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Literature summary for 1.14.13.9 extracted from

  • Crozier-Reabe, K.R.; Phillips, R.S.; Moran, G.R.
    Kynurenine 3-monooxygenase from Pseudomonas fluorescens: substrate-like inhibitors both stimulate flavin reduction and stabilize the flavin-peroxo intermediate yet result in the production of hydrogen peroxide (2008), Biochemistry, 47, 12420-12433.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Pseudomonas fluorescens

Inhibitors

Inhibitors Comment Organism Structure
benzoylalanine KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH Pseudomonas fluorescens
m-nitrobenzoylalanine KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH Pseudomonas fluorescens
additional information targeted inhibition of KMO is a viable strategy for achieving local elevation of kynurenate concentrations Pseudomonas fluorescens

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl stabilizes Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas fluorescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-kynurenine + NADPH + O2 binding of L-kynurenine to the oxidized enzyme is relatively slow and involves at least two reversible steps Pseudomonas fluorescens 3-hydroxy-L-kynurenine + NADP+ + H2O
-
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Synonyms

Synonyms Comment Organism
KMO
-
Pseudomonas fluorescens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Pseudomonas fluorescens
NADPH
-
Pseudomonas fluorescens