Protein Variants | Comment | Organism |
---|---|---|
T169A | site-directed mutagenesis, the hydrogen bond between residue 169 and the N5 atom of FAD is absent, resulting in a change in the kinetic mechanism to one that consists of a ternary complex | Trametes ochracea |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state and pre-steady-state kinetics, and kinetic isotope effects, of oxidative half-reaction and overall reaction, overview | 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 | - |
? | |
additional information | Trametes ochracea | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trametes ochracea | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Trametes ochracea |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucose + O2 | - |
Trametes ochracea | 2-dehydro-D-glucose + H2O2 | - |
? | |
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 | Trametes ochracea | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
P2O | - |
Trametes ochracea |
pyranose 2-Oxidase | - |
Trametes ochracea |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Trametes ochracea |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
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. The protonation of the group which controls the mode of flavin oxidation cannot be rapidly equilibrated with outside solvent. Using a double-mixing stopped-flow experiment, a rate constant for proton dissociation from the reaction site is determined to be 21.0 s-1 | Trametes ochracea |
5 | 10 | activity range | Trametes ochracea |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoenzyme | Trametes ochracea |
General Information | Comment | Organism |
---|---|---|
additional information | 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 | Trametes ochracea |