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Literature summary for 1.11.1.10 extracted from
- Examining the role of glutamic acid 183 in chloroperoxidase catalysis (2003), J. Biol. Chem., 278, 13855-13859.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of E183H in Escherichia coli | Leptoxyphium fumago |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E183H | the mutation is detrimental to the chlorination and dismutation activity of chloroperoxidase, activities are reduced by 85% and 50% of the wild-type activity. Epoxidation activity of the mutant enzyme is significantly enhanced, about 2.5fold | Leptoxyphium fumago |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leptoxyphium fumago | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| partial | Leptoxyphium fumago |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| H2O2 + methylene blue | - |
Leptoxyphium fumago | oxidized methylene blue + H2O | - |
? |  |
| monochlorodimedone + Cl- + H2O2 | - |
Leptoxyphium fumago | dichlorodimedone + H2O | - |
? | |
| p-nitrostyrene + H2O2 | - |
Leptoxyphium fumago | p-nitrostyrene oxide + H2O | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 2.7 | 5 | wild-type enzyme, chlorination activity | Leptoxyphium fumago |
| 3 | - |
mutant enzyme E183H, chlorination activity | Leptoxyphium fumago |
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