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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

Reaction

5-(dihydroxymethyl)furan-2-carbaldehyde
+
O2
=
5-formylfuran-2-carboxylate
 +
H2O2

Synonyms

5-hydroxymethylfurfural oxidase, AAO, AOX1, GaoB, Glox2, Glox3, GLRG_02805, HFMO, HMF oxidase, HMF/furfural oxidoreductase, HmfH, HMFO, MPQ_0130

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.47 5-(hydroxymethyl)furfural oxidase

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
-
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
V465T/W466H
significant improvement of conversion rate
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