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Literature summary extracted from
- Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1 (1995), J. Biochem., 117, 579-585.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.1 | Trinitrobenzenesulfonic acid | irreversible inactivation, modification of a lysine residue results in loss of NADH-dehydrogenase activity suggesting its role in the NADH-binding site of the enzyme | Pseudomonas putida |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.1 | 0.0016 | - |
salicylate | native enzyme | Pseudomonas putida | |
| 1.14.13.1 | 0.0018 | - |
salicylate | modified enzyme | Pseudomonas putida | |
| 1.14.13.1 | 0.0037 | - |
NADH | native enzyme | Pseudomonas putida | |
| 1.14.13.1 | 0.049 | - |
NADH | modified enzyme | 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 | salicylate + NADH + H+ + O2 | - |
Pseudomonas putida | catechol + NAD+ + H2O + CO2 | - |
? | |
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