MetaCyc Enzyme: L-lysine monooxygenase

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]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Created 18-Aug-2006 by Fulcher CA , SRI International

Enzymatic reaction of: L-lysine monooxygenase

EC Number:

L-lysine + oxygen <=> 5-aminopentanamide + CO2 + H2O

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.

Alternative Substrates for L-lysine: S-(2-aminoethyl)-L-cysteine [Takeda69 ] , L-ornithine [Takeda69 ] , L-arginine [Takeda69 ]

In Pathways: superpathway of L-lysine degradation , L-lysine degradation IV

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]

Cofactors or Prosthetic Groups: FAD [Flashner74]

Inhibitors (Competitive): 6-aminohexanoate [Flashner74a] , Mn2+ [Nakazawa72] , Mg2+ [Nakazawa72] , spermidine [Nakazawa72]

Inhibitors (Unknown Mechanism): ammonium [Flashner74] , Na+ [Flashner74] , K+ [Flashner74] , p-chloromercuribenzoate [Nakazawa72] , Hg2+ [Nakazawa72]

Kinetic Parameters:

Km (μM)

pH(opt): 8.8-9.0 [Flashner74]


Flashner74: Flashner MI, Massey V (1974). "Purification and properties of L-lysine monooxygenase from Pseudomonas fluorescens." J Biol Chem 249(8);2579-86. PMID: 4207122

Flashner74a: Flashner MI, Massey V (1974). "Regulatory properties of the flavoprotein L-lysine monooxygenase." J Biol Chem 249(8);2587-92. PMID: 4207123

Nakazawa72: Nakazawa T, Hori K, Hayaishi O (1972). "Studies on monooxygenases. V. Manifestation of amino acid oxidase activity by L-lysine monooxygenase." J Biol Chem 247(11);3439-44. PMID: 4624115

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

Takeda69: Takeda H, Yamamoto S, Kojima Y, Hayaishi O (1969). "Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase." J Biol Chem 244(11);2935-41. PMID: 5772467

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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