mannitol-2-dehydrogenase, MDH, mt-dh, MtDH,
MtlD, NAD+-dependent mannitol dehydrogenase,
more
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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-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
-
-
-
-
?
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+
-
-
-
-
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+
-
-
-
?
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 + NADPH + H+

D-mannitol + NADP+
also active on fructose with NADPH
-
-
?
D-fructose + NADPH + H+
D-mannitol + NADP+
also active on fructose with NADPH
-
-
?
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+
-
-
-
-
?, 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+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
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
-
-
?
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
?
-
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
?
-
-
the enzyme shows no activity with xylitol, inositol, sorbitol, rhamnose, mannose and xylose, and with NADPH and NADP+ as cofactors
-
-
?
additional information
?
-
-
the enzyme shows no activity with xylitol, inositol, sorbitol, rhamnose, mannose and xylose, and with NADPH and NADP+ as cofactors
-
-
?
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citrate
50 mM, pH 5.4, 72% inhibition
CuSO4
-
1 mM, 28% inhibition of D-fructose reduction, 18% inhibition of D-sorbitol oxidation
D-fructose
-
substrate inhibition, Ki: 1.356 mM
D-mannitol
-
product inhibition, Ki: 24.6 mM
FeCl2
-
10 mM, 88% inhibition
imidazole
175 mM,pH 7.0, 74% inhibition
Methyl mercurinitrate
-
complete inhibition
MnCl2
-
10 mM, 48% inhibition
p-chloromercuribenzoate
-
0.1 mM, 100% inhibition
PCMB
0.1 mM, complete inhibition
ZnCl2
-
10 mM, 60% inhibition
Cu2+

-
1 mM, 61% inhibition
Cu2+
-
about 20% residual activity at 1 mM
EDTA

20 mM, complete inhibition, can be restored by 20 mM Zn2+, but not by Mn2+ or Mg2+
EDTA
activity of MtDH pretreated with 10 mM EDTA for 20 min at 37°C decreases 96%. Adding 20 mM ZnCl2 to the EDTA-treated enzyme restores activity up to 80% of the control (enzyme not treated with EDTA). Adding 20 mM CoCl2 and 20 mM MnCl2 to the EDTA-treated enzyme restores activity up to 132% and 94% of the control, respectively. In contrast, adding 20 mM MgCl2 or CaCl2 does not increase the activity of the EDTA-treated enzyme.; activity of MtDH pretreated with 10 mM for 20 min at 37°C decreases 96%. Adding 20 mM ZnCl2 to the EDTA-treated enzyme restores activity up to 80% of the control. Adding 20 mM CoCl2 and 20 mM MnCl2 to the EDTA-treated enzyme restores activity up to 132% and 94% of the control, respectively
NaCl

the enzyme displays a 4.37fold decrease of activity in 600 mM and about 1000fold decrease of activity in 1000 mM NaCl
NaCl
-
with increasing NaCl concentrations enzyme activity decreases, 1.5 M NaCl 74% inhibition for oxidation and 72% inhibition for reduction
NAD+

-
NAD+
-
product inhibition, Ki: 0.6 mM
p-hydroxymercuribenzoate

-
complete inhibition
p-hydroxymercuribenzoate
-
1 mM, 56% inhibition
Zn2+

-
1 mM, 94% inhibition
additional information

-
no inhibitory effect on D-fructose reduction detected for MgSO4, CaSO4, Na2SO4, ZnSO4 and MnSO4
-
additional information
no inhibition of M2DH by bovine serum albumin
-
additional information
-
no inhibition of M2DH by bovine serum albumin
-
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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
0.24
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
-
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

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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
162
D-arabinitol
pH 10.0, 25°C
64
D-xylulose
pH 7.1, 25°C
60
L-sorbitol
pH 10.0, 25°C
0.0012 - 0.599
meso-erythritol
0.0013
D-arabitol

mutant enzyme N300D, at pH 7.4 and 25°C
0.0017
D-arabitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.0029
D-arabitol
mutant enzyme D230A, at pH 7.4 and 25°C
0.034
D-arabitol
mutant enzyme R373A, at pH 7.4 and 25°C
0.044
D-arabitol
mutant enzyme N191A, at pH 7.4 and 25°C
0.06
D-arabitol
mutant enzyme N300S, at pH 7.4 and 25°C
0.092
D-arabitol
mutant enzyme N300A, at pH 7.4 and 25°C
0.29
D-arabitol
mutant enzyme H303A, at pH 7.4 and 25°C
0.37
D-arabitol
mutant enzyme K381A, at pH 7.4 and 25°C
5.5
D-arabitol
mutant enzyme E133Q, at pH 7.4 and 25°C
6.59
D-arabitol
wild type enzyme, at pH 7.4 and 25°C
7.3
D-arabitol
mutant enzyme E133A, at pH 7.4 and 25°C
0.15
D-fructose

mutant N191D/N300D, pH 10.0, temperature not specified in the publication
0.8
D-fructose
mutant N300D, pH 10.0, temperature not specified in the publication
0.9
D-fructose
mutant N300D, pH 6.8, temperature not specified in the publication
2.7
D-fructose
mutant N191D, pH 7.1, temperature not specified in the publication
8.2
D-fructose
mutant N191D, pH 10.0, temperature not specified in the publication
20
D-fructose
-
in 50 mM glycine/NaOH buffer at pH 10.0
61
D-fructose
wild-type, pH 7.1, temperature not specified in the publication
86
D-fructose
pH 7.1, 25°C
180
D-fructose
-
at pH 6.5 and 90°C
0.00055
D-mannitol

mutant N191D, pH 7.1, temperature not specified in the publication
0.00083
D-mannitol
mutant enzyme N300D, at pH 7.4 and 25°C
0.001
D-mannitol
mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C
0.0011
D-mannitol
mutant N191D, pH 10.0, temperature not specified in the publication
0.0014
D-mannitol
mutant N300D, pH 6.8, temperature not specified in the publication
0.0015
D-mannitol
mutant N300D, pH 10.0, temperature not specified in the publication
0.018
D-mannitol
mutant enzyme R373A, at pH 7.4 and 25°C
0.096
D-mannitol
mutant enzyme N300S, at pH 7.4 and 25°C
0.19
D-mannitol
mutant enzyme K381A, at pH 7.4 and 25°C
0.209
D-mannitol
mutant enzyme N191A, at pH 7.4 and 25°C
0.21
D-mannitol
mutant enzyme N300A, at pH 7.4 and 25°C
0.39
D-mannitol
mutant enzyme D230A, at pH 7.4 and 25°C
0.49
D-mannitol
mutant enzyme H303A, at pH 7.4 and 25°C
3.22
D-mannitol
mutant enzyme E133Q, at pH 7.4 and 25°C
3.99
D-mannitol
mutant enzyme E133A, at pH 7.4 and 25°C
4.39
D-mannitol
wild type enzyme, at pH 7.4 and 25°C
15.9
D-mannitol
wild-type, pH 7.1, temperature not specified in the publication
40
D-mannitol
-
in 50 mM glycine/NaOH buffer at pH 10.0
212
D-mannitol
pH 10.0, 25°C
0.0012
meso-erythritol

mutant enzyme N191A, at pH 7.4 and 25°C
0.0024
meso-erythritol
mutant enzyme N300S, at pH 7.4 and 25°C
0.0036
meso-erythritol
mutant enzyme N300A, at pH 7.4 and 25°C
0.0159
meso-erythritol
mutant enzyme H303A, at pH 7.4 and 25°C
0.489
meso-erythritol
mutant enzyme E133Q, at pH 7.4 and 25°C
0.538
meso-erythritol
mutant enzyme E133A, at pH 7.4 and 25°C
0.599
meso-erythritol
wild type enzyme, at pH 7.4 and 25°C
3
NAD(P)H

wild-type
12
NAD(P)H
mutant D69A/D69A
0.04
NAD+

mutant N191A/N300A, pH 10.0, 25°C
0.55
NAD+
mutant N191L, pH 10.0, 25°C
2.78
NAD+
mutant N191A, pH 10.0, 25°C
20
NAD+
-
recombinant protein
40
NAD+
wild-type, pH 10.0, 25°C
0.00045
NADH

mutant N191A/N300A, pH 7.1, 25°C
0.55
NADH
mutant N191L, pH 7.1, 25°C
0.56
NADH
mutant N191A, pH 7.1, 25°C
4.6
NADH
mutant D69A/D69A
54
NADH
-
recombinant protein
61
NADH
wild-type, pH 7.1, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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 enzymeâNAD+-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 enzymeâNAD+-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
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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
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BLR(DE3) cells
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli strain BL21pLysS
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expression in Escherichia coli
expression in Escherichia coli, effecting strong catalytic activity of an NADH-dependent reduction of D-fructose to D-mannitol in cell extracts of the recombinant Escherichia coli strain
expression of wild-type and mutant enzymes in Escherichia coli strain JM109
expression of wild-type enzyme and mutant enzymes in Escherichia coli
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fusion of six His codons to the 3'-end of the mdh gene and expression in Escherichia coli M15. The enzyme shares significant sequence similarity with the medium-chain dehydrogenase/reductase protein family
gene mdh, high level expression in Bacillus megaterium requiring the adaptation of the corresponding ribosome binding site, the fdh gene is adapted to Bacillus megaterium codon usage via complete chemical gene synthesis, overview
gene mtdh, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
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MtDH is expressed in Escherichia coli BL21(DE3)
subcloned into vector pDEST110 and overexpressed in different strains of Escherichia coli (BL21 (DE3) plysS, JM109, Origami(DE3) or M15)
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the TM0298 gene subcloned into the NdeI and XhoI sites of pET24a(+) to yield plasmid pTmMtDH, from which MtDH is expressed with a C-terminal His6-tag in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells

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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli

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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
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