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Literature summary for 1.11.1.10 extracted from
- Multiple catalytic roles of chloroperoxidase in the transformation of phenol products and pathways (2019), Ecotoxicol. Environ. Saf., 179, 96-103 .
Application
| Application | Comment | Organism |
|---|---|---|
| environmental protection | CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters | Leptoxyphium fumago |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| monochlorodimedon + chloride + H2O2 | Leptoxyphium fumago | - |
dichlorodimedon + 2 H2O | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leptoxyphium fumago | P04963 | Caldariomyces fumago | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| monochlorodimedon + chloride + H2O2 | - |
Leptoxyphium fumago | dichlorodimedon + 2 H2O | - |
? | |
| monochlorodimedon + chloride + H2O2 | H2O2 activation of the heme group | Leptoxyphium fumago | dichlorodimedon + 2 H2O | - |
? | |
| additional information | LC-MS/MS and gas chromatography-mass spectrometry (GC-MS) are used for product identification, overview. Hydroxylated polybrominated diphenyl ethers (diOH-PBDEs) and hydroxylated polybrominated biphenyls (diOH-PBBs) formed by dihydroxyl group substitutions in the ortho-positions relative to the diphenyl ether bond or the single bond in biphenyl, may undergo intramolecular cyclization | Leptoxyphium fumago | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chloroperoxidase | - |
Leptoxyphium fumago |
| CPO | - |
Leptoxyphium fumago |
| More | see also EC 1.11.1.18 | Leptoxyphium fumago |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Leptoxyphium fumago |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3 | - |
- |
Leptoxyphium fumago |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | H2O2 activation of the heme group | Leptoxyphium fumago | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | chloroperoxidase (CPO) is a hybrid of two different families of enzymes, peroxidases and P450s | Leptoxyphium fumago |
| physiological function | containing both a P450-like proximal pocket and a peroxidase-like distal pocket, enzyme chloroperoxidase (CPO) is a versatile heme-containing enzyme that possesses the catalytic capacities of both peroxidase and P450 enzyme families. CPO has multiple catalytic functions, attributable to four CPO-mediated processes, including bromination, radical coupling, intramolecular cyclization and debromination. Phenol is readily transformed into a variety of brominated organic compounds (BOCs) via the CPO-mediated oxidative process. Higher bromide concentrations and lower pH conditions both facilitate the formation of brominated products. While a higher bromination capacity is observed in pH 3.0 solutions, CPO-mediated radical couplings are more favorable at pH 5.0 and pH 6.0. Although CPO might catalyze chlorination when chloride and bromide coexisted in the solution, BOCs are the dominant products of CPO-mediated phenol oxidation. Bromination (EC 1.11.1.18) is preferable to chlorination (EC 1.11.1.10) in the CPO-mediated reaction in the presence of both bromide and chloride | Leptoxyphium fumago |
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