Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
salicylate + NADH + 2 H+ + O2 | Pseudomonas putida | - |
catechol + NAD+ + H2O + CO2 | - |
? | |
salicylate + NADH + 2 H+ + O2 | Pseudomonas putida S-1 | - |
catechol + NAD+ + H2O + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | Q59713 | - |
- |
Pseudomonas putida S-1 | Q59713 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
salicylate + NADH + H+ + O2 = catechol + NAD+ + H2O + CO2 | analysis of the reaction mechanism of SALH using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview. The whole enzymatic reaction contains two parts: the hydroxylation and decarboxylation. The deprotonated substrate is the active form, whereas the neutral form of salicylate corresponds to very a high energy barrier (39.8 kcal/mol) for the hydroxylation process, which is in line with the experimental result that the optimum pH is 7.6. The calculated results with the deprotonated substrate indicate that the hydroxylation and decarboxylation occur in a stepwise manner and the decarboxylation process is calculated to be the rate-limiting step with an energy barrier of 14.5 kal/mol. The catalytic reaction is highly exothermic. It proceeds via a C4a-hydorperoxyflavin | Pseudomonas putida |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
salicylate + NADH + 2 H+ + O2 | - |
Pseudomonas putida | catechol + NAD+ + H2O + CO2 | - |
? | |
salicylate + NADH + 2 H+ + O2 | - |
Pseudomonas putida S-1 | catechol + NAD+ + H2O + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
flavin-dependent monooxygenase salicylate hydroxylase | - |
Pseudomonas putida |
SALH | - |
Pseudomonas putida |
salicylate hydroxylase | - |
Pseudomonas putida |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | SALH is a typical flavin adenine dinucleotide (FAD)-dependent monooxygenase. The enzyme reaction proceeds via a C4a-hydorperoxyflavin intermediate | Pseudomonas putida | |
NADH | - |
Pseudomonas putida |
General Information | Comment | Organism |
---|---|---|
additional information | structure-function relationship and analysis using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview | Pseudomonas putida |
physiological function | salicylate hydroxylase (SALH) is a member of oxygen oxidoreductases, which catalyzes the hydroxylation and decarboxylation of salicylate to generate catechol | Pseudomonas putida |