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 Maximum [Da] | Comment | Organism |
---|---|---|---|
270000 | - |
- |
Trametes ochracea |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucose + O2 | Trametes ochracea | - |
2-dehydro-D-glucose + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trametes ochracea | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
homotetramer | - |
Trametes ochracea |
Synonyms | Comment | Organism |
---|---|---|
P2O | - |
Trametes ochracea |
pyranose 2-Oxidase | - |
Trametes ochracea |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Trametes ochracea |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Trametes ochracea |
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 | 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 |