EC Number   |
Reaction |
Reference |
|---|
   1.1.3.10 | D-glucose + O2 = 2-dehydro-D-glucose + H2O2 |
- |
- |
| 1.1.3.10 | 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 |
725714 |
| 1.1.3.10 | D-glucose + O2 = 2-dehydro-D-glucose + H2O2 |
investigation of the reaction mechanism by determining the rate constants |
696332 |
| 1.1.3.10 | 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 |
724979 |
| 1.1.3.10 | 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 |
724753 |
| 1.1.3.10 | 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 |
724369 |
| 1.1.3.10 | 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 |
-, 725054 |
