EC Number   |
Reaction |
Reference |
|---|
   1.10.3.3 | 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
binding mode of phenolic inhibitors and substrate to active site, binding site in a pocket near type I copper center |
655740 |
| 1.10.3.3 | 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
intramolecular electron transfer from type I copper to type III copper is probably the rate-limiting step in enzyme catalysis |
439900 |
| 1.10.3.3 | 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
mechanism and rate constants |
656442 |
| 1.10.3.3 | 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
mechanism: Cu2+ is reduced to Cu+, which is then reoxidized by oxygen |
439889 |
| 1.10.3.3 | 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
multiple displacement mechanism, enzyme exhibits enzymic memory |
439916 |
| 1.10.3.3 | 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
rate determining step in the catalytic mechanism may involve protonation of an intermediate |
439923 |
| 1.10.3.3 | 4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
the transition from native dimer to the dimeric intermediate is characterized by the release of copper ions forming the tri-nuclear copper center located at the interface between domain 2 and 3 of each subunit |
673569 |
