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Literature summary extracted from
- Functional modification of an arginine residue on salicylate hydroxylase (1990), Biochim. Biophys. Acta, 1040, 327-336.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.1 | additional information | chemical modification of one arginine residue with glyoxal causes the enzyme to act as dehydrogenase, but not as oxygenase | Pseudomonas putida |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.1 | Pseudomonas putida | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.1 | additional information | by chemical treatment of the enzyme with dicarbonyl reagents, such as glyoxal, the original oxygenase activity is converted to the salicylate-dependent NADH-dehydrogenase activity with free FAD as electron acceptor | Pseudomonas putida | ? | - |
? |  |
| 1.14.13.1 | salicylate + NADH + H+ + O2 | - |
Pseudomonas putida | catechol + NAD+ + H2O + CO2 | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.1 | NADH | - |
Pseudomonas putida | |
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Release 2023.1 (January 2023)
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