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Literature summary for 1.1.3.4 extracted from
- Aspects of the mechanism of catalysis of glucose oxidase: a docking, molecular mechanics and quantum chemical study (1998), J. Comput. Aided Mol. Des., 12, 425-440.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | P13006 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | His516 plays an important role in the reductive and oxidative half reaction | Aspergillus niger | ? | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | semiempirical quantum chemical calculations are used to investigate the role of FAD in the catalytic oxidation of glucose. Only the hydride ion is transferred to the FAD coenzyme | Aspergillus niger | |
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