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Information on EC 1.1.3.41 - alditol oxidase
for references in articles please use BRENDA:EC1.1.3.41
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.41 alditol oxidase
IUBMB 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 .
The enzyme appears in viruses and cellular organisms
- 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
showSynonyms
alditol oxidase, hotaldo, more
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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
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: product identification by NMR
Products: product identification by NMR
?
(R)-1-phenyl-1,2-ethanediol + O2
mandelic acid + H2O2
-
Substrates: the enzyme is highly enantioselective for the oxidation of (R)-1-phenyl-1,2-ethanediol
Products: -
Products: -
?
1,4-butanediol + O2
?
-
Substrates: very poor substrate
Products: -
Products: -
?
1-phenyl-1,2-ethanediol + O2
?
-
Substrates: 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
Products: -
Products: -
?
xylitol + O2
D-xylose + H2O2
-
Substrates: best substrate
Products: -
Products: -
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(R)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(S)-1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
-
Substrates: -
Products: product identification by NMR
Products: product identification by NMR
?
1,2-pentanediol + O2
2-hydroxypentanoic acid + H2O2
-
Substrates: 50% conversion after 22 h
Products: -
Products: -
?
1,3-butanediol + O2
3-hydroxybutanal + H2O2
-
Substrates: -
Products: -
Products: -
?
1,3-butanediol + O2
3-hydroxybutanal + H2O2
-
Substrates: -
Products: product identification by GC-MS
Products: product identification by GC-MS
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-ethanediol + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde + O2
D-glycerate + H2O2
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde + O2
D-glycerate + H2O2
-
Substrates: -
Products: -
Products: -
?
glycerol + O2
D-glyceraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
glycerol + O2
D-glyceraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
xylitol + O2
xylose + H2O2
Substrates: -
Products: -
Products: -
?
xylitol + O2
xylose + H2O2
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: AldO catalyzes the C1 oxidation of several polyols
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to perform oxidations of alcohols into aldehydes/ketones (single oxidation) and oxidations of alcohols into acids (double oxidation)
Products: -
Products: -
?
additional information
?
-
-
Substrates: AldO catalyzes the C1 oxidation of several polyols
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
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, 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
-
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
68
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
-
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
42
4-pentene-1,2-diol
-
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
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
0.1
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 25°C, recombinant enzyme
0.74
(R)-1-phenyl-1,2-ethanediol
pH 7.5, 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, 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
-
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
0.1
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
-
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
0.35
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
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