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Literature summary extracted from

  • Wang, X.; Hou, Q.; Liu, Y.
    Insights into the decarboxylative hydroxylation of salicylate catalyzed by the flavin-dependent monooxygenase salicylate hydroxylase (2018), Theoret. Chem. Accounts, 137, 89 .
No PubMed abstract available

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.1 salicylate + NADH + 2 H+ + O2 Pseudomonas putida
-
 catechol + NAD+ + H2O + CO2
-
 ?
1.14.13.1 salicylate + NADH + 2 H+ + O2 Pseudomonas putida S-1
-
 catechol + NAD+ + H2O + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.1 Pseudomonas putida Q59713
-
-
1.14.13.1 Pseudomonas putida S-1 Q59713
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.1 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.1 salicylate + NADH + 2 H+ + O2
-
 Pseudomonas putida catechol + NAD+ + H2O + CO2
-
 ?
1.14.13.1 salicylate + NADH + 2 H+ + O2
-
 Pseudomonas putida S-1 catechol + NAD+ + H2O + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.1 flavin-dependent monooxygenase salicylate hydroxylase
-
 Pseudomonas putida
1.14.13.1 SALH
-
 Pseudomonas putida
1.14.13.1 salicylate hydroxylase
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.1 FAD SALH is a typical flavin adenine dinucleotide (FAD)-dependent monooxygenase. The enzyme reaction proceeds via a C4a-hydorperoxyflavin intermediate Pseudomonas putida
1.14.13.1 NADH
-
 Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.14.13.1 additional information structure-function relationship and analysis using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview Pseudomonas putida
1.14.13.1 physiological function salicylate hydroxylase (SALH) is a member of oxygen oxidoreductases, which catalyzes the hydroxylation and decarboxylation of salicylate to generate catechol Pseudomonas putida