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Literature summary for 1.11.1.10 extracted from
- Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance (2006), Appl. Microbiol. Biotechnol., 71, 276-288.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Aspergillus niger | Leptoxyphium fumago |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 42000 | - |
- |
Leptoxyphium fumago |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leptoxyphium fumago | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | heavily glycosylated protein (2530% carbohydrates, two high-mannose N-glycosylation sites) | Leptoxyphium fumago |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | catalyzes the unspecific chlorination, bromination, and iodation (but no fluorination) of a variety of electrophilic organic substrates via hypohalous acid as actual halogenating agent. In the absence of halide, CPO resembles cytochrome P450s and epoxidizes and hydroxylates activated substrates such as organic sulfides and olefins. Aromatic rings are not susceptible to CPO-catalyzed oxygen-transfer | Leptoxyphium fumago | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CPO | - |
Leptoxyphium fumago |
| heme-thiolate chloroperoxidase | - |
Leptoxyphium fumago |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | - |
Leptoxyphium fumago | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Leptoxyphium fumago | - |
- |
4 |
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