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Information on EC 1.1.3.41 - alditol oxidase
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1.1.3.41 alditol oxidaseIUBMB Comments
The enzyme from Streptomyces sp. IKD472 and from Streptomyces coelicolor is a monomeric oxidase containing one molecule of FAD per molecule of protein [1,2]. While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly [1,2]. Belongs in the vanillyl-alcohol-oxidase family of enzymes .
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Word Map
- 1.1.3.41
- alditols
- coelicolor
- aldos
- xylitol
- polyols
- flavoprotein
- flavin
-
one-pot
- oxidases
- fad
- medicine
-
biocatalytic
- jeotgalicoccus
-
oxidase-peroxidase
-
feedstock
- dhap
-
biofuels
-
biodiesel
- synthesis
-
oletje
-
regioselective
- d-glycerate
- dihydroxyacetone
The enzyme appears in viruses and cellular organisms
Synonyms
AldO, HotAldO, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AldO
HotAldO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xylitol + O2 = xylose + H2O2
-
-
-
-
an alditol + O2 = an aldose + H2O2
catalytic mechanism and stereoselectivity, substrate binding occurs through a lock-and-key mechanism and does not induce conformational changes with respect to the ligand-free protein, overview
an alditol + O2 = an aldose + H2O2
proposed mechanism for the oxidation of 1,2-diols to the alpha-hydroxy acids, overview
-
an alditol + O2 = an aldose + H2O2
proposed mechanism for the oxidation of 1,2-diols to the alpha-hydroxy acids, overview
-
-
an alditol + O2 = an aldose + H2O2
catalytic mechanism and stereoselectivity, substrate binding occurs through a lock-and-key mechanism and does not induce conformational changes with respect to the ligand-free protein, overview
-
-
an alditol + O2 = an aldose + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
alditol:oxygen oxidoreductase
The enzyme from Streptomyces sp. IKD472 and from Streptomyces coelicolor is a monomeric oxidase containing one molecule of FAD per molecule of protein [1,2]. While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly [1,2]. Belongs in the vanillyl-alcohol-oxidase family of enzymes [2].
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CAS REGISTRY NUMBER
COMMENTARY
177322-52-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
-
?
1,3-butanediol + O2
3-hydroxybutanal + H2O2
-
-
product identification by GC-MS
-
?
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
-
-
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
-
-
product identification by NMR
-
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
-
50% conversion after 22 h
-
-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
a flavoprotein, the flavin cofactor is covalently linked to the polypeptide chain, covalent anchoring of the FAD cofactor is an autocatalytic process and that only occurs upon correct folding of the polypeptide chain
FAD
flavin-dependent oxidase with covalently linked FAD which is located at the bottom of a funnel-shaped pocket that forms the active site
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
101
(R)-1-phenyl-1,2-ethanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
101
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
18
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
27
(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
86
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
170
1,2,4-butanetriol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
150
1,2-Butanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
97
1,2-hexanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
52
1,2-pentanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
83
1-phenyl-1,2-ethanediol
-
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
35
2-amino-1-pentanol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
250
3-butene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
480
3-butenol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
42
4-pentene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
36
D-mannitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
1.4
D-sorbitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
430
L-arabinose
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
25
L-Threitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.29 - 0.35
xylitol
recombinant oxidase-peroxidase fusion mutant enzyme, pH 7.5, temperature not specified in the publication
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.1
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.0004
(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
0.008
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
4.4
1,2,4-butanetriol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.29
1,2-Butanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
2
1,2-hexanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.85
1,2-pentanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 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
0.1
1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
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
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 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
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
9.2
D-mannitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
17
D-sorbitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
1.7
L-arabinose
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
6.3
L-Threitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
9.1 - 12.2
xylitol
recombinant oxidase-peroxidase fusion mutant enzyme, pH 7.5, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0006
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
0.0073
(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
0.0056
(R)-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
0.00001
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.0001
(S)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.0043
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
0.0015
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
12
D-sorbitol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
0.0046
glycerol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
55
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (296 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45100
47000
50000
x * 50000, recombinant oxidase-peroxidase fusion mutant enzyme, SDS-PAGE
47000
1 * 47000, SDS-PAGE, 1 * 46800, about, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 50000, recombinant oxidase-peroxidase fusion mutant enzyme, SDS-PAGE
?
-
x * 50000, recombinant oxidase-peroxidase fusion mutant enzyme, SDS-PAGE
-
monomer
1 * 47000, SDS-PAGE, 1 * 46800, about, sequence calculation
monomer
-
1 * 47000, SDS-PAGE, 1 * 46800, about, sequence calculation
-
additional information
AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes, three-dimensional structure analysis, overview
additional information
-
AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes, three-dimensional structure analysis, overview
additional information
-
AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes, three-dimensional structure analysis, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native wild-type enzyme, hanging-drop vapor diffusion method at 4°C by mixing equal volumes of 14 mg/mL AldO solution in 50 mM potassium phosphate buffer, pH 7.5, with reservoir solutions containing 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2 and 18-20% w/v PEG4000, 3-4 days, substrate incorporation by soaking the wild-type AldO crystals in a solution consisting of 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2, 25% w/v PEG 4000, 17.5% sucrose, and 25 mM substrate for 3 h, X-ray diffraction structure determination and analysis at 1.1-1.9 A resolution
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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
-
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
-
additional information
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 60
inactivation at 60°C and 50% remaining activity at 55°C
25 - 84
AldO is a highly thermostable enzyme with an unfolding temperature of 84°C, inactivation above, and an activity half-life at 75°C of 112 min
37 - 50
-
the enzyme has a half-life of 40 h at 37°C and 4 h at 50°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
under conditions which are applied for the oxidation experiments (10 mM of aldoitol oxidase in 50 mM sodium phosphate buffer, pH 7.5, at 30°C and rotary shaking (100 rpm)) the enzyme has a half-life of 30 h
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, factor Xa protease cleavage of the His-tag
recombinant His6-tagged enzyme from Escherichia coli strain MC1061
recombinant oxidase-peroxidase fusion mutant enzyme from Escherichia coli strain BL21(DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, expression of His6-tagged enzyme in Escherichia coli strain MC1061
functional expression of recombinant oxidase-peroxidase fusion mutant enzyme in Escherichia coli strain BL21(DE3) periplasm
gene aldO, DNA and amino acid sequence determination and analysis, sequence comparison, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant enzyme expression in the periplasm or on the cell surface of Escherichia coli cells of different strains. The enzyme is differently tagged, i.e. expressed as Tat-AldO or INP-AldO, and exported to the periplasm or to the cell surface of the transformed cells, overview. AldO is successfully displayed at the surface of Escherichia coli using a truncated INP variant, it contains covalently bound FAD, thus has attained a correctly folded and active conformation
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
synthesis
-
AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
synthesis
-
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
-
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
-
AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
-
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), Acidothermus cellulolyticus 11B (A0LST6), Acidothermus cellulolyticus 11B, Streptomyces coelicolor (Q9ZBU1), Streptomyces coelicolor A3(2) (Q9ZBU1), Streptomyces coelicolor A3(2)
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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)
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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
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