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Literature summary for 1.1.3.10 extracted from

  • Wongnate, T.; Sucharitakul, J.; Chaiyen, P.
    Identification of a catalytic base for sugar oxidation in the pyranose 2-oxidase reaction (2011), ChemBioChem, 12, 2577-2586.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H167A site-directed mutagenesis, reductive activity of the mutant is highly reduced compared to the wild-type enzyme, the mutation ablates the covalent histidyl-FAD linkage. The H167A mutant enzyme oxidizes D-glucose regiospecifically at the C2 position, similarly to the wild-type enzyme, but noncovalent flavin in H167A mainly decreases the flavin reduction rate constant by 22fold Trametes ochracea
H167A/H548A site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD Trametes ochracea
H167A/H548D site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD Trametes ochracea
H167A/H548N site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD Trametes ochracea
H167A/H548R site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD Trametes ochracea
H167A/H548S site-directed mutagenesis, reductively inactive mutant, contains noncovalently linked FAD Trametes ochracea
H548A site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD Trametes ochracea
H548D site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD Trametes ochracea
H548N site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD Trametes ochracea
H548R site-directed mutagenesis, reductive activity of the mutant is slightly reduced compared to the wild-type enzyme, contains some noncovalently and mostly covalently linked FAD Trametes ochracea
H548S site-directed mutagenesis, reductive activity of the mutant is reduced compared to the wild-type enzyme, contains noncovalently and covalently linked FAD Trametes ochracea
additional information redox potential of wild-type and mutant enzymes, overview. Single mutants of H548 result in mixed populations of noncovalently bound and covalently linked FAD. Double mutants containing H167A are constructed, in which the covalent histidyl-FAD linkage is removed in addition to having the H548 mutation Trametes ochracea
N593H site-directed mutagenesis, the enzyme contains a covalently linked FAD, similar to the wild-type enzyme Trametes ochracea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
270000
-
-
Trametes ochracea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + O2 Trametes ochracea
-
2-dehydro-D-glucose + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Trametes ochracea
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Trametes ochracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + O2
-
Trametes ochracea 2-dehydro-D-glucose + H2O2
-
?
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 Trametes ochracea ?
-
?

Subunits

Subunits Comment Organism
homotetramer
-
Trametes ochracea

Synonyms

Synonyms Comment Organism
P2O
-
Trametes ochracea
pyranose 2-Oxidase
-
Trametes ochracea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Trametes ochracea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Trametes ochracea

Cofactor

Cofactor Comment Organism Structure
FAD each subunit contains one FAD covalently linked at the C8 methyl group of FAD to Ne2 of residue His167 Trametes ochracea

General Information

General Information Comment Organism
evolution the enzyme belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily Trametes ochracea
additional information redox potential of wild-type and mutant enzymes, overview Trametes ochracea