EC Number   |
Reference |
|---|
   1.11.1.10 | chloroperoxidase A and B |
348316 |
| 1.11.1.10 | hanging drop method, crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate |
674622 |
| 1.11.1.10 | molecular docking. Orange G binds within the wide channel of CPO |
741781 |
| 1.11.1.10 | sitting drop vapor diffusion method, crystals are modified by several cross-linkers, but only glutaraldehyde is able to produce catalytically active and insoluble crystals. Although the cross-linked crystals are catalytically active, they show lower specific activity than the soluble enzyme |
657725 |
| 1.11.1.10 | structure model comparison of isoforms CPO and CPO2, high conservation of the active site and the substrate channel. Amino acids Cys30, Met62, Met154 and Trp226 of CPO, which are oxidized upon treatment of the enzyme with a CPO-inactivating H 2 O 2 concentration, are also contained in CPO2 |
743123 |
