Any feedback?
Information on EC 1.1.3.41 - alditol oxidase
for references in articles please use BRENDA:EC1.1.3.41Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 .
Specify your search results
Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
alditol oxidase, hotaldo, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AldO
HotAldO
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
177322-52-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
0.1
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