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Literature summary for 1.11.1.11 extracted from
- Autocatalytic formation of a covalent link between tryptophan 41 and the heme in ascorbate peroxidase (2007), Biochemistry, 46, 2174-2180.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Glycine max | 5829 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Glycine max | Q43758 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Glycine max |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-ascorbate + H2O2 | - |
Glycine max | dehydroascorbate + H2O | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation | Glycine max | |
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