EC Number   |
General Information |
Reference |
|---|
   1.1.3.10 | evolution |
the enzyme belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily |
724753 |
| 1.1.3.10 | evolution |
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 |
724979 |
| 1.1.3.10 | more |
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 |
725776 |
| 1.1.3.10 | more |
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 |
724369 |
| 1.1.3.10 | more |
redox potential of wild-type and mutant enzymes, overview |
724753 |
| 1.1.3.10 | more |
substrate recognition loop, active-site protein interactions for D-glucose, and structural determinants of the productive glucose C2-oxidation mode, detailed overview |
725714 |
| 1.1.3.10 | physiological function |
pyranose 2-oxidase, rather than glucose 1-oxidase, represents a major source of sugar-derived H2O2 under the culture conditions used |
741789 |
