|Gene:||davB||Accession Number: G-9514 (MetaCyc)|
Synonyms: lysine 2-monooxygenase
Species: Pseudomonas fluorescens
Subunit composition of
L-lysine monooxygenase = [DavB]4
L-lysine monooxygenase subunit = DavB
L-lysine monooxygenase is classified as an internal flavin oxygenase. It contains four enzyme-bound FAD molecules, one per subunit. The relative molecular mass of the native protein was estimated by thin layer gel filtration. [Flashner74]
The relative molecular mass of the subunit was estimated by SDS-PAGE [Flashner74].
Gene Citations: [Revelles05]
Molecular Weight of Polypeptide: 61 kD (experimental) [Flashner74 ]
Molecular Weight of Multimer: 246 kD (experimental) [Flashner74]
Enzymatic reaction of: L-lysine monooxygenase
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pseudomonas putida the synthesis of L-lysine monooxygenase is induced by L-lysine. L-lysine monooxygenase catalyzes the oxidative decarboxylation of L-lysine. This reaction involves a concomitant decarboxylation of L-lysine with incorporation of one atom of molecular oxygen. The enzyme is specific for molecular oxygen as electron acceptor. The enzyme is also specific for the L-isomer of lysine. [Takeda69] [Flashner74a]
L-ornithine is also a substrate, but the reaction is an oxidase-type reaction, rather than an oxygenase reaction. Lysine and ornithine act as both a substrate and an effector for this enzyme. The catalytic activity is a sigmoidal function of the lysine or ornithine concentration, suggesting a regulatory site(s) within the enzyme which when saturated, increases its catalytic capacity. [Flashner74a, Nakazawa72]
pH(opt): 8.8-9.0 [Flashner74]
Revelles05: Revelles O, Espinosa-Urgel M, Fuhrer T, Sauer U, Ramos JL (2005). "Multiple and interconnected pathways for L-lysine catabolism in Pseudomonas putida KT2440." J Bacteriol 187(21);7500-10. PMID: 16237033
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