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Literature summary for 1.11.1.10 extracted from
- C. fumago chloroperoxidase is also a dehaloperoxidase: oxidative dehalogenation of halophenols (2006), J. Am. Chem. Soc., 128, 1036-1037.
Application
| Application | Comment | Organism |
|---|---|---|
| environmental protection | chloroperoxidase shows oxidative dehalogenation activity and is significantly more robust than other peroxidases and functions under harsher reaction conditions compared to other biocatalysts. Expanding the scope of reactivity achieved by the enzyme may be beneficial for industrial and biotechnological functions in the future. This considerable extension of already known activities could lead to the use of the enzyme as a biocatalyst in the field of bioremediation and a broader understanding of both how peroxidases and cytochrome P450s react with halogenated organic substrates | Leptoxyphium fumago |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leptoxyphium fumago | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme can dehalogenate trihalophenols and p-halophenols. CCPO catalyzes H2O2-dependent defluorination, debromination, and deiodination reactions. Two main products, p-benzoquinone (minor) and the halophenol dimer (major), are observed for all p-halophenol-CCPO-catalyzed dehalogenation reactions | Leptoxyphium fumago | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCPO | - |
Leptoxyphium fumago |
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