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
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1.1.3.10
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trametes
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multicolor
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1,4-benzoquinone
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chrysosporium
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phanerochaete
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white-rot
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nivale
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microdochium
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l-sorbose
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aldopyranoses
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synthesis
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1,5-anhydro-d-glucitol
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flavinylated
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ligninolytic
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ochracea
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glucose-methanol-choline
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1,5-anhydroglucitol
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peniophora
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c4a-hydroperoxyflavin
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biotechnology
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food industry
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energy production
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biofuel production
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analysis
- 1.1.3.10
- trametes
- multicolor
- 1,4-benzoquinone
- chrysosporium
- phanerochaete
-
white-rot
- nivale
-
microdochium
- l-sorbose
- aldopyranoses
- synthesis
- 1,5-anhydro-d-glucitol
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flavinylated
-
ligninolytic
- ochracea
-
glucose-methanol-choline
- 1,5-anhydroglucitol
- peniophora
-
c4a-hydroperoxyflavin
- biotechnology
- food industry
- energy production
- biofuel production
- analysis
Reaction
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
Advanced search results
Engineering
Engineering on EC 1.1.3.10 - pyranose oxidase
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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
F454A
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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
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the mutant shows about 3.5fold reduced catalytic efficiency compared to the wild type enzyme
H167A
H167A/H548A
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site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H167A/H548D
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site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H167A/H548N
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site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H167A/H548R
H167A/H548S
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site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
H169S
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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
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site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD
H548N
H548R
H548S
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site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD
L545C
L547R
N593C
N593H
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site-directed mutagenesis, the enzyme contains a covalently linked FAD, similar to the wild-type enzyme
Q448H
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
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/E539K
increase in catalytic activity, shift in optimum temperature by 10 degrees
additional information
E542K
the mutant is characterized by reduced KM values for both D-glucose and D-galactose and significantly increased stability
the apparent kcat value with D-glucose and O2 (fixed at a concentration of 0.256 mM, air saturation) as substrates decreases dramatically compared to the wild type enzyme
F454N
the mutant shows decreased catalytic efficiency for D-glucose/O2 compared to the wild type enzyme
H167A
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the mutant catalyzes the oxidation of D-glucose regiospecifically at the C2 position. The rate constant of flavin reduction decreases about 22fold compared to that of the wild type enzyme
H167A
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site-directed mutagenesis, reductive activity of the mutant is highly reduced compared to the wild-type enzyme, the mutation ablates the covalent histidyl-FAD linkage. The H167A mutant enzyme oxidizes D-glucose regiospecifically at the C2 position, similarly to the wild-type enzyme, but noncovalent flavin in H167A mainly decreases the flavin reduction rate constant by 22fold
H167A
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site-directed mutagenesis, reductive activity of the mutant is highly reduced compared to the wild-type enzyme, the mutation ablates the covalent histidyl-FAD linkage. The H167A mutant enzyme oxidizes D-glucose regiospecifically at the C2 position, similarly to the wild-type enzyme, but noncovalent flavin in H167A mainly decreases the flavin reduction rate constant by 22fold. In the crystal complex of the H167A mutant and 2FG (C3 oxidation), the substrate-recognition loop swings further away from the active site to assume the open conformation, whereas in the C2 oxidation complex of the H167A mutant and 3FG, the gating segment (residues 452-456) swings towards the active site to provide a binding pocket for the substrate
H167A
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site-directed mutagenesis, the covalent linkag of the isoalloxazine ring of the cofactor FAD to His167 is destroyed, molecular dynamics, overview
H167A
the P2O mutant in complex with the slow substrate 2-deoxy-2-fluoro-D-glucose shows a substrate-binding mode compatible with oxidation at C3. To accommodate the sugar, a gating segment, 454FSY456, in the substrate recognition loop partly unfolded to create a spacious and more polar active site that is distinct from the closed state of P2O. With 3-deoxy-3-fluoro-D-glucose the mutant prefers C2 oxidation, crystal structure of the ordered complex of P2O H167A with at 1.35 A resolution, overview
H167A
the mutant exhibits reduced D-glucose conversion and no D-galactose conversion activity
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site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently linked FAD, highest reductive activity at pH 10.5
H167A/H548R
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site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD
the mutant shows a 3.6fold decrease in KM together with a 1.4fold increase in kcat for its substrate D-galactose and an overall improvement in the catalytic efficiency by a factor of 5 compared to the wild type enzyme
H450G
the mutant exhibits reduced D-glucose conversion and improved D-galactose conversion activity
mutant with increased activity with D-galactose, high activity with D-glucose, and considerably increased stability for the latter variant
H450G/V546C
the mutant exhibits reduced D-glucose conversion and improved D-galactose conversion activity
H548A
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site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD
H548N
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site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD
H548R
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site-directed mutagenesis, reductive activity of the mutant is slightly reduced compared to the wild-type enzyme, contains some noncovalently and mostly covalently linked FAD
L545C
pre-steady-state kinetics of the oxidative half-reaction show higher kinetic constants as compared to the wild-type. The variant immobilized on glassy carbon electrodes displays high catalytic efficiency. L545C performs best among the variants studied
L547R
pre-steady-state kinetics of the oxidative half-reaction show higher kinetic constants as compared to the wild-type. The variant immobilized on glassy carbon electrodes displays high catalytic efficiency
N593C
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the mutant shows a complete loss of the oxidase function with full preservation of substrate (dehydrogenase) activity
Q448H
pre-steady-state kinetics of the oxidative half-reaction show higher kinetic constants as compared to the wild-type. The variant immobilized on glassy carbon electrodes displays high catalytic efficiency
T166R
pre-steady-state kinetics of the oxidative half-reaction show higher kinetic constants as compared to the wild-type. The variant immobilized on glassy carbon electrodes displays high catalytic efficiency
T169A
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the mutant shows severely decreased catalytic efficiency for D-glucose and D-galactose compared to the wild type enzyme
T169A
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site-directed mutagenesis, the hydrogen bond between residue 169 and the N5 atom of FAD is absent, resulting in a change in the kinetic mechanism to one that consists of a ternary complex
T169A
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site-directed mutagenesis, the hydrogen bond between Thr169 and the N5 atom of FAD is absent in the mutant.The kinetic mechanism of the T169A mutant with D-glucose or D-galactose indicates that a 2-keto-sugar product remains bound at the active site during the oxidative half-reaction
T169G
the FAD content of the mutant enzyme is similar to the wild type enzyme
T169G
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the mutant shows decreased catalytic efficiency for D-glucose and D-galactose compared to the wild type enzyme
T169G
the mutant exhibits reduced D-glucose conversion and D-galactose conversion activities
T169N
the FAD content of the mutant enzyme is similar to the wild type enzyme
T169N
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the mutant shows decreased catalytic efficiency for D-glucose and increased catalytic efficiency for D-galactose compared to the wild type enzyme
T169S
the FAD content of the mutant enzyme is similar to the wild type enzyme
T169S
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the mutant shows increased kcat and Km values for D-glucose and D-galactose compared to the wild type enzyme
V546C
the mutant is characterized by elevated kcat values for both sugar substrates D-glucose and D-galactose, which is accompanied by elevated KM values
V546C
the mutant exhibits reduced D-glucose and D-galactose conversion activities
the deletion mutant DELTA454-456 shows 6fold lower kcat (D-galactose/O2), and 0.8fold elevated Km (D-galactose) value compared to the wild type enzyme
additional information
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the deletion mutant DELTA454-456 shows 6fold lower kcat (D-galactose/O2), and 0.8fold elevated Km (D-galactose) value compared to the wild type enzyme
additional information
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comparison the P2O active site in H167A, T169S or T169S-acetate complex with wild-type P2O-acetate complex, molecuar dynamics and spectroscopic analysi, detailed overview
additional information
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mutagenesis of Phe454 and Tyr456 results in inactive enzymes, indicating that this region is functionally important for P2O
additional information
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redox potential of wild-type and mutant enzymes, overview. Single mutants of H548 result in mixed populations of noncovalently bound and covalently linked FAD. Double mutants containing H167A are constructed, in which the covalent histidyl-FAD linkage is removed in addition to having the H548 mutation