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Literature summary for 1.14.13.1 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)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida Q59713
-
-
Pseudomonas putida S-1 Q59713
-
-

Reaction

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 and Products (Substrate)

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

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

Cofactor

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

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