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

BRENDA support

Literature summary for 1.13.12.2 extracted from

  • Flashner, M.S.; Massey, V.
    Flavoprotein oxygenases (1974), Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York, , 245-283.
No PubMed abstract available
Search for more literature for 1.13.12.2

Inhibitors

Inhibitors Comment Organism Structure
SDS
-
 Pseudomonas fluorescens
sulfhydryl inhibitors
-
 Pseudomonas fluorescens

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metals play no role in lysine monooxygenase Pseudomonas fluorescens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
191000
-
 sedimentation velocity experiments Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + O2 monooxygenase activity Pseudomonas fluorescens 5-aminopentanamide + CO2 + H2O
-
 ?
L-lysine + O2 oxidase activity Pseudomonas fluorescens 2-keto-6-amino-n-hexanoate + NH3 + H2O2
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Pseudomonas fluorescens
FAD FAD cannot be replaced by FMN or riboflavin Pseudomonas fluorescens