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Literature summary for 1.14.13.1 extracted from

  • Pereira, M.S.; de Araujo, S.S.; Nagem, R.A.P.; Richard, J.P.; Brandao, T.A.S.
    The role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylase (2022), Bioorg. Chem., 119, 105561 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

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 G7
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catechol + NAD+ + H2O + CO2
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida Q8RMN4
-
-
Pseudomonas putida G7 Q8RMN4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information salicylate hydroxylase NahG has a single redox site in which FAD is reduced by NADH, the O2 is activated by the reduced flavin, and salicylate undergoes an oxidative decarboxylation by a C(4a)-hydroperoxyflavin intermediate to give catechol Pseudomonas putida ?
-
-
additional information salicylate hydroxylase NahG has a single redox site in which FAD is reduced by NADH, the O2 is activated by the reduced flavin, and salicylate undergoes an oxidative decarboxylation by a C(4a)-hydroperoxyflavin intermediate to give catechol Pseudomonas putida G7 ?
-
-
salicylate + NADH + 2 H+ + O2
-
Pseudomonas putida catechol + NAD+ + H2O + CO2
-
?
salicylate + NADH + 2 H+ + O2
-
Pseudomonas putida G7 catechol + NAD+ + H2O + CO2
-
?

Synonyms

Synonyms Comment Organism
NahG
-
Pseudomonas putida
salicylate hydroxylase
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Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
FAD required, contribution of individual pieces of the FAD cofactor to the observed enzymatic activity for turnover of the whole cofactor. Comparison of the kinetic parameters and products for the NahG-catalyzed reactions of FMN and riboflavin cofactor fragments reveal that the adenosine monophosphate (AMP) and ribitol phosphate pieces of FAD act to anchor the flavin to the enzyme and to direct the partitioning of the C(4a)-hydroperoxyflavin reaction intermediate towards hydroxylation of salicylate. The addition of AMP or ribitol phosphate pieces to solutions of the truncated flavins results in a partial restoration of the enzymatic activity lost upon truncation of FAD, and the pieces direct the reaction of the C(4a)-hydroperoxyflavin intermediate towards hydroxylation of salicylate Pseudomonas putida
NADH
-
Pseudomonas putida