Information on EC 1.1.3.41 - alditol oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.3.41
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RECOMMENDED NAME
GeneOntology No.
alditol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an alditol + O2 = an aldose + H2O2
show the reaction diagram
xylitol + O2 = xylose + H2O2
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
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Metabolic pathways
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Pentose and glucuronate interconversions
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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-arabitol (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].
CAS REGISTRY NUMBER
COMMENTARY hide
177322-52-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-1-phenyl-1,2-ethanediol + O2
?
show the reaction diagram
-
-
-
-
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
show the reaction diagram
(R)-1-phenyl-1,2-ethanediol + O2
hydroxy(phenyl)acetic acid + H2O2
show the reaction diagram
-
-
product identification by NMR
-
?
(R)-1-phenyl-1,2-ethanediol + O2
mandelic acid + H2O2
show the reaction diagram
-
the enzyme is highly enantioselective for the oxidation of (R)-1-phenyl-1,2-ethanediol
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
?
show the reaction diagram
-
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
show the reaction diagram
1,2,4-butanetriol + O2
?
show the reaction diagram
-
-
-
-
?
1,2-butanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,2-hexanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
show the reaction diagram
1,2-propanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,3,5-pentanetriol + O2
?
show the reaction diagram
-
-
-
-
?
1,3-butanediol + O2
3-hydroxybutanal + H2O2
show the reaction diagram
-
-
product identification by GC-MS
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?
1,4-butanediol + O2
?
show the reaction diagram
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very poor substrate
-
-
?
1-phenyl-1,2-ethanediol + O2
?
show the reaction diagram
-
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
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-
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
show the reaction diagram
2-amino-1-pentanol + O2
?
show the reaction diagram
-
-
-
-
?
3-butene-1,2-diol + O2
?
show the reaction diagram
-
-
-
-
?
3-butenol + O2
?
show the reaction diagram
-
-
-
-
?
4-pentene-1,2-diol + O2
?
show the reaction diagram
-
-
-
-
?
cis-2-butene-1,4-diol + O2
?
show the reaction diagram
-
-
-
-
?
D-galactose + O2
?
show the reaction diagram
-
very poor substrate
-
-
?
D-mannitol + O2
?
show the reaction diagram
D-mannitol + O2
? + H2O2
show the reaction diagram
D-sorbitol + O2
?
show the reaction diagram
D-sorbitol + O2
? + H2O2
show the reaction diagram
glycerol + O2
?
show the reaction diagram
-
-
-
-
?
glycerol + O2
? + H2O2
show the reaction diagram
L-arabinose + O2
?
show the reaction diagram
L-threitol + O2
?
show the reaction diagram
-
-
-
-
?
sorbitol + O2
?
show the reaction diagram
xylitol + O2
?
show the reaction diagram
xylitol + O2
D-xylose + H2O2
show the reaction diagram
-
best substrate
-
-
?
xylitol + O2
xylose + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-mannitol + O2
?
show the reaction diagram
D-sorbitol + O2
?
show the reaction diagram
sorbitol + O2
?
show the reaction diagram
xylitol + O2
?
show the reaction diagram
-
-
-
-
?
xylitol + O2
xylose + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10 - 101
(R)-1-phenyl-1,2-ethanediol
27 - 86
(S)-1-phenyl-1,2-ethanediol
170
1,2,4-butanetriol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
150
1,2-Butanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
97
1,2-hexanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
52
1,2-pentanediol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
68 - 83
1-phenyl-1,2-ethanediol
35
2-amino-1-pentanol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
250
3-butene-1,2-diol
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
480
3-butenol
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in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
42
4-pentene-1,2-diol
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in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
5.5 - 36
D-mannitol
0.44 - 1.4
D-sorbitol
270 - 350
glycerol
430
L-arabinose
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
25
L-Threitol
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in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
0.007 - 0.35
xylitol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.74
(R)-1-phenyl-1,2-ethanediol
0.0004 - 0.008
(S)-1-phenyl-1,2-ethanediol
4.4
1,2,4-butanetriol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
0.29
1,2-Butanediol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
2
1,2-hexanediol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
0.85
1,2-pentanediol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
0.1 - 0.36
1-phenyl-1,2-ethanediol
0.017
2-amino-1-pentanol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
0.34
3-butene-1,2-diol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
0.1
3-butenol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
0.35
4-pentene-1,2-diol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
2.5 - 9.2
D-mannitol
1.2 - 17
D-sorbitol
1.3 - 1.6
glycerol
1.7
L-arabinose
Streptomyces coelicolor
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in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
6.3
L-Threitol
Streptomyces coelicolor
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in 50 mM sodium phosphate buffer, at pH 7.5 and 30C; pH 7.5, 30C
1.9 - 13
xylitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0056 - 0.0073
(R)-1-phenyl-1,2-ethanediol
3890
0.00001 - 0.0001
(S)-1-phenyl-1,2-ethanediol
4171
0.026
1,2,4-butanetriol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
8983
0.0019
1,2-Butanediol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
2456
0.021
1,2-hexanediol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
5696
0.016
1,2-pentanediol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
6145
0.0003
1,2-propanediol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
862
0.0078
1,3,5-pentanetriol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
163624
0.0015 - 0.0043
1-phenyl-1,2-ethanediol
5046
0.0006
2-amino-1-pentanol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
11992
0.0014
3-butene-1,2-diol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
7818
0.0002
3-butenol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
11991
0.0083
4-pentene-1,2-diol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
11990
0.0003
D-galactose
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
71
0.26 - 0.45
D-mannitol
495
2.7 - 12
D-sorbitol
627
0.0046 - 0.0048
glycerol
135
0.004
L-arabinose
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
206
0.25
L-Threitol
Streptomyces coelicolor
-
in 50 mM sodium phosphate buffer, at pH 7.5 and 30C
5568
27 - 41
xylitol
416
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17.3
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substrate xylitol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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; over 80% of maximal activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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gel filtration
45100
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1 * 45100
46800
about, sequence calculation
50000
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x * 50000, recombinant oxidase-peroxidase fusion mutant enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native wild-type enzyme, hanging-drop vapor diffusion method at 4C 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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
-
-
440251
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 84
AldO is a highly thermostable enzyme with an unfolding temperature of 84C, inactivation above, and an activity half-life at 75C of 112 min
25 - 60
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inactivation at 60C and 50% remaining activity at 55C
37 - 50
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the enzyme has a half-life of 40 h at 37C and 4 h at 50C
37
-
half-life of 40 h
50
-
half-life of 4 h
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 30C 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
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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
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expressed in Escherichia coli Top10 cells
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expression in Escherichia coli
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functional expression of recombinant oxidase-peroxidase fusion mutant enzyme in Escherichia coli strain BL21(DE3) periplasm
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
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