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Enzyme Nomenclature
Information on EC 1.1.3.10 - pyranose oxidase
for references in articles please use BRENDA:EC1.1.3.10
Word Map on EC 1.1.3.10
- 1.1.3.10
- trametes
- multicolor
- 1,4-benzoquinone
- chrysosporium
- aldopyranoses
- synthesis
- l-sorbose
- nivale
-
microdochium
- phanerochaete
-
white-rot
-
coriolus
-
ligninolytic
-
flavinylated
- peniophora
- 1,5-anhydro-d-glucitol
-
2-keto
- 1,5-anhydroglucitol
-
c4a-hydroperoxyflavin
- biotechnology
- ochracea
- food industry
- energy production
- biofuel production
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.3.10
-
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RECOMMENDED NAME
GeneOntology No.
pyranose oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + O2 = 2-dehydro-D-glucose + H2O2
-
-
-
-
D-glucose + O2 = 2-dehydro-D-glucose + H2O2
investigation of the reaction mechanism by determining the rate constants
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D-glucose + O2 = 2-dehydro-D-glucose + H2O2
ping-pong reaction mechanism, but change in the enzyme kinetic mechanism from a ping-pong type mechanism at pH values below 7.0 to a ternary complex type mechanism at pH values above 7.0. The switching of reaction mechanism from the ping-pong to the ternary complex type may be resulting from the change of structural dynamics of the substrate loop in the T169A mutant or at higher pH values, overview
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D-glucose + O2 = 2-dehydro-D-glucose + H2O2
ping pong bi bi reaction mechanism, the catalytic reaction of P2O can be divided into a reductive half-reaction in which two electrons are transferred as a hydride equivalent from a sugar substrate to a flavin to generate reduced FAD and a 2-oxo-sugar, and an oxidative half-reaction in which two electrons are transferred from the reduced flavin to oxygen to form hydrogen peroxide, formation of C(4a)-hydroperoxyflavin was observed during enzyme turnovers, overview
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D-glucose + O2 = 2-dehydro-D-glucose + H2O2
ping pong bi bi reaction mechanism, sugar oxidation and flavin reduction activation and mechanism, regiospecificity and selectivity of sugar oxidation, overview. The 2-oxo-sugar product is released prior to the oxygen reaction, overview. The enzyme shows a hydride transfer mechanism in which there is stepwise formation of D-glucose alkoxide prior to the hydride transfer, and a C4a-hydroperoxyflavin as an intermediate during the oxidative half-reaction, the C4a-hydroperoxyflavin merely eliminates H2O2 to generate oxidized FAD. The breakage of the flavin N (5)-H bond controls the overall process of H2O2 elimination from C4a-hydroperoxyflavin
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D-glucose + O2 = 2-dehydro-D-glucose + H2O2
the enzyme shows a ping pong bi bi mechanism, a specialised bi bi mechanism in which substrate binding and release of products are ordered and the enzyme shuttles between a free and a substrate-modified intermediate conformation
-
D-glucose + O2 = 2-dehydro-D-glucose + H2O2
highly regioselective mechanism, overview. The different conformations of the 454FSY456 gating segment in the semiopen and closed states induce backbone and side-chain movements of Thr169 and Asp452 that add further differential stabilization to the individual states
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D-glucose + O2 = 2-dehydro-D-glucose + H2O2
the enzyme shows a ping pong bi bi mechanism, a specialised bi bi mechanism in which substrate binding and release of products are ordered and the enzyme shuttles between a free and a substrate-modified intermediate conformation
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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-
-
-
reduction
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-
-
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oxidation
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-
-
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SYSTEMATIC NAME
IUBMB Comments
pyranose:oxygen 2-oxidoreductase
A flavoprotein (FAD). Also oxidizes D-xylose, L-sorbose and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4.
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CAS REGISTRY NUMBER
COMMENTARY
37250-80-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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389649, 654180, 656544, 687890, 695870, 696332, 696791, 699076, 711239, 712500, 724369, 724753, 724979, 725776, 741113, 741252
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SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
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pyranose 2-oxidase, rather than glucose 1-oxidase, represents a major source of sugar-derived H2O2 under the culture conditions used
additional information
evolution
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the enzyme belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily
evolution
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the enzyme belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily, comparison of P2O and other enzymes in the GMC family, overview. Although all of the GMC enzymes share similar structural folding and use the hydride transfer mechanism for flavin reduction, they appear to have subtle differences in the fine-tuned details of how they catalyze substrate oxidation
additional information
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flavin oxidation occurs via different pathways depending on the pH of the environment. At pH values lower than 8.0, the reduced enzyme reacts with O2 to form a C4a-hydroperoxyflavin intermediate, leading to elimination of H2O2. At pH 8.0 and higher, the majority of the reduced enzyme reacts with O2 via a pathway that does not allow detection of the C4a-hydroperoxyflavin, and flavin oxidation occurs with decreased rate constants upon the rise in pH. The switching between the two modes of enzyme oxidation is controlled by protonation of a group which has a pKa of 7.6, stopped-flow spectrophotometry, overview
additional information
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redox potential of wild-type and mutant enzymes, overview
additional information
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substrate recognition loop, active-site protein interactions for D-glucose, and structural determinants of the productive glucose C2-oxidation mode, detailed overview
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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-fructose + O2
1,5-anhydro-3-keto-D-fructose + H2O2
-
-
yield of 1,5-anhydro-3-keto-D-fructose: 33%
?
1,5-anhydro-D-glucitol + O2
1,5-anhydro-D-fructose + H2O2
Phanerochaete gigantea
-
8% relative activity to D-glucose
yield of 1,5-anhydro-D-fructose: 100%
?
1,5-anhydro-D-glucitol + O2
?
-
18.4% of the activity with D-glucose
-
-
?
1-beta-aurothioglucose + O2
?
-
91% relative activity to D-glucose
-
-
?
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) + O2
? + H2O2
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-
-
?
2-deoxy-2-fluoro-D-glucose + O2
2-deoxy-3-dehydro-D-glucose + H2O2
slow substrate
-
-
?
2-deoxy-D-galactose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
2-deoxy-D-glucose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
3-O-methyl-D-glucose + O2
2-keto-3-O-methyl-D-glucose + H2O2
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8.6% relative activity to D-glucose
-
?
beta-D-galactose + O2
2-dehydro-D-galactose + H2O2
poor substrate
-
-
?
cellobiose + O2
2-dehydrocellobiose + H2O2
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17.8% activity compared to D-glucose
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-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + hydroquinone
-
-
-
?
D-galactose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-galactose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
-
?
D-galactose + ferrocenium hexafluorophosphate
2-dehydro-D-galactose + ferrocene
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-
-
?
D-glucono-1,5-lactone + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucono-1,5-lactone
D-glucono-1,5-lactone + O2
2-dehydro-D-glucono-1,5-lactone + H2O2
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107% activity compared to D-glucose
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-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + hydroquinone
1,4-benzoquinone is a physiologically relevant alternative electron acceptor in the oxidative half-reaction
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?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
2-dehydro-D-glucose + ?
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-
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?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocenium ion
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-
-
-
?
D-glucose + ferrocenium hexafluorophosphate
2-dehydro-D-glucose + ferrocene
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-
-
?
D-glucose + O2
D-arabino-2-hexosulose + H2O2
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the enzyme is produced during glucose starvation
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?
D-maltoheptaose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-maltopentaose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-maltotriose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-mannose + O2
2-dehydro-D-mannose + H2O2
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18.4% activity compared to D-glucose
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-
?
D-mannose + O2
2-keto-D-mannose + H2O2
-
0.9% relative activity to D-glucose
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?
D-ribose + 1,4-benzoquinone
2-dehydro-D-ribose + 1,4-hydroquinone
-
-
-
-
?
D-trehalose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-xylose + 1,4-benzoquinone
2-dehydro-D-xylose + 1,4-hydroquinone
-
-
-
-
?
L-arabinose + 1,4-benzoquinone
2-dehydro-L-arabinose + 1,4-hydroquinone
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-
-
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?
lactose + O2
2-dehydrolactose + H2O2
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0.71% activity compared to D-glucose
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?
maltose + O2
2-dehydro-D-maltose + H2O2
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92.2% activity compared to D-glucose
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-
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
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-
-
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
-
25% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
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18% relative activity to D-glucose
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?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
-
18% relative activity to D-glucose
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?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
Phanerochaete gigantea
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1% relative activity to D-glucose
yield: 75%
?
3-deoxy-3-fluoro-beta-D-glucose + H2O2
?
slow substrate
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-
?
3-deoxy-D-glucose + O2
2-keto-3-deoxy-D-glucose + H2O2
Phanerochaete gigantea
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96% relative activity to D-glucose
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?
5-thioglucose + O2
2-keto-5-thioglucose + H2O2
-
30% relative activity to D-glucose
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?
5-thioglucose + O2
2-keto-5-thioglucose + H2O2
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24% relative activity to D-glucose
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?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
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-
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?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
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76% relative activity to D-glucose
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?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
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73% relative activity to D-glucose
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?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
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73% relative activity to D-glucose
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?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
Phanerochaete gigantea
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15% relative activity to D-glucose
-
?
alpha-D-melibiose + O2
? + H2O2
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1.9% relative activity to D-glucose
-
?
D-cellobiose + O2
?
17% of the activity with D-glucose
-
-
?
D-cellobiose + O2
?
17% of the activity with D-glucose
-
-
?
D-cellobiose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-fructose + O2
2-dehydro-D-fructose + H2O2
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12.4% activity compared to D-glucose
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-
?
D-fructose + O2
? + H2O2
-
6.5% relative activity to D-glucose
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
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-
-
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?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
-
-
-
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?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
?
D-fucose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
38.8% activity compared to D-glucose
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
38.8% activity compared to D-glucose
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
5% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
5% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
4% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
7.7% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
8.5% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
5.7% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
His-tagged recombinant wild type enzyme strongly prefers D-glucose to D-galactose as its substrate
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
mutants T169S, T169N, and T169G
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
0.9% relative activity to D-glucose
-
?
D-galactose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-glucono-1,5-lactone + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucono-1,5-lactone
-
-
-
-
?
D-glucono-1,5-lactone + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucono-1,5-lactone
-
-
-
-
?
D-glucono-1,5-lactone + O2
?
68% of the activity with D-glucose
-
-
?
D-glucono-1,5-lactone + O2
?
68% of the activity with D-glucose
-
-
?
D-gluconolactone + O2
? + H2O2
-
activity about 10% that of D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
60% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
60% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
44% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
1.5% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
Polyporus obtusus
-
14% relative activity to D-glucose, two main products, i.e., 2-ketogluconic acid and araboascorbic acid are formed
-
?
D-gluconolactone + O2
? + H2O2
-
64% relative activity to D-glucose
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
-
?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
-
?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
-
?
D-glucose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucose + ?
-
-
-
-
?
D-glucose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucose + ?
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
D-glucose is the best substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
D-glucose is the best substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
656544, 695870, 696791, 696887, 696888, 697917, 699076, 711239, 712500, 724369, 724753, 724979, 725776, 741113, 741252
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
immobilized and soluble pyranose 2-oxidase analyzed
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
recombinant pyranose 2-oxidase analyzed
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
His-tagged recombinant wild type enzyme strongly prefers D-glucose to D-galactose as its substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
the wild type enzyme displays a clear preference for D-glucose over D-galactose
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
highly regioselective mechanism
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
recombinant pyranose 2-oxidase analyzed
-
-
?
D-glucose + O2
D-arabino-hexos-2-ulose + H2O2
Polyporus obtusus
-
-
the product is a specific tautomeric form of D-arabino-hexos-2-ulose (form IV, 20%) being in equilibrium with three other forms of D-arabinohexos-2-ulose in solution
-
?
D-glucose + O2
D-arabino-hexos-2-ulose + H2O2
Polyporus obtusus AU124PD
-
-
the product is a specific tautomeric form of D-arabino-hexos-2-ulose (form IV, 20%) being in equilibrium with three other forms of D-arabinohexos-2-ulose in solution
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
alpha-D-glucose has a 104% relative activity compared to D-glucose, beta-D-glucose has a 80% relative activity compared to D-glucose
-
?
D-glucose + O2
D-glucosone + H2O2
-
the activation energy for D-glucose activation is 24.7 kJ/mol
-
?
D-glucose + O2
D-glucosone + H2O2
-
activation energy for the conversion of D-glucose is 34.6 kJ/mol
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
other electron acceptors: 2,6-dichlorophenolindophenol, cytochrome c
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Trametes cinnabarinus
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
both alpha- and beta-anomeric forms can serve almost equally as substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
other electron acceptors: 2,6-dichlorophenolindophenol, cytochrome c
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-xylose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-xylose + ?
-
-
-
-
?
D-xylose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-xylose + ?
-
-
-
-
?
D-xylose + O2
2-dehydro-D-xylose + H2O2
-
75.1% activity compared to D-glucose
-
-
?
D-xylose + O2
?
35% of the activity with D-glucose
-
-
?
D-xylose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
activity about 10% that of D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
30% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
37% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
37% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
50% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
43.7% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
Polyporus obtusus
-
38% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
56% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
2.6% relative activity to D-glucose
-
?
gentibiose + O2
2-keto-D-gentibiose + H2O2
-
23% relative activity to D-glucose
-
?
L-arabinose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
L-sorbose + 3-methyl-2-benzothiazolinone hydrazone
?
-
-
-
-
?
L-sorbose + O2
2-dehydro-L-sorbose + H2O2
-
122% activity compared to D-glucose
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
activity about 10% that of D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
68% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
52% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
52% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
96.3% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
109% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
Polyporus obtusus
-
59% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
99% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
3.4% relative activity to D-glucose
-
?
maltose + O2
? + H2O2
-
26% relative activity to D-glucose
-
-
methyl alpha-D-glucoside + O2
2-dehydro-alpha-D-methylglucoside + H2O2
-
3% relative activity to D-glucose
-
-
?
methyl alpha-D-glucoside + O2
2-dehydro-alpha-D-methylglucoside + H2O2
-
1.9% relative activity to D-glucose
-
-
?
methyl beta-D-glucoside + O2
2-dehydro-beta-D-methylglucoside + H2O2
-
26.3% relative activity to D-glucose
-
-
?
methyl beta-D-glucoside + O2
2-dehydro-beta-D-methylglucoside + H2O2
-
9.6% relative activity to D-glucose
-
-
?
additional information
?
-
-
no activity with mannose and lactose as substrates. The enzyme catalyzes the two-electron reduction of 1,4-benzoquinone, several substituted benzoquinones and 2,6-dichloroindophenol. Some of these quinone electron acceptors are better substrates for pyranose oxidase than oxygen. Peroxidase-coupled assay using [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)] as the chromogen
-
-
-
additional information
?
-
-
no activity with D-fructose, mannose and lactose as substrates. Peroxidase-coupled assay using [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)] as the chromogen
-
-
-
additional information
?
-
evidence that the enzyme has a role in lignocellulose degradation
-
-
-
additional information
?
-
-
at 10 mM concentration, glucose is the best substrate, but xylose, sorbose, and D-glucono-1,5-lactone have more than half of its activity
-
-
-
additional information
?
-
-
evidence that the enzyme has a role in lignocellulose degradation
-
-
-
additional information
?
-
evidence that the enzyme has a role in lignocellulose degradation
-
-
-
additional information
?
-
-
at 10 mM concentration, glucose is the best substrate, but xylose, sorbose, and D-glucono-1,5-lactone have more than half of its activity
-
-
-
additional information
?
-
-
no activity in the presence of D-mannose, D-fructose, maltose, trehalose, lactose and D-melibiose
-
-
-
additional information
?
-
-
no activity in the presence of D-mannose, D-fructose, maltose, trehalose, lactose and D-melibiose
-
-
-
additional information
?
-
-
pyranose 2-oxidase from Trametes multicolor is a flavoenzyme that catalyzes the oxidation of D-glucose and other aldopyranose sugars at the C2 position by using O2 as an electron acceptor to form the corresponding 2-oxo-sugars and H2O2
-
-
-
additional information
?
-
-
ferulic acid oxidation in a model system and of thiol oxidation in a wheat flour extract, overview. L-arabinose is a poor substrate. Dehydroascorbic acid does not act as electron acceptor
-
-
-
additional information
?
-
-
most of the catalytic dehydrogenation of substrates by flavoprotein oxidases in the GMC class is initiated by the removal of a hydroxyl proton followed by the transfer of a hydride moiety. Pyranose 2-oxidase catalyzes the oxidation of several aldopyranoses by molecular oxygen at the C2 position to yield the corresponding 2-keto-aldoses and hydrogen peroxide
-
-
-
additional information
?
-
ferulic acid oxidation in a model system and of thiol oxidation in a wheat flour extract, overview. L-arabinose is a poor substrate. Dehydroascorbic acid does not act as electron acceptor
-
-
-
additional information
?
-
-
the rate of bioconversion of D-glucose by glucose 2-oxidase in the presence of either nitrogen or supercritical CO2 at 110 bar is very low compared with the use of compressed air at the same pressure
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
mutants T169S, T169N, and T169G
-
-
?
D-glucose + O2
D-arabino-2-hexosulose + H2O2
-
the enzyme is produced during glucose starvation
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
724369, 724753, 724979, 725776, 741113, 741252, 712768, 725054, 740474, 740564, 740893, 741294, 741299
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
highly regioselective mechanism
-
-
?
additional information
?
-
Q6QWR1
evidence that the enzyme has a role in lignocellulose degradation
-
-
-
additional information
?
-
-
evidence that the enzyme has a role in lignocellulose degradation
-
-
-
additional information
?
-
Q6QWR1
evidence that the enzyme has a role in lignocellulose degradation
-
-
-
additional information
?
-
-
pyranose 2-oxidase from Trametes multicolor is a flavoenzyme that catalyzes the oxidation of D-glucose and other aldopyranose sugars at the C2 position by using O2 as an electron acceptor to form the corresponding 2-oxo-sugars and H2O2
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the type of aminoacyl flavin covalent link is 8alpha-(N3-histidyl)-FAD
FAD
-
each subunit contains one FAD covalently linked at the C8 methyl group of FAD to Ne2 of residue His167
FAD
-
the FAD cofactor in P2O is covalently linked through a histidyl linkage at His167
FAD
-
one FAD per subunit, Trp168 residue near the flavin isoalloxazine ring can potentially act as an electron donor to the excited flavin isoalloxazine ring, isoalloxazine is covalently linked to His167
FAD
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-keto-D-glucose
-
5% reduction at 100 mM, 10% reduction at 200 mM, no deactivating effect determined
Sodium azide
-
slightly inhibitory at 1 mM, more than 85% activity remains
alpha,alpha'-dipyridyl
-
slightly inhibitory at 1 mM, more than 85% activity remains
H2O2
-
oxidation of Phe454, which is located at the flexible active-site loop of the enzyme, is the first and main step in the inactivation of the enzyme by hydrogen peroxide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
an increase in the pressure with compressed air results in higher rates of bioconversion of D-glucose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1,4-benzoquinone
-
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; 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; 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; 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
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical
-
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
2,6-dichloroindophenol
-
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
2-chloro-1,4-benzoquinone
-
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
2-methoxy-1,4-benzoquinone
-
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
D-Allose
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
D-fructose
-
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
D-galactose
-
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; 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
D-glucose
-
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; 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; 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; 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; 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 Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 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 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
D-melibiose
-
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
D-xylose
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
ferricenium hexafluorophosphate
-
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
0.15
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
0.22
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
0.29
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
0.33
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
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
ferricenium ion
-
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