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Information on EC 1.1.3.47 - 5-(hydroxymethyl)furfural oxidase
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1.1.3.47 5-(hydroxymethyl)furfural oxidaseIUBMB Comments
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 . The enzyme has a broad substrate range that overlaps with EC 1.1.3.7, aryl-alcohol oxidase.
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Word Map
- 1.1.3.47
- synthesis
-
2,5-furandicarboxylic
-
biocatalyst
-
bio-based
-
biocatalytic
- oxidases
- putida
- methylovorus
- basilensis
-
fed-batch
-
petroleum-based
- terephthalate
-
cupriavidus
- flavin
- ornithinolytica
-
biomass-derived
-
raoultella
- eugenol
-
enantioselective
-
polyesters
-
cosolvents
-
one-pot
-
fusing
- biotechnology
- biofuel production
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
3
+
2
=
+
3
Synonyms
5-hydroxymethylfurfural oxidase, AAO, HFMO, HMF oxidase, HMF/furfural oxidoreductase, HmfH, HMFO, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAO
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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 SOURCE
PATHWAYS
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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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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-(hydroxymethyl)furan-2-carboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
very low activity
-
-
?
5-formylfuran-2-carboxylate + H2O
5-(dihydroxymethyl)furan-2-carboxylate
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-hydroxymethylfurancarboxylic acid + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic 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-(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
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 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 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
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
?
-
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
-
-
-
?
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
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
20
(S)-1-phenylethanol
mutant enzyme W466A, at pH 7.5 and 25°C
98
(S)-1-phenylethanol
mutant enzyme W466F, at pH 7.5 and 25°C
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
0.01
(S)-1-phenylethanol
mutant enzyme W466F, at pH 7.5 and 25°C
0.011
(S)-1-phenylethanol
mutant enzyme W466A, at pH 7.5 and 25°C
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
0.0001
(S)-1-phenylethanol
mutant enzyme W466F, at pH 7.5 and 25°C
0.00055
(S)-1-phenylethanol
mutant enzyme W466A, at pH 7.5 and 25°C
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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 degradation of 5-(hydroxymethyl)furfural
metabolism
the enzyme is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural
metabolism
the enzyme is important in the 5-hydroxymethylfurfural degradation pathway, verview
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
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A6J5BCV3_9BURK
573
0
61874
TrEMBL
-
A0A2S6QEV9_9PROT
566
0
62396
TrEMBL
-
A0A7W5Z5G9_9RHIZ
562
0
60183
TrEMBL
-
A0A2S6U1Z2_9PROT
570
0
62280
TrEMBL
-
A0A7Y9TGR9_9RHIZ
568
0
60829
TrEMBL
-
A0A6J5A2I5_9BURK
566
0
61177
TrEMBL
-
A0A2S6QD34_9PROT
582
0
64157
TrEMBL
-
A0A2S6U1Y0_9PROT
96
0
10263
TrEMBL
-
B1FZU1_PARG4
Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)
565
0
60476
TrEMBL
-
A0A2S6T6A2_9PROT
449
0
50125
TrEMBL
-
A0A6J5KAC7_9BURK
566
0
61050
TrEMBL
-
A0A2S6QES4_9PROT
567
0
62242
TrEMBL
-
A0A6J5K0Y4_9BURK
573
0
61872
TrEMBL
-
A0A2S6TXM6_9PROT
571
0
63056
TrEMBL
-
A0A6J5GT55_9BURK
608
0
65024
TrEMBL
-
A0A7Y9TRN0_9RHIZ
568
0
60829
TrEMBL
-
O94219_PLEER
593
0
63709
TrEMBL
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
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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PROTEIN VARIANTS
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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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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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
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dijkman, W.; Groothuis, D.; Fraaije, M.
Enzyme-catalyzed oxidation of 5-hydroxymethylfurfural to furan-2,5-dicarboxylic acid
Angew. Chem. Int. Ed. Engl.
53
6515-6518
2014
Methylovorus sp. MP688 (E4QP00)
brenda
Dijkman, W.; Fraaije, M.
Discovery and characterization of a 5-hydroxymethylfurfural oxidase from Methylovorus sp. strain MP688
Appl. Environ. Microbiol.
80
1082-1090
2014
Methylovorus sp. MP688 (E4QP00), Methylovorus sp. MP688
brenda
Koopman, F.; Wierckx, N.; De Winde, J.; Ruijssenaars, H.
Identification and characterization of the furfural and 5-(hydroxymethyl)furfural degradation pathways of Cupriavidus basilensis HMF14
Proc. Natl. Acad. Sci. USA
107
4919-4924
2010
Cupriavidus basilensis (D5KB61)
brenda
Dijkman, W.; Binda, C.; Fraaije, M.; Mattevi, A.
Structure-based enzyme tailoring of 5-hydroxymethylfurfural oxidase
ACS Catal.
5
1833-1839
2015
Methylovorus sp. MP688 (E4QP00)
-
brenda
Feldman, D.; Kowbel, D.J.; Glass, N.L.; Yarden, O.; Hadar, Y.
Detoxification of 5-hydroxymethylfurfural by the Pleurotus ostreatus lignolytic enzymes aryl alcohol oxidase and dehydrogenase
Biotechnol. Biofuels
8
63
2015
Pleurotus ostreatus (E5CZV8), Pleurotus ostreatus PC9 (E5CZV8)
brenda
Ferreira, P.; Hernandez-Ortega, A.; Lucas, F.; Carro, J.; Herguedas, B.; Borrelli, K.W.; Guallar, V.; Martinez, A.T.; Medina, M.
Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
FEBS J.
282
3091-3106
2015
Pleurotus eryngii (O94219)
brenda
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