1.1.3.47: 5-(hydroxymethyl)furfural oxidase
This is an abbreviated version!
For detailed information about 5-(hydroxymethyl)furfural oxidase, go to the full flat file.
Word Map on EC 1.1.3.47
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1.1.3.47
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synthesis
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2,5-furandicarboxylic
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biocatalyst
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bio-based
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biocatalytic
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oxidases
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putida
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methylovorus
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basilensis
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fed-batch
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petroleum-based
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terephthalate
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cupriavidus
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flavin
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ornithinolytica
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biomass-derived
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raoultella
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eugenol
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enantioselective
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polyesters
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cosolvents
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one-pot
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fusing
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biotechnology
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biofuel production
- 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
Reaction
Synonyms
5-hydroxymethylfurfural oxidase, AAO, AOX1, GaoB, Glox2, Glox3, GLRG_02805, HFMO, HMF oxidase, HMF/furfural oxidoreductase, HmfH, HMFO, MPQ_0130
ECTree
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Engineering
Engineering on EC 1.1.3.47 - 5-(hydroxymethyl)furfural oxidase
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Y334F
mutant exhibits specific activities comparable to the wild-type for carbohydrates, diols, aryl alcohols, 5-hydroxymethylfurfural and 5-hydroxymethyl-2-furancarboxylic acid
Y334W
mutant exhibits increased specific activity toward carbohydrates and decreased activity toward diols, aryl alcohols, and furans
Y334F
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mutant exhibits specific activities comparable to the wild-type for carbohydrates, diols, aryl alcohols, 5-hydroxymethylfurfural and 5-hydroxymethyl-2-furancarboxylic acid
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Y334W
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mutant exhibits increased specific activity toward carbohydrates and decreased activity toward diols, aryl alcohols, and furans
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F434A
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
H467A
I73V/H74Y/G356H/V367L/T414K/A419Y/A435E
most thermostable variant isolated with an improvement of melting temperature of 12 degrees compared to wild-type
I73V/H74Y/G356H/V367R/T414K/A419Y/A435E/W466F
introduction of mutation W466F to mutant I73V/H74Y/G356H/V367L/T414K/A419Y/A435E leads to a decrease in thermostability but improved synthesis of furan-2,5-dicarboxylate. At 25°C, an almost full conversion in 24 h can be achieved
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
synthesis
expression of HMFO and HMF/furfural oxidoreductase HmfH from Cupriavidus basilensis HMF14 in Raoultella ornithinolytica BF60 results in an increase in 2,5-furandicarboxylic acid production from 51.0 to 93.6 mM, and the molar conversion ratio of 5-hydroxymethylfurfural to 2,5-furandicarboxylic acid increases from 51.0 to 93.6%
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
V465A
the mutant shows reduced activity with 4-hydroxy-3-methoxybenzyl alcohol compared to the wild type enzyme
V465S
V465T
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
F397Y
mutant shows improved production of 2,5-furandicarboxylic acid, with 70% yield
F501H
mutant shows improved production of 2,5-furandicarboxylic acid, with 97% yield
H91N/L170M
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M/F501W
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M/I500M/F501W
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
I500M
mutant shows improved production of 2,5-furandicarboxylic acid, with 80% yield
I500M/F501 W
mutant shows improved production of 2,5-furandicarboxylic acid, reaching a total turnover number over 16,000 in presence of 15 mM 5-hydroxymethylfurfural
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
the mutant shows strongly increased activity with 5-formylfuran-2-carboxylate compared to the wild type enzyme
V465S
the active site is additionally enlarged by a Thr residue. This residue establishes a hydrogen-bonding interaction with the substrates and allows for enantioselective oxidation of a range of sec-thiols
significant improvement of conversion rate and enantioselectivity with sec-allylic alcohols
V465T
the active site is additionally enlarged by a Thr residue. This residue establishes a hydrogen-bonding interaction with the substrates and allows for enantioselective oxidation of a range of sec-thiols