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Enzyme Nomenclature
Information on EC 1.1.3.47 - 5-(hydroxymethyl)furfural oxidase
for references in articles please use BRENDA:EC1.1.3.47
Word Map on EC 1.1.3.47
- 1.1.3.47
-
biocatalyst
-
2,5-furandicarboxylic
- methylovorus
- flavoprotein
-
biotransformation
-
oxidases
-
one-pot
-
whole-cell
-
bio-based
-
cupriavidus
- terephthalate
- biofuel production
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.3.47
-
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RECOMMENDED NAME
GeneOntology No.
5-(hydroxymethyl)furfural oxidase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-(dihydroxymethyl)furan-2-carbaldehyde + O2 = 5-formylfuran-2-carboxylate + H2O2
(1c)
-
-
-
5-(dihydroxymethyl)furan-2-carboxylate + O2 = furan-2,5-dicarboxylate + H2O2
(1e)
-
-
-
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O = furan-2,5-dicarboxylate + 3 H2O2
overall reaction
-
-
-
5-(hydroxymethyl)furfural + O2 = furan-2,5-dicarbaldehyde + H2O2
(1a)
-
-
-
5-formylfuran-2-carboxylate + H2O = 5-(dihydroxymethyl)furan-2-carboxylate
(1d), spontaneous
-
-
-
furan-2,5-dicarbaldehyde + H2O = 5-(dihydroxymethyl)furan-2-carbaldehyde
(1b), spontaneous
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
5-(hydroxymethyl)furfural:oxygen oxidoreductase
The enzyme, characterized from the bacterium Methylovorus sp. strain MP688, is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural. The enzyme acts only on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation [3]. The enzyme has a broad substrate range that overlaps with EC 1.1.3.7, aryl-alcohol oxidase.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
mutants with a disrupted hmfH gene accumulate 5-hydroxymethylfuroic acid when cultured in the presence of 5-(hydroxymethyl)furfural
metabolism
physiological function
evolution
the enzyme is a member of the glucosemethanol-choline oxidase (GMC) oxidoreductase superfamily and the AAO family. Phylogenetic analysis of the AAOs in Pleurotus ostreatous revealed that they cluster into two groups
evolution
-
the enzyme is a member of the glucosemethanol-choline oxidase (GMC) oxidoreductase superfamily and the AAO family. Phylogenetic analysis of the AAOs in Pleurotus ostreatous revealed that they cluster into two groups
-
metabolism
-
the enzyme is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural
metabolism
the enzyme is involved in degradation of 5-(hydroxymethyl)furfural
metabolism
the enzyme is important in the 5-hydroxymethylfurfural degradation pathway, verview
physiological function
the enzyme is involved in the degradation of 5-hydroxymethylfurfural. Two enzymes groups, which belong to the ligninolytic system, aryl-alcohol oxidase and a dehydrogenase, are involved in this process
physiological function
the enzyme is involved in lignin degradation. Within this multienzymatic process, which enables the recycling of carbon fixed by photosynthesis in land ecosystems, AAO reduces O2, providing the H2O2 required by ligninolytic peroxidases to oxidize the recalcitrant lignin polymer
physiological function
-
the enzyme is involved in the degradation of 5-hydroxymethylfurfural. Two enzymes groups, which belong to the ligninolytic system, aryl-alcohol oxidase and a dehydrogenase, are involved in this process
-
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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
2,5-hydroxymethylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
very low activity
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
-
?
5-formylfuran-2-carboxylate + H2O
5-(dihydroxymethyl)furan-2-carboxylate
-
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-hydroxymethylfurancarboxylic acid + H2O2
-
-
-
?
furan-2,5-dicarbaldehyde + H2O
5-(dihydroxymethyl)furan-2-carbaldehyde
-
-
-
-
?
2,5-diformylfuran + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
?
5-(dihydroxymethyl)furan-2-carbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
-
-
-
?
5-(dihydroxymethyl)furan-2-carbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
spontaneous formation of 5-(dihydroxymethyl)furan-2-carboxylate from 5-formylfuran-2-carboxylate
-
?
5-(dihydroxymethyl)furan-2-carbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
-
spontaneous formation of 5-(dihydroxymethyl)furan-2-carboxylate from 5-formylfuran-2-carboxylate
-
?
5-(dihydroxymethyl)furan-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
-
-
?
5-(dihydroxymethyl)furan-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
-
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
overall reaction
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
overall reaction. the enzyme is involved in degradation of 5-(hydroxymethyl)furfural
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
overall reaction
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
-
overall reaction
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
-
the enzyme is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
spontaneous formation of 5-(dihydroxymethyl)furan-2-carbaldehyde from furan-2,5-dicarbaldehyde
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
spontaneous formation of 5-(dihydroxymethyl)furan-2-carbaldehyde from furan-2,5-dicarbaldehyde
-
?
additional information
?
-
-
the enzyme has a broad substrate range that overlaps with EC 1.1.3.7, aryl-alcohol oxidase
-
-
-
additional information
?
-
the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid
-
-
-
additional information
?
-
enzyme AAO is also able to oxidize some furanic compounds such as 5-hydroxymethylfurfural (HMF) and 2,5-diformylfuran (DFF), it has very low activity on 2,5-hydroxymethylfurancarboxylic acid, no activity with 2,5-formylfurancarboxylic acid. NMR analysis of the compounds
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
5-(dihydroxymethyl)furan-2-carbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
-
-
-
?
5-(dihydroxymethyl)furan-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
-
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
-
?
5-formylfuran-2-carboxylate + H2O
5-(dihydroxymethyl)furan-2-carboxylate
-
-
-
-
?
furan-2,5-dicarbaldehyde + H2O
5-(dihydroxymethyl)furan-2-carbaldehyde
-
-
-
-
?
additional information
?
-
O94219
the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid
-
-
-
2,5-diformylfuran + O2
2,5-furandicarboxylic acid + H2O2
E5CZV8
-
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
D5KB61
overall reaction. the enzyme is involved in degradation of 5-(hydroxymethyl)furfural
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
-
overall reaction
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
-
the enzyme is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W466F, at pH 7.5 and 25°C
0.28
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V367R, at pH 7.5 and 25°C
0.29
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V367K, at pH 7.5 and 25°C
0.72
4-Hydroxy-3-methoxybenzyl alcohol
-
wild type enzyme, at pH 7.5 and 25°C
0.82
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme H467A, at pH 7.5 and 25°C
0.92
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V465A, at pH 7.5 and 25°C
1
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W466A, at pH 7.5 and 25°C
1.1
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W369A, at pH 7.5 and 25°C
1.2
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme F434A, at pH 7.5 and 25°C
1.8
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme M103A, at pH 7.5 and 25°C
2
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme N511A, at pH 7.5 and 25°C
0.21
5-formylfuran-2-carboxylate
-
mutant enzyme V367R/W466F, at pH 7.5 and 25°C
1.4
5-formylfuran-2-carboxylate
-
mutant enzyme V367R, at pH 7.5 and 25°C
3
5-formylfuran-2-carboxylate
-
mutant enzyme W466F, at pH 7.5 and 25°C
4
5-formylfuran-2-carboxylate
-
Km above 4.0 mM, wild type enzyme, at pH 7.5 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0047
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme H467A, at pH 7.5 and 25°C
0.75
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W466A, at pH 7.5 and 25°C
1
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme N511A, at pH 7.5 and 25°C
1.5
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V465A, at pH 7.5 and 25°C
1.7
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W466F, at pH 7.5 and 25°C
3.3
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme M103A, at pH 7.5 and 25°C
4.3
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W369A, at pH 7.5 and 25°C
5.1
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V367K, at pH 7.5 and 25°C
6
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V367R, at pH 7.5 and 25°C
15
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme F434A, at pH 7.5 and 25°C
21
4-Hydroxy-3-methoxybenzyl alcohol
-
wild type enzyme, at pH 7.5 and 25°C
0.056
5-formylfuran-2-carboxylate
-
mutant enzyme V367R, at pH 7.5 and 25°C
0.079
5-formylfuran-2-carboxylate
-
mutant enzyme W466F, at pH 7.5 and 25°C
0.46
5-formylfuran-2-carboxylate
-
mutant enzyme V367R/W466F, at pH 7.5 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0057
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme H467A, at pH 7.5 and 25°C
0.55
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme N511A, at pH 7.5 and 25°C
0.75
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W466A, at pH 7.5 and 25°C
1.6
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V465A, at pH 7.5 and 25°C
1.8
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme M103A, at pH 7.5 and 25°C
3.9
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W369A, at pH 7.5 and 25°C
8.5
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme W466F, at pH 7.5 and 25°C
12
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme F434A, at pH 7.5 and 25°C
18
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V367K, at pH 7.5 and 25°C
21
4-Hydroxy-3-methoxybenzyl alcohol
-
mutant enzyme V367R, at pH 7.5 and 25°C
29
4-Hydroxy-3-methoxybenzyl alcohol
-
wild type enzyme, at pH 7.5 and 25°C
0.005
5-formylfuran-2-carboxylate
-
wild type enzyme, at pH 7.5 and 25°C
0.026
5-formylfuran-2-carboxylate
-
mutant enzyme W466F, at pH 7.5 and 25°C
0.041
5-formylfuran-2-carboxylate
-
mutant enzyme V367R, at pH 7.5 and 25°C
2.2
5-formylfuran-2-carboxylate
-
mutant enzyme V367R/W466F, at pH 7.5 and 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 16-22% (w/v) PEG3350 and 200 mM magnesium formate
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
when the structural genes of the furfural catabolic pathway are expressed in a heterologous host, Pseudomonas putida S12, they yield a strain capable of utilizing 5-(hydroxymethyl)furfural and furfural as sole carbon sources
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
5-hydroxymethylfurfural increases the expression, translation, and activity of enzymes involved in the ligninolytic system, including aryl-alcohol oxidases and a dehydrogenase
5-hydroxymethylfurfural increases the expression, translation, and activity of enzymes involved in the ligninolytic system, including aryl-alcohol oxidases and a dehydrogenase
5-hydroxymethylfurfural increases the expression, translation, and activity of enzymes involved in the ligninolytic system, including aryl-alcohol oxidases and a dehydrogenase
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F434A
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
H467A
M103A
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
N511A
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
V367
-
the mutant shows increased activity with 5-formylfuran-2-carboxylate compared to the wild type enzyme
V367K
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
V367R/W466F
-
the mutant shows strongly increased activity with 5-formylfuran-2-carboxylate compared to the wild type enzyme
V465A
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
W369A
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
W466A
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
W466F
-
the mutant shows increased activity with 5-formylfuran-2-carboxylate compared to the wild type enzyme
H467A
-
catalysis of the mutant enzyme is severely reduced compared to that of the wild-type enzyme. With vanillyl alcohol as the substrate, the kcat value of the mutant enzyme is 4400 times lower than that of the wild-type enzyme
H467A
-
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
synthesis
-
biocatalytic production of furan-2,5-dicarboxylate, a biobased platform chemical for the production of polymers
biofuel production
current large-scale pretreatment processes for lignocellulosic biomass are generally accompanied by the formation of toxic degradation products, such as 5-hydroxymethylfurfural (HMF), which inhibit cellulolytic enzymes and fermentation by ethanol-producing yeast. Overcoming these toxic effects is a key technical barrier in the biochemical conversion of plant biomass to biofuels. Pleurotus ostreatus, a white-rot fungus, can efficiently degrade lignocellulose, and it can tolerate and metabolize HMF involving HMF oxidase (HMFO) encoded by HmfH
biofuel production
-
current large-scale pretreatment processes for lignocellulosic biomass are generally accompanied by the formation of toxic degradation products, such as 5-hydroxymethylfurfural (HMF), which inhibit cellulolytic enzymes and fermentation by ethanol-producing yeast. Overcoming these toxic effects is a key technical barrier in the biochemical conversion of plant biomass to biofuels. Pleurotus ostreatus, a white-rot fungus, can efficiently degrade lignocellulose, and it can tolerate and metabolize HMF involving HMF oxidase (HMFO) encoded by HmfH
-
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