Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.196 extracted from

  • Romero, E.; Robinson, R.; Sobrado, P.
    Monitoring the reductive and oxidative half-reactions of a flavin-dependent monooxygenase using stopped-flow spectrophotometry (2012), J. Vis. Exp., 18, pii: 3803.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ornithine + NADPH + H+ + O2 Aspergillus fumigatus the enzyme catalyzes the hydroxylation of ornithine in the biosynthesis of hydroxamate siderophores that are essential for virulence N5-hydroxy-L-ornithine + NADP+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus Q5SE95
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ornithine + NADPH + H+ + O2 the enzyme catalyzes the hydroxylation of ornithine in the biosynthesis of hydroxamate siderophores that are essential for virulence Aspergillus fumigatus N5-hydroxy-L-ornithine + NADP+ + H2O
-
?
L-ornithine + NADPH + H+ + O2 in the reductive half-reaction, the oxidized FAD bound to the enzyme, is reduced by NADPH. In the oxidative half-reaction, the reduced cofactor reacts with molecular oxygen to form a C4a-hydroperoxyflavin intermediate, which transfers an oxygen atom to ornithine Aspergillus fumigatus N5-hydroxy-L-ornithine + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
SidA
-
Aspergillus fumigatus
siderophore A
-
Aspergillus fumigatus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information monitoring the reductive and oxidative half-reactions of a flavin-dependent monooxygenase using stopped-flow spectrophotometry Aspergillus fumigatus

Cofactor

Cofactor Comment Organism Structure
FAD FAD-containing enzyme. In the reductive half-reaction, the oxidized FAD bound to the enzyme, is reduced by NADPH. In the oxidative half-reaction, the reduced cofactor reacts with molecular oxygen to form a C4a-hydroperoxyflavin intermediate, which transfers an oxygen atom to ornithine Aspergillus fumigatus