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Literature summary 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)

EC Number Cloned (Comment) Organism
1.14.13.9
-
Pseudomonas fluorescens

Inhibitors

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.9 NaCl stabilizes Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.9 Pseudomonas fluorescens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.9
-
Pseudomonas fluorescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.9 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

EC Number Synonyms Comment Organism
1.14.13.9 KMO
-
Pseudomonas fluorescens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.9 FAD
-
Pseudomonas fluorescens
1.14.13.9 NADPH
-
Pseudomonas fluorescens