EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.B10 | protoporphyrin IX + ascorbate + O2 | Escherichia coli | cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2 | hematinic acid + a tripyrrole + Fe3+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.B10 | Escherichia coli | Q8X5N8 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.B10 | additional information | enzyme binds and degrades heme in a reaction that releases carbon monoxide. Initial intermediates of the reaction of ChuS with hydrogen peroxide, i.e. a ferrous keto pi neutral radical and ferric verdoheme, are in common with heme oxygenases, while a further reaction step, involving the cleavage of the porphyrin ring at adjacent meso-carbons, results in the release of hematinic acid, a tripyrrole product and non-heme iron in the ferric oxidation state | Escherichia coli | ? | - |
? | |
1.14.14.B10 | protoporphyrin IX + ascorbate + O2 | cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2 | Escherichia coli | hematinic acid + a tripyrrole + Fe3+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.B10 | ChuS | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.B10 | heme | spectrum shows bands at 409, 549, and 586 nm | Escherichia coli |