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
-
multicolor
-
1,4-benzoquinone
-
chrysosporium
-
phanerochaete
-
white-rot
-
nivale
-
microdochium
-
l-sorbose
-
aldopyranoses
-
synthesis
-
1,5-anhydro-d-glucitol
-
flavinylated
-
ligninolytic
-
ochracea
-
glucose-methanol-choline
-
1,5-anhydroglucitol
-
peniophora
-
c4a-hydroperoxyflavin
-
biotechnology
-
food industry
-
energy production
-
biofuel production
-
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
-
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
KM Value
KM Value on EC 1.1.3.10 - pyranose oxidase
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180
D-ribose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
3.43
ferricyanide
substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.187
ferrocenium ion
using D-glucose as cosubstrate, at 30°C, pH 6.5
0.0052
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0071
1,4-benzoquinone
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0089
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.01
1,4-benzoquinone
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.013
1,4-benzoquinone
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.027
1,4-benzoquinone
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.029
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.029
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.032
1,4-benzoquinone
L537W/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.033
1,4-benzoquinone
using D-glucose as cosubstrate, at 30°C, pH 6.5
0.036
1,4-benzoquinone
L537W mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.037
1,4-benzoquinone
L537G/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.038
1,4-benzoquinone
L537W/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.04
1,4-benzoquinone
E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.04
1,4-benzoquinone
L537G/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.042
1,4-benzoquinone
substrate 1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 4.5
0.043
1,4-benzoquinone
-
V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.048
1,4-benzoquinone
L537G mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.049
1,4-benzoquinone
E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.052
1,4-benzoquinone
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.065
1,4-benzoquinone
wild-type, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.072
1,4-benzoquinone
-
V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.072
1,4-benzoquinone
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.072
1,4-benzoquinone
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.078
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.11
1,4-benzoquinone
substrate 1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.12
1,4-benzoquinone
-
with D-glucose as cosubstrate, at pH 6.5 and 37°C
0.13
1,4-benzoquinone
L537W mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.136
1,4-benzoquinone
E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.137
1,4-benzoquinone
L537W/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.14
1,4-benzoquinone
L537W/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.14
1,4-benzoquinone
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.15
1,4-benzoquinone
L537G/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.155
1,4-benzoquinone
L537G/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.176
1,4-benzoquinone
L537G mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.182
1,4-benzoquinone
E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.24
1,4-benzoquinone
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.241
1,4-benzoquinone
wild-type, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.28
1,4-benzoquinone
-
V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.3
1,4-benzoquinone
-
soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0
0.37
1,4-benzoquinone
-
V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.18
1,4-benzoquinone
-
V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.5 - 2
1,4-benzoquinone
-
V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.07
-
pH 6.5, substrate: D-glucose
0.09
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical
substrate 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.051
substrate 2,6-dichloroindophenol (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.187
2,6-dichloroindophenol
using D-glucose as cosubstrate, at 30°C, pH 6.5
1.59
2,6-dimethyl-1,4-benzoquinone
substrate 2,6-dimethyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.31
substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
79
2-deoxy-D-glucose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
99.3
2-deoxy-D-glucose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
0.21
substrate 2-methoxy-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.51
2-methyl-1,4-benzoquinone
substrate 2-methyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
22.1
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
68
D-allose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
103
substrate D-fructose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.093
T169G/E542K/V546C, mutant, 30°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.19
D-galactose
T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.23
D-galactose
wild-type, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.25
D-galactose
wild-type, mutant, 30°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.4
D-galactose
-
V546C/T169G mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.4
D-galactose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
0.86
D-galactose
-
V546C/T169G/L537W mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.983
D-galactose
V546P/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.66
D-galactose
T169G/E542K/V546C, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
2.45
D-galactose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
2.45
D-galactose
mutant enzyme H450G, pH and temperature not specified in the publication
2.48
D-galactose
T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.48
D-galactose
mutant enzyme T169G, pH and temperature not specified in the publication
2.76
D-galactose
T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
2.94
D-galactose
substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
3.1
D-galactose
-
mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 25°C
3.56
D-galactose
T169N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
3.87
D-galactose
E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
3.87
D-galactose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
4.26
D-galactose
E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.19
D-galactose
L537W/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.49
D-galactose
L537W/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.77
D-galactose
L537G/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
6.01
D-galactose
L537G/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
6.1
D-galactose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
6.1
D-galactose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
6.3
D-galactose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
6.38
D-galactose
R472G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
7.21
D-galactose
R472L, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
7.39
D-galactose
N593R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
7.8
D-galactose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
7.94
D-galactose
wild-type, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
8.09
D-galactose
wild-type, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
8.79
D-galactose
wild-type, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
8.79
D-galactose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
8.79
D-galactose
wild type enzyme, pH and temperature not specified in the publication
9.27
D-galactose
H548R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
9.4
D-galactose
L537W mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
9.47
D-galactose
L537G mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
9.89
D-galactose
H548I, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
10
D-galactose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
10.4
D-galactose
V546C/T169N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
12
D-galactose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
12
D-galactose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
12.9
D-galactose
T169S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
13
D-galactose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
13
D-galactose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
14.6
D-galactose
wild-type, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
15
D-galactose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 25°C
16
D-galactose
-
mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 25°C
16.2
D-galactose
-
mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 25°C
24.6
D-galactose
-
V546C/E542K mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
26
D-galactose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
29
D-galactose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
29.4
D-galactose
V546G/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
34
D-galactose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
46.2
D-galactose
V546C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
46.2
D-galactose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
46.2
D-galactose
mutant enzyme V546C, pH and temperature not specified in the publication
50
D-galactose
-
mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 25°C
50.6
D-galactose
V546P, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
101
D-galactose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
200
D-galactose
V546G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
750
D-galactose
Q448S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
940
D-galactose
Q448N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1260
D-galactose
Q448C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.018
mutant enzyme L547R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.042
D-glucose
mutant enzyme L545C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.046
D-glucose
mutant enzyme L545C, with O2 as electron acceptor, at pH 6.5 and 30°C
0.057
D-glucose
mutant enzyme Q448H, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.082
D-glucose
mutant enzyme Q448H, with O2 as electron acceptor, at pH 6.5 and 30°C
0.092
D-glucose
mutant enzyme T166R, with O2 as electron acceptor, at pH 6.5 and 30°C
0.12
D-glucose
mutant enzyme L545C, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.13
D-glucose
wild type enzyme, with O2 as electron acceptor, at pH 6.5 and 30°C
0.14
D-glucose
mutant enzyme N593C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.14
D-glucose
mutant enzyme T166R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.18
D-glucose
mutant enzyme N593C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
0.22
D-glucose
T169G/E542K/V546C, mutant, 30°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.23
D-glucose
mutant enzyme L547R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.24
D-glucose
mutant enzyme Q448H, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
0.24
D-glucose
wild type enzyme, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.25
D-glucose
wild type enzyme, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.31
D-glucose
T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.32
D-glucose
wild-type protein, 0.1 M ethanolamine buffer at pH 10.5
0.327
D-glucose
T169N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.35
D-glucose
recombinant protein with a hexa-histidine tag, 0.1 M ethanolamine buffer at pH 10.5
0.394
D-glucose
T169S, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.4
D-glucose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
0.4
D-glucose
wild-type, mutant, 30°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.4
D-glucose
mutant enzyme L547R, with O2 as electron acceptor, at pH 6.5 and 30°C
0.419
D-glucose
L537W/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.432
D-glucose
L537W/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.44
D-glucose
-
V546C/T169G mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.44
D-glucose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
0.441
D-glucose
L537G/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.487
D-glucose
L537G/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.489
D-glucose
E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.49
D-glucose
-
V546C/T169G/L537W mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.521
D-glucose
E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.521
D-glucose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.527
D-glucose
N593R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.56
D-glucose
mutant enzyme Q448H, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.6
D-glucose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
0.64
D-glucose
T169G/E542K/V546C, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.658
D-glucose
V546P/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.69
D-glucose
mutant enzyme T169G, pH and temperature not specified in the publication
0.691
D-glucose
T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.698
D-glucose
wild-type, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.72
D-glucose
mutant enzyme L545C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
0.749
D-glucose
L537W mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.76
D-glucose
wild-type, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.76
D-glucose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.77
D-glucose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.773
D-glucose
R472G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.78
D-glucose
wild-type, mutant, 50°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.8 - 11
D-glucose
H548I, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.81
D-glucose
mutant enzyme N593C, with 1 ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.84
D-glucose
substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.851
D-glucose
L537G mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.88
D-glucose
H548R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.886
D-glucose
R472L, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.9
D-glucose
-
mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.939
D-glucose
wild-type, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.939
D-glucose
wild type enzyme, pH and temperature not specified in the publication
0.952
D-glucose
V546C/T169N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.98
D-glucose
mutant enzyme N593C, with O2 as electron acceptor, at pH 6.5 and 30°C
0.984
D-glucose
V546G/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.987
D-glucose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.987
D-glucose
mutant enzyme H450G, pH and temperature not specified in the publication
0.99
D-glucose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
1.1
D-glucose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
1.13
D-glucose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 4°C
1.15
D-glucose
T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
1.18
D-glucose
wild-type, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
1.5
D-glucose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.5
D-glucose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.5 - 2
D-glucose
-
V546C/E542K mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.51
D-glucose
E542K with a hexa-histidine tag, 0.1 M ethanolamine buffer at pH 10.5
1.6
D-glucose
mutant enzyme T166R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
1.7
D-glucose
-
mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 4°C
1.7
D-glucose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.7
D-glucose
mutant enzyme L547R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
1.8
D-glucose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.9
D-glucose
-
O2 concentration constant, pH 7.0, absorbance at 420 nm resulting from the oxidation of diammonium-2,2'-azinobis-(3-ethylbenzthiazolin-6-sulfonic acid) by H2O2
1.9
D-glucose
wild type enzyme, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
2.1
D-glucose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.1
D-glucose
mutant enzyme T166R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
2.1
D-glucose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
2.2
D-glucose
V546P, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.3
D-glucose
-
wild type enzyme, at pH 6.5, temperature not specified in the publication
2.43
D-glucose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
2.43
D-glucose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
2.5
D-glucose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.5
D-glucose
-
mutant enzyme N593C, at pH 6.5, temperature not specified in the publication
3.06
D-glucose
V546C, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
3.06
D-glucose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
3.06
D-glucose
mutant enzyme V546C, pH and temperature not specified in the publication
3.2
D-glucose
-
O2 concentration constant, pH 7.0, calculated with kinetic equation
4.6
D-glucose
-
mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 4°C
5.7
D-glucose
V546G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
5.97
D-glucose
mutant enzyme H167A, pH and temperature not specified in the publication
28
D-glucose
Q448N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
30
D-glucose
Q448S, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
30
D-glucose
-
mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 4°C
45
D-glucose
-
pH 7.0, 25°C, reductive half-reaction, wild-type enzyme and mutant T169S
100
D-glucose
Q448C, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2 - 3
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
50
D-melibiose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
240
D-melibiose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
260
D-melibiose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
350
D-melibiose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
390
D-melibiose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1500
D-melibiose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.4
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
6.6
D-xylose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
20.9
D-xylose
substrate D-xylose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
73
D-xylose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.092
-
V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.092
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C
0.15
ferricenium hexafluorophosphate
-
V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.15
ferricenium hexafluorophosphate
-
mutant enzyme V546C/E542K, at pH 6.5 and 30°C
0.22
ferricenium hexafluorophosphate
-
V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.22
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C
0.29
ferricenium hexafluorophosphate
substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 8.0
0.31
ferricenium hexafluorophosphate
-
V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.31
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G, at pH 6.5 and 30°C
0.33
ferricenium hexafluorophosphate
substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.5
ferricenium hexafluorophosphate
-
V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.5
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G, at pH 6.5 and 30°C
1.06
ferricenium hexafluorophosphate
-
V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.054
L537G/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.063
ferricenium ion
L537W mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.068
ferricenium ion
E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.07
ferricenium ion
wild-type, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.072
ferricenium ion
L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.074
ferricenium ion
L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.086
ferricenium ion
L537G mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.09
ferricenium ion
L537W/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.183
ferricenium ion
E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.253
ferricenium ion
L537W mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.254
ferricenium ion
wild-type, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.281
ferricenium ion
L537W/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.289
ferricenium ion
L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.29
ferricenium ion
E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.296
ferricenium ion
L537G/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.319
ferricenium ion
E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.328
ferricenium ion
L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.408
ferricenium ion
L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.015
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.016
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.023
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.025
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.041
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.049
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.1
ferrocenium hexafluorophosphate
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.14
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.15
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.24
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.28
ferrocenium hexafluorophosphate
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.35
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.38
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.4
ferrocenium hexafluorophosphate
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.79
-
immobilized enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0
0.85
glucose
-
soluble enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0
14
L-arabinose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
2.9
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
5.4
L-sorbose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
23.5
L-sorbose
substrate L-sorbose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
50
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
261
methyl-beta-D-glucoside
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
0.03
-
wild type enzyme, using D-galactose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.04
O2
-
pH 5.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.04
O2
-
pH 8.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.07
O2
-
mutant enzyme T169S, using D-galactose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.09
O2
-
wild type enzyme, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.1
O2
-
pH 6.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.1
O2
-
pH 7.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.132
O2
-
glucose concentration constant, pH 7.0, calculated with kinetic equation
0.2
O2
-
pH 7.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.2
O2
-
mutant enzyme T169A, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.22
O2
-
D-glucose concentration constant, pH 7.0, absorbance at 420 nm resulting from the oxidation of diammonium-2,2'-azinobis-(3-ethylbenzthiazolin-6-sulfonic acid) by H2O2
0.3
O2
-
pH 5.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.4
O2
-
mutant enzyme T169A, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
0.5
O2
-
pH 8.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.9
O2
-
pH 6.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.99
O2
-
mutant enzyme T169S, using D-glucose as cosubstrate ,in 50 mM sodium phosphate (pH 7.0), at 4°C
1.22
O2
substrate O2 (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.32
O2
-
mutant enzyme T169N, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
3.7
O2
-
mutant enzyme T169G, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
4.5
O2
-
mutant enzyme T169G, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
4.8
O2
-
mutant enzyme T169N, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.64
tetrafluoro-1,4-benzoquinone
substrate tetrafluoro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
D-mannose, glucosamine, beta-lactose, sucrose and D-maltose lack response signal, higher maltooligosaccharides good substrates for pyranose 2-oxidase-based biosensor
-
additional information
additional information
-
kinetic parameters of the reaction measured (substrates D-glucose or 2-deoxy-D-glucose), pH 7.0
-
additional information
additional information
-
steady-state and pre-steady-state kinetics, and kinetic isotope effects, of oxidative half-reaction and overall reaction, overview
-
additional information
additional information
-
the steady-state kinetics of P2O can be classified as a ping pong bi-bi type, because the 2-keto-sugar product is released prior to the oxygen reaction, transient kinetics and isotope effects, overview
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