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1.1.3.10: pyranose oxidase

This is an abbreviated version!
For detailed information about pyranose oxidase, go to the full flat file.

Word Map on EC 1.1.3.10

Reaction

D-glucose
+
O2
=
2-dehydro-D-glucose
+
H2O2

Synonyms

C-2 specific pyranose-2-oxidase, carbohydrate oxidase, glucose 2-oxidase, glucose-2-oxidase, P2O, P2Ox, POX, PROD, PyOx, pyranose 2-Oxidase, pyranose oxidase, pyranose-2-oxidase, pyranose/oxygen 2-oxidoreductase, pyranose: oxygen 2-oxidoreductase, pyranose:oxygen 2-oxidoreductase, pyranose:oxygen-2-oxidoreductase, TmP2Ox

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.10 pyranose oxidase

Engineering

Engineering on EC 1.1.3.10 - pyranose oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E540K
mutant with increased thermo- and pH-stability compared with wild-type, concomitantly with increased catalytic efficiencies (turnover number/KM-value) for D-xylose and L-sorbose
K312E
mutant enzyme with significant improvements with respect to the ratio of turnover number to Km-value for D-glucose (5.3fold), methyl-beta-D-glucoside (2.0fold), D-galactose (4.8fold), D-xylose (59.9fold), and L-sorbose (69.9fold) compared with wild-type P2Ox
D452A/R472A
the mutant shows drastic effects on the binding constant for D-glucose
E542K
E542R
mutant, analysis of kinetic parameters
F454A
-
the mutant shows about 40fold reduced catalytic efficiency compared to the wild type enzyme
F454A/S455A/Y456A
the mutant shows decreased catalytic efficiency for D-glucose/O2 compared to the wild type enzyme
F454A/Y456A
the mutant shows decreased catalytic efficiency for D-glucose/O2 compared to the wild type enzyme
F454N
F454P
the mutant shows strongly decreased catalytic efficiency for D-glucose/O2 compared to the wild type enzyme
F454Y
-
the mutant shows about 3.5fold reduced catalytic efficiency compared to the wild type enzyme
H167A
H167A/H548A
-
site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H167A/H548D
-
site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H167A/H548N
-
site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H167A/H548R
H167A/H548S
-
site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H169S
-
site-directed mutagenesis, spectroscopic analysis and molecular dynamics of the T169S P2O-acetate complex
H450G
H450G/E542K/V546C
mutant shows catalytic efficiency for its substrate D-galactose that is increased 1.2fold compared to the wild type enzyme while kcat/KM for D-glucose is decreased to 17% of its original value
H450G/V546C
H450Q
the turnover number for the electron donor/acceptor substrate pair D-galactose/O2 is comparable to that of the wild type enzyme
H548A
H548D
-
site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD
H548I
mutant, analysis of kinetic parameters
H548N
H548R
H548S
-
site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD
L537G
mutant, analysis of kinetic parameters
L537G/E542K
mutant, analysis of kinetic parameters
L537G/E542R
mutant, analysis of kinetic parameters
L537W
mutant, analysis of kinetic parameters
L537W/E542K
mutant, analysis of kinetic parameters
L537W/E542R
mutant, analysis of kinetic parameters
L545C
L547R
N593C
N593H
-
site-directed mutagenesis, the enzyme contains a covalently linked FAD, similar to the wild-type enzyme
N593R
mutant, analysis of kinetic parameters
Q448C
mutant, analysis of kinetic parameters
Q448H
Q448N
mutant, analysis of kinetic parameters
Q448S
mutant, analysis of kinetic parameters
R472G
mutant, analysis of kinetic parameters
R472L
mutant, analysis of kinetic parameters
T166R
T169A
T169G
T169G/E542K/V546C
mutant, analysis of kinetic parameters and thermal stability
T169N
T169S
T196G/V546C
the mutant exhibits reduced D-glucose conversion and D-galactose conversion activities
V546C
V546C/E542K
-
mutant, analysis of kinetic parameters
V546C/T169G
-
mutant, analysis of kinetic parameters
V546C/T169G/L537W
-
mutant, analysis of kinetic parameters
V546C/T169N
mutant, analysis of kinetic parameters
V546G
mutant, analysis of kinetic parameters
V546G/T169G
mutant, analysis of kinetic parameters
V546P
mutant, analysis of kinetic parameters
V546P/T169G
mutant, analysis of kinetic parameters
Y456W
the turnover number for the electron donor/acceptor substrate pair D-galactose/O2 is comparable to that of the wild type enzyme
E539K
increase in catalytic activity, shift in optimum temperature by 10 degrees
K312E
increase in catalytic activity
K312E/E539K
increase in catalytic activity, shift in optimum temperature by 10 degrees
T166A/E539K
increase in catalytic activity
additional information