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Literature summary extracted from
- Paramagnetic nuclear magnetic resonance relaxation and molecular mechanics studies of the chloroperoxidase-indole complex: Insights into the mechanism of chloroperoxidase-catalyzed regioselective oxidation of indole (2013), Biochemistry, 52, 3688-3701.
No PubMed abstract available
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.1.10 | Leptoxyphium fumago | - |
ATCC 16373 | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.10 | indole + chloride + H2O2 | - |
Leptoxyphium fumago | ? | - |
? |  |
| 1.11.1.10 | additional information | the enzyme is incapable of catalyzing the halogenation of indole | Leptoxyphium fumago | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.11.1.10 | chloroperoxidase | - |
Leptoxyphium fumago |
| 1.11.1.10 | CPO | - |
Leptoxyphium fumago |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.10 | heme | a heme-thiolate protein | Leptoxyphium fumago | |
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Release 2023.1 (January 2023)
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