Information on EC 1.1.3.47 - 5-(hydroxymethyl)furfural oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.3.47
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RECOMMENDED NAME
GeneOntology No.
5-(hydroxymethyl)furfural oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-(dihydroxymethyl)furan-2-carbaldehyde + O2 = 5-formylfuran-2-carboxylate + H2O2
show the reaction diagram
(1c)
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5-(dihydroxymethyl)furan-2-carboxylate + O2 = furan-2,5-dicarboxylate + H2O2
show the reaction diagram
(1e)
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5-(hydroxymethyl)furfural + 3 O2 + 2 H2O = furan-2,5-dicarboxylate + 3 H2O2
show the reaction diagram
overall reaction
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5-(hydroxymethyl)furfural + O2 = furan-2,5-dicarbaldehyde + H2O2
show the reaction diagram
(1a)
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5-formylfuran-2-carboxylate + H2O = 5-(dihydroxymethyl)furan-2-carboxylate
show the reaction diagram
(1d), spontaneous
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furan-2,5-dicarbaldehyde + H2O = 5-(dihydroxymethyl)furan-2-carbaldehyde
show the reaction diagram
(1b), spontaneous
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Furfural degradation
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Microbial metabolism in diverse environments
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutants with a disrupted hmfH gene accumulate 5-hydroxymethylfuroic acid when cultured in the presence of 5-(hydroxymethyl)furfural
metabolism
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-phenylethanol + O2
acetophenone + H2O2
show the reaction diagram
-
-
-
-
?
(S)-1-phenylethanol + O2
acetophenone + H2O2
show the reaction diagram
-
-
-
-
?
4-(hydroxymethyl)benzaldehyde + O2 + H2O
?
show the reaction diagram
-
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
5-(dihydroxymethyl)furan-2-carbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
show the reaction diagram
5-(dihydroxymethyl)furan-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
show the reaction diagram
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
show the reaction diagram
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
show the reaction diagram
5-formylfuran-2-carboxylate + H2O
5-(dihydroxymethyl)furan-2-carboxylate
show the reaction diagram
-
-
-
-
?
furan-2,5-dicarbaldehyde + H2O
5-(dihydroxymethyl)furan-2-carbaldehyde
show the reaction diagram
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-
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?
terephthaldehyde + O2 + H2O
?
show the reaction diagram
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?
additional information
?
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the enzyme has a broad substrate range that overlaps with EC 1.1.3.7, aryl-alcohol oxidase
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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
5-(dihydroxymethyl)furan-2-carbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
show the reaction diagram
-
-
-
-
?
5-(dihydroxymethyl)furan-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
show the reaction diagram
-
-
-
-
?
5-(hydroxymethyl)furfural + 3 O2 + 2 H2O
furan-2,5-dicarboxylate + 3 H2O2
show the reaction diagram
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
show the reaction diagram
-
-
-
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?
5-formylfuran-2-carboxylate + H2O
5-(dihydroxymethyl)furan-2-carboxylate
show the reaction diagram
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-
-
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?
furan-2,5-dicarbaldehyde + H2O
5-(dihydroxymethyl)furan-2-carbaldehyde
show the reaction diagram
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-
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
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the flavin cofactor is dissociable
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20 - 98
(S)-1-phenylethanol
0.15
4-(Hydroxymethyl)benzaldehyde
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pH 7.0, 25C
0.2 - 2
4-Hydroxy-3-methoxybenzyl alcohol
1.4
5-(hydroxymethyl)furfural
0.21 - 4
5-formylfuran-2-carboxylate
1.7
furan-2,5-dicarbaldehyde
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pH 7.0, 25C
0.085
terephthaldehyde
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pH 7.0, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.011
(S)-1-phenylethanol
8.6
4-(Hydroxymethyl)benzaldehyde
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pH 7.0, 25C
0.0047 - 21
4-Hydroxy-3-methoxybenzyl alcohol
9.9
5-(hydroxymethyl)furfural
0.056 - 0.46
5-formylfuran-2-carboxylate
1.6
furan-2,5-dicarbaldehyde
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pH 7.0, 25C
1.3
terephthaldehyde
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pH 7.0, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001 - 0.00055
(S)-1-phenylethanol
57
4-(Hydroxymethyl)benzaldehyde
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pH 7.0, 25C
0.0057 - 29
4-Hydroxy-3-methoxybenzyl alcohol
7 - 7.1
5-(hydroxymethyl)furfural
0.005 - 2.2
5-formylfuran-2-carboxylate
0.94
furan-2,5-dicarbaldehyde
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pH 7.0, 25C
15
terephthaldehyde
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pH 7.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methylovorus sp. (strain MP688)
Methylovorus sp. (strain MP688)
Methylovorus sp. (strain MP688)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
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x * 70000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 70000, SDS-PAGE
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
HisTrap column chromatography and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F434A
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the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
M103A
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the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
N511A
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the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
V367
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the mutant shows increased activity with 5-formylfuran-2-carboxylate compared to the wild type enzyme
V367K
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the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
V367R/W466F
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the mutant shows strongly increased activity with 5-formylfuran-2-carboxylate compared to the wild type enzyme
V465A
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the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
W369A
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the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
W466A
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the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
W466F
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the mutant shows increased activity with 5-formylfuran-2-carboxylate compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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biocatalytic production of furan-2,5-dicarboxylate, a biobased platform chemical for the production of polymers