1.1.3.41: alditol oxidase
This is an abbreviated version!
For detailed information about alditol oxidase, go to the full flat file.
Word Map on EC 1.1.3.41
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1.1.3.41
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alditols
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coelicolor
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aldos
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synthesis
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xylitol
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polyols
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flavoprotein
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fad
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flavin
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oxidases
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medicine
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one-pot
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jeotgalicoccus
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oletje
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d-glycerate
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oxidase-peroxidase
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biodiesel
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regioselective
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biofuels
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dhap
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biocatalytic
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feedstock
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dihydroxyacetone
- 1.1.3.41
- alditols
- coelicolor
- aldos
- synthesis
- xylitol
- polyols
- flavoprotein
- fad
- flavin
- oxidases
- medicine
-
one-pot
- jeotgalicoccus
-
oletje
- d-glycerate
-
oxidase-peroxidase
-
biodiesel
-
regioselective
-
biofuels
- dhap
-
biocatalytic
-
feedstock
- dihydroxyacetone
Reaction
Synonyms
AldO, HotAldO
ECTree
1.1.3.41 alditol oxidaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.3.41 - alditol oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
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E50P
-
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
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K18R/E19R
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site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
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T16R/A17P
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site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
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T16R/A17P/K18R/G19R
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site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme
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synthesis
additional information
synthesis
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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
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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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