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(R)-1-phenyl-1,2-ethanediol + O2
?
-
-
-
-
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
(R)-1-phenyl-1,2-ethanediol + O2
hydroxy(phenyl)acetic acid + H2O2
-
-
product identification by NMR
-
?
(R)-1-phenyl-1,2-ethanediol + O2
mandelic acid + H2O2
-
the enzyme is highly enantioselective for the oxidation of (R)-1-phenyl-1,2-ethanediol
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
?
-
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
1,2,4-butanetriol + O2
?
-
-
-
-
?
1,2-butanediol + O2
?
-
-
-
-
?
1,2-hexanediol + O2
?
-
-
-
-
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
1,2-propanediol + O2
?
-
-
-
-
?
1,3,5-pentanetriol + O2
?
-
-
-
-
?
1,3-butanediol + O2
3-hydroxybutanal + H2O2
-
-
product identification by GC-MS
-
?
1,4-butanediol + O2
?
-
very poor substrate
-
-
?
1-phenyl-1,2-ethanediol + O2
?
-
the enzyme is highly enantioselective for the oxidation of 1-phenyl-1,2-ethanediol, 35% conversion to mandelic acid and two minor by-products (less than 5%) is observed after 65 h
-
-
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
2-amino-1-pentanol + O2
?
-
-
-
-
?
3-butene-1,2-diol + O2
?
-
-
-
-
?
3-butenol + O2
?
-
-
-
-
?
4-pentene-1,2-diol + O2
?
-
-
-
-
?
cis-2-butene-1,4-diol + O2
?
-
-
-
-
?
D-galactose + O2
?
-
very poor substrate
-
-
?
D-glyceraldehyde + O2
D-glycerate + H2O2
glycerol + O2
?
-
-
-
-
?
glycerol + O2
D-glyceraldehyde + H2O2
glycerol + O2
glyceraldehyde + H2O2
-
-
-
-
?
L-threitol + O2
?
-
-
-
-
?
xylitol + O2
D-xylose + H2O2
-
best substrate
-
-
?
xylitol + O2
xylose + H2O2
additional information
?
-
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
-
-
product identification by NMR
-
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
-
50% conversion after 22 h
-
-
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
-
-
-
?
D-glyceraldehyde + O2
D-glycerate + H2O2
-
-
-
-
?
D-glyceraldehyde + O2
D-glycerate + H2O2
-
-
-
-
?
D-mannitol + O2
?
-
-
-
-
?
D-mannitol + O2
?
-
-
-
?
D-mannitol + O2
?
-
-
-
?
D-mannitol + O2
? + H2O2
-
-
-
?
D-mannitol + O2
? + H2O2
-
-
-
?
D-sorbitol + O2
?
-
-
-
-
?
D-sorbitol + O2
?
-
-
-
?
D-sorbitol + O2
?
-
-
-
?
D-sorbitol + O2
? + H2O2
-
-
-
?
D-sorbitol + O2
? + H2O2
-
-
-
?
glycerol + O2
? + H2O2
-
-
-
?
glycerol + O2
? + H2O2
-
-
-
?
glycerol + O2
? + H2O2
-
-
-
?
glycerol + O2
? + H2O2
-
-
-
?
glycerol + O2
D-glyceraldehyde + H2O2
-
-
-
-
?
glycerol + O2
D-glyceraldehyde + H2O2
-
-
-
-
?
L-arabinose + O2
?
-
-
-
-
?
L-arabinose + O2
?
-
very poor substrate
-
-
?
sorbitol + O2
?
-
-
-
-
?
sorbitol + O2
?
-
-
-
-
?
xylitol + O2
?
-
-
-
-
?
xylitol + O2
?
-
best substrate
-
-
?
xylitol + O2
xylose + H2O2
-
-
-
?
xylitol + O2
xylose + H2O2
-
-
-
?
xylitol + O2
xylose + H2O2
-
-
-
-
?
xylitol + O2
xylose + H2O2
-
-
-
?
xylitol + O2
xylose + H2O2
-
-
-
?
xylitol + O2
xylose + H2O2
-
-
-
-
?
xylitol + O2
xylose + H2O2
-
-
-
?
additional information
?
-
-
AldO catalyzes the C1 oxidation of several polyols
-
-
?
additional information
?
-
-
substrate specificity, besides alditols, 1,2-diols are reasonable substrates indicating that two adjacent hydroxy groups at C-1 and C-2 seem to be a minimal requirement for a compound in order to be effectively oxidized by AldO, overview
-
-
?
additional information
?
-
-
the enzyme is able to perform oxidations of alcohols into aldehydes/ketones (single oxidation) and oxidations of alcohols into acids (double oxidation)
-
-
?
additional information
?
-
-
AldO catalyzes the C1 oxidation of several polyols
-
-
?
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10 - 101
(R)-1-phenyl-1,2-ethanediol
27 - 86
(S)-1-phenyl-1,2-ethanediol
68 - 83
1-phenyl-1,2-ethanediol
additional information
additional information
-
10
(R)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
18
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
101
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
101
(R)-1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
27
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
86
(S)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
86
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
86
(S)-1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
170
1,2,4-butanetriol
-
pH 7.5, 30°C
170
1,2,4-butanetriol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
150
1,2-Butanediol
-
pH 7.5, 30°C
150
1,2-Butanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
97
1,2-hexanediol
-
pH 7.5, 30°C
97
1,2-hexanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
52
1,2-pentanediol
-
pH 7.5, 30°C
52
1,2-pentanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
68
1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
83
1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
83
1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
83
1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
35
2-amino-1-pentanol
-
pH 7.5, 30°C
35
2-amino-1-pentanol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
250
3-butene-1,2-diol
-
pH 7.5, 30°C
250
3-butene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
480
3-butenol
-
pH 7.5, 30°C
480
3-butenol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
42
4-pentene-1,2-diol
-
pH 7.5, 30°C
42
4-pentene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
5.5
D-mannitol
pH 7.5, 25°C, recombinant enzyme
36
D-mannitol
-
pH 7.5, 30°C
36
D-mannitol
pH 7.5, 25°C, recombinant enzyme
36
D-mannitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.44
D-sorbitol
pH 7.5, 25°C, recombinant enzyme
1.4
D-sorbitol
-
pH 7.5, 30°C
1.4
D-sorbitol
pH 7.5, 25°C, recombinant enzyme
1.4
D-sorbitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
270
glycerol
pH 7.5, 25°C, recombinant enzyme
350
glycerol
-
pH 7.5, 30°C
350
glycerol
pH 7.5, 25°C, recombinant enzyme
350
glycerol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
430
L-arabinose
-
pH 7.5, 30°C
430
L-arabinose
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
25
L-Threitol
-
pH 7.5, 30°C
25
L-Threitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.007
xylitol
pH 7.5, 25°C, recombinant enzyme
0.29 - 0.35
xylitol
recombinant oxidase-peroxidase fusion mutant enzyme, pH 7.5, temperature not specified in the publication
0.32
xylitol
-
pH 7.5, 30°C
0.32
xylitol
pH 7.5, 25°C, recombinant enzyme
0.32
xylitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
additional information
additional information
-
substrate specificity and steady state kinetics, overview
-
additional information
additional information
steady-state kinetic analysis, overview
-
additional information
additional information
steady-state kinetic analysis, overview
-
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0.1 - 0.74
(R)-1-phenyl-1,2-ethanediol
0.0004 - 0.008
(S)-1-phenyl-1,2-ethanediol
0.1 - 0.36
1-phenyl-1,2-ethanediol
0.1
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.74
(R)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
0.74
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.74
(R)-1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0004
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.008
(S)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
0.008
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.008
(S)-1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
4.4
1,2,4-butanetriol
-
pH 7.5, 30°C
4.4
1,2,4-butanetriol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.29
1,2-Butanediol
-
pH 7.5, 30°C
0.29
1,2-Butanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
2
1,2-hexanediol
-
pH 7.5, 30°C
2
1,2-hexanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.85
1,2-pentanediol
-
pH 7.5, 30°C
0.85
1,2-pentanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.1
1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.36
1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
0.36
1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.36
1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.017
2-amino-1-pentanol
-
pH 7.5, 30°C
0.017
2-amino-1-pentanol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.34
3-butene-1,2-diol
-
pH 7.5, 30°C
0.34
3-butene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.1
3-butenol
-
pH 7.5, 30°C
0.1
3-butenol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.35
4-pentene-1,2-diol
-
pH 7.5, 30°C
0.35
4-pentene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
2.5
D-mannitol
pH 7.5, 25°C, recombinant enzyme
9.2
D-mannitol
-
pH 7.5, 30°C
9.2
D-mannitol
pH 7.5, 25°C, recombinant enzyme
9.2
D-mannitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
1.2
D-sorbitol
pH 7.5, 25°C, recombinant enzyme
17
D-sorbitol
-
pH 7.5, 30°C
17
D-sorbitol
pH 7.5, 25°C, recombinant enzyme
17
D-sorbitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
1.3
glycerol
pH 7.5, 25°C, recombinant enzyme
1.6
glycerol
-
pH 7.5, 30°C
1.6
glycerol
pH 7.5, 25°C, recombinant enzyme
1.6
glycerol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
1.7
L-arabinose
-
pH 7.5, 30°C
1.7
L-arabinose
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
6.3
L-Threitol
-
pH 7.5, 30°C
6.3
L-Threitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
1.9
xylitol
pH 7.5, 25°C, recombinant enzyme
9.1 - 12.2
xylitol
recombinant oxidase-peroxidase fusion mutant enzyme, pH 7.5, temperature not specified in the publication
13
xylitol
-
pH 7.5, 30°C
13
xylitol
pH 7.5, 25°C, recombinant enzyme
13
xylitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0056 - 0.0073
(R)-1-phenyl-1,2-ethanediol
0.00001 - 0.0001
(S)-1-phenyl-1,2-ethanediol
0.026
1,2,4-butanetriol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0019
1,2-Butanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.021
1,2-hexanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.016
1,2-pentanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0003
1,2-propanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0078
1,3,5-pentanetriol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0015 - 0.0043
1-phenyl-1,2-ethanediol
0.0006
2-amino-1-pentanol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0014
3-butene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0002
3-butenol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0083
4-pentene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0003
D-galactose
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.004
L-arabinose
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.25
L-Threitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0056
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.0073
(R)-1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0073
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.00001
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.0001
(S)-1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0001
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.0015
1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.0043
1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0043
1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.26
D-mannitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.26
D-mannitol
pH 7.5, 25°C, recombinant enzyme
0.45
D-mannitol
pH 7.5, 25°C, recombinant enzyme
2.7
D-sorbitol
pH 7.5, 25°C, recombinant enzyme
12
D-sorbitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
12
D-sorbitol
pH 7.5, 25°C, recombinant enzyme
0.0046
glycerol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0046
glycerol
pH 7.5, 25°C, recombinant enzyme
0.0048
glycerol
pH 7.5, 25°C, recombinant enzyme
27
xylitol
pH 7.5, 25°C, recombinant enzyme
41
xylitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
41
xylitol
pH 7.5, 25°C, recombinant enzyme
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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.
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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E154P
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
E50P
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
K18R/E19R
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
L234R/D235P
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
R232A/P233G
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
R232A/P233G/L234R/D235P
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
T16R/A17P
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
T16R/A17P/K18R/G19R
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
E154P
-
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
-
E50P
-
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
-
K18R/E19R
-
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
-
T16R/A17P
-
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
-
T16R/A17P/K18R/G19R
-
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
-
synthesis
-
synthesis of rare sugars using Escherichia coli whole cells. The donor substrate dihydroxyacetone phosphate (DHAP) is generated from glycerol by glycerol kinase (GK) and glycerol phosphate oxidase (GPO). The acceptor D-glyceraldehyde is directly produced from glycerol by alditol oxidase. The aldol reaction between DHAP and D-glyceraldehyde is performed by L-rhamnulose-1-phosphate aldolase (RhaD) to generate the corresponding sugar-1-phosphate. Finally, the phosphate group is removed by fructose-1-phosphatase (YqaB) to obtain the rare sugars D-sorbose and D-psicose. Under the optimized conditions, the cascade produces 7.9 g/l of D-sorbose and D-psicose with a total conversion rate of 17.7% from glycerol
synthesis
-
synthesis of rare sugars using Escherichia coli whole cells. The donor substrate dihydroxyacetone phosphate (DHAP) is generated from glycerol by glycerol kinase (GK) and glycerol phosphate oxidase (GPO). The acceptor D-glyceraldehyde is directly produced from glycerol by alditol oxidase. The aldol reaction between DHAP and D-glyceraldehyde is performed by L-rhamnulose-1-phosphate aldolase (RhaD) to generate the corresponding sugar-1-phosphate. Finally, the phosphate group is removed by fructose-1-phosphatase (YqaB) to obtain the rare sugars D-sorbose and D-psicose. Under the optimized conditions, the cascade produces 7.9 g/l of D-sorbose and D-psicose with a total conversion rate of 17.7% from glycerol
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additional information
construction of an AldO mutant synthetic bifunctional enzyme, the enzyme from Streptomyces coelicolor A3(2) is endowed with an extra catalytic functionality by fusing it to a microperoxidase. The mutant is functional and a both fully covalently flavinylated and heminylated: an oxiperoxidase. Replacement of portions of the wild-type AldO sequence with the bacterial cytochrome c CXXCH heme-binding motif, domain structure, overview
additional information
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construction of an AldO mutant synthetic bifunctional enzyme, the enzyme from Streptomyces coelicolor A3(2) is endowed with an extra catalytic functionality by fusing it to a microperoxidase. The mutant is functional and a both fully covalently flavinylated and heminylated: an oxiperoxidase. Replacement of portions of the wild-type AldO sequence with the bacterial cytochrome c CXXCH heme-binding motif, domain structure, overview
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medicine
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medicine
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monitoring xylitol using immobilized xylitol oxidase
medicine
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quantitative analysis of xylitol
synthesis
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AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
synthesis
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utilization of recombinant enzyme expressed in the periplasm or on the cell surface of Escherichia coli as biocatalyst in a non-laborious and non-costly whole-cell application for reacting on towards different polyols such as xylitol and sorbitol
synthesis
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biosynthetic production of glycolate from glycerol using a variant of alditol oxidase, 2-hydroxyglutarate-pyruvate transhydrogenase from Saccharomyces cerevisiae, alpha-ketoisovalerate decarboxylase from Lactococcus lactis, and aldehyde dehydrogenase from Escherichia coli in an artificial operon expressed in Escherichia coli. To redirect glycerol flux toward glycolate synthesis, key genes of the native glycerol assimilation pathways are deleted and a second plasmid expressing Dld3 to reduce the accumulation of the intermediate D-glycerate is introduced. The final engineered strain produces 0.64 g/l glycolate in shake flasks, which is increased to 4.74 g/l in fed-batch fermentation
synthesis
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one-pot biocatalytic system converting a range of triacylglycerols/natural oils into alpha-olefins. The system consists of CRL from Candida rugosa (for triacylglycerol hydrolysis to provide free fatty acids and glycerol), AldO (for in situ H2O2 generation upon glycerol oxidation), and OleTJE (for free fatty acid decarboxylation using H2O2 as cofactor) and is independent of exogenous addition of H2O2. The reaction system achieves a 68.5% total alkene yield from 500 microM coconut oil. About 0.5 g/l of alpha-olefins are produced from coconut oil (1500 microM) upon some reaction optimization
synthesis
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production of ethylene glycol from glycerol by an artificial enzymatic cascade comprised of alditol oxidase, catalase, glyoxylate/hydroxypyruvate reductase, pyruvate decarboxylase and lactaldehyde:propanediol oxidoreductase. The NADH generated during the dehydrogenation of the glycerol oxidation product D-glycerate can be used as the reductant to support the ethylene glycol production. Using this in vitro synthetic system with self-sufficient NADH recycling, 7.64 mM ethylene glycol is produced from 10 mM glycerol in 10 h, with a yield of 0.515 g/g
synthesis
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synthesis of rare ketoses from glycerol and D-/L-glyceraldehyde in a one-pot multienzyme fashion in which the only carbon source is glycerol. Glycerol is phosphorylated and then oxidized at C2 to afford dihydroxyacetone phosphate. The primary alcohol of glycerol is also oxidized to give the acceptor molecule glycerol aldehyde in situ (D- or L-isomer can be formed stereospecifically with either alditol oxidase or horse liver alcohol dehydrogenase). Different dihydroxyacetone phosphate-dependent aldolases are used to generate the aldol adducts (rare ketohexose phosphates) with various stereoconfigurations and diastereomeric ratios
synthesis
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utilization of recombinant enzyme expressed in the periplasm or on the cell surface of Escherichia coli as biocatalyst in a non-laborious and non-costly whole-cell application for reacting on towards different polyols such as xylitol and sorbitol
-
synthesis
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biosynthetic production of glycolate from glycerol using a variant of alditol oxidase, 2-hydroxyglutarate-pyruvate transhydrogenase from Saccharomyces cerevisiae, alpha-ketoisovalerate decarboxylase from Lactococcus lactis, and aldehyde dehydrogenase from Escherichia coli in an artificial operon expressed in Escherichia coli. To redirect glycerol flux toward glycolate synthesis, key genes of the native glycerol assimilation pathways are deleted and a second plasmid expressing Dld3 to reduce the accumulation of the intermediate D-glycerate is introduced. The final engineered strain produces 0.64 g/l glycolate in shake flasks, which is increased to 4.74 g/l in fed-batch fermentation
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synthesis
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one-pot biocatalytic system converting a range of triacylglycerols/natural oils into alpha-olefins. The system consists of CRL from Candida rugosa (for triacylglycerol hydrolysis to provide free fatty acids and glycerol), AldO (for in situ H2O2 generation upon glycerol oxidation), and OleTJE (for free fatty acid decarboxylation using H2O2 as cofactor) and is independent of exogenous addition of H2O2. The reaction system achieves a 68.5% total alkene yield from 500 microM coconut oil. About 0.5 g/l of alpha-olefins are produced from coconut oil (1500 microM) upon some reaction optimization
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synthesis
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production of ethylene glycol from glycerol by an artificial enzymatic cascade comprised of alditol oxidase, catalase, glyoxylate/hydroxypyruvate reductase, pyruvate decarboxylase and lactaldehyde:propanediol oxidoreductase. The NADH generated during the dehydrogenation of the glycerol oxidation product D-glycerate can be used as the reductant to support the ethylene glycol production. Using this in vitro synthetic system with self-sufficient NADH recycling, 7.64 mM ethylene glycol is produced from 10 mM glycerol in 10 h, with a yield of 0.515 g/g
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synthesis
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synthesis of rare ketoses from glycerol and D-/L-glyceraldehyde in a one-pot multienzyme fashion in which the only carbon source is glycerol. Glycerol is phosphorylated and then oxidized at C2 to afford dihydroxyacetone phosphate. The primary alcohol of glycerol is also oxidized to give the acceptor molecule glycerol aldehyde in situ (D- or L-isomer can be formed stereospecifically with either alditol oxidase or horse liver alcohol dehydrogenase). Different dihydroxyacetone phosphate-dependent aldolases are used to generate the aldol adducts (rare ketohexose phosphates) with various stereoconfigurations and diastereomeric ratios
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synthesis
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AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
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Yamashita, M.; Omura, H.; Okamoto, E.; Furuya, Y.; Yabuuchi, M.; Fukahi, K.; Murooka, Y.
Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472
J. Biosci. Bioeng.
89
350-360
2000
Streptomyces sp.
brenda
Murooka, Y.; Yamashita, M.
Genetic and protein engineering of diagnostic enzymes, cholesterol oxidase and xylitol oxidase
J. Biosci. Bioeng.
91
433-441
2001
Streptomyces sp.
brenda
Rhee, J.I.; Yamashita, M.; Scheper, T.
Development of xylitol oxidase-based flow injection analysis for monitoring of xylitol concentrations
Anal. Chim. Acta
456
293-301
2002
Streptomyces sp.
-
brenda
Van Hellemond, E.; Vermote, L.; Koolen, W.; Sonke, T.; Zandvoort, E.; Heuts, D.; Janssen, D.; Fraaije, M.
Exploring the biocatalytic scope of alditol oxidase from Streptomyces coelicolor
Adv. Synth. Catal.
351
1523-1530
2009
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
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brenda
van Bloois, E.; Winter, R.T.; Janssen, D.B.; Fraaije, M.W.
Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis
Appl. Microbiol. Biotechnol.
83
679-687
2009
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Forneris, F.; Heuts, D.; Delvecchio, M.; Rovida, S.; Fraaije, M.; Mattevi, A.
Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase
Biochemistry
47
978-985
2008
Streptomyces coelicolor (Q9ZBU1), Streptomyces coelicolor, Streptomyces coelicolor A3(2) (Q9ZBU1), Streptomyces coelicolor A3(2)
brenda
Winter, R.T.; Heuts, D.P.; Rijpkema, E.M.; van Bloois, E.; Wijma, H.J.; Fraaije, M.W.
Hot or not? Discovery and characterization of a thermostable alditol oxidase from Acidothermus cellulolyticus 11B
Appl. Microbiol. Biotechnol.
95
389-403
2012
Acidothermus cellulolyticus (A0LST6), Streptomyces coelicolor (Q9ZBU1), Acidothermus cellulolyticus 11B (A0LST6), Acidothermus cellulolyticus 11B, Streptomyces coelicolor A3(2) (Q9ZBU1), Streptomyces coelicolor A3(2)
brenda
Winter, R.T.; van den Berg, T.E.; Colpa, D.I.; van Bloois, E.; Fraaije, M.W.
Functionalization of oxidases with peroxidase activity creates oxiperoxidases: a new breed of hybrid enzyme capable of cascade chemistry
ChemBioChem
13
252-258
2012
Streptomyces coelicolor (Q9ZBU1), Streptomyces coelicolor A3(2) (Q9ZBU1), Streptomyces coelicolor A3(2)
brenda
Matthews, S.; Tee, K.L.; Rattray, N.J.; McLean, K.J.; Leys, D.; Parker, D.A.; Blankley, R.T.; Munro, A.W.
Production of alkenes and novel secondary products by P450 OleTJE using novel H2O2-generating fusion protein systems
FEBS Lett.
591
737-750
2017
Streptomyces coelicolor
brenda
Zhan, T.; Chen, Q.; Zhang, C.; Bi, C.; Zhang, X.
Constructing a novel biosynthetic pathway for the production of glycolate from glycerol in Escherichia coli
ACS Synth. Biol.
9
2600-2609
2020
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Chen, Z.; Li, Z.; Li, F.; Wang, N.; Gao, X.D.
Characterization of alditol oxidase from Streptomyces coelicolor and its application in the production of rare sugars
Bioorg. Med. Chem.
28
115464
2020
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Jiang, Y.; Li, Z.; Zheng, S.; Xu, H.; Zhou, Y.; Gao, Z.; Meng, C.; Li, S.
Establishing an enzyme cascade for one-pot production of alpha-olefins from low-cost triglycerides and oils without exogenous H2O2 addition
Biotechnol. Biofuels
13
52
2020
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Li, K.; Sun, W.; Meng, W.; Yan, J.; Zhang, Y.; Guo, S.; Lue, C.; Ma, C.; Gao, C.
Production of ethylene glycol from glycerol using an in vitro enzymatic cascade
Catalysts
11
214
2021
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
-
brenda
Li, Z.; Li, F.; Cai, L.; Chen, Z.; Qin, L.; Gao, X.D.
One-pot multienzyme synthesis of rare ketoses from glycerol
J. Agric. Food Chem.
68
1347-1353
2020
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda