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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
-
bio-based
- terephthalate
- methylovorus
- flavoprotein
-
one-pot
-
cupriavidus
-
whole-cell
-
oxidases
-
biotransformation
- synthesis
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The enzyme appears in viruses and cellular organisms
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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
malfunction
mutants with a disrupted hmfH gene accumulate 5-hydroxymethylfuroic acid when cultured in the presence of 5-(hydroxymethyl)furfural
metabolism
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
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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
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
-
?
5-formylfuran-2-carboxylate + H2O
5-(dihydroxymethyl)furan-2-carboxylate
-
-
-
-
?
furan-2,5-dicarbaldehyde + H2O
5-(dihydroxymethyl)furan-2-carbaldehyde
-
-
-
-
?
additional information
?
-
-
the enzyme has a broad substrate range that overlaps with EC 1.1.3.7, aryl-alcohol oxidase
-
-
-
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
-
?
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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
-
-
-
-
?
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
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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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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
synthesis
-
biocatalytic production of furan-2,5-dicarboxylate, a biobased platform chemical for the production of polymers
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.3.47)
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