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Literature summary extracted from
- FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EC 222 (1993), Eur. J. Biochem., 213, 995-1002.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.59 | FAD analogs | complete loss of activity after prolonged incubation with 8-chloro-FAD, 8-fluoro-FAD, 8-mercapto-FAD or 8-methoxy-FAD | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.59 | Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.59 | L-Lys + NADPH + O2 | - |
Escherichia coli | N6-Hydroxy-L-Lys + NADP+ + H2O | - |
? |  |
| 1.14.13.59 | additional information | in absence of substrate, the enzyme has an NADPH oxidase activity which results in generation of H2O2 | Escherichia coli | ? | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.59 | FAD | requires FAD | Escherichia coli | |
| 1.14.13.59 | FAD | binding is very weak | Escherichia coli | |
| 1.14.13.59 | FAD | Km: 0.0007 mM | Escherichia coli | |
| 1.14.13.59 | NADPH | required | Escherichia coli | |
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