Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
twitter

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

Summary:
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

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


Enzymatic reaction of: L-lysine monooxygenase

EC Number: 1.13.12.2

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

Summary:
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:

Substrate
Km (μM)
Citations
L-lysine
620.0
[Nakazawa72]
oxygen
440.0
[Nakazawa72]

pH(opt): 8.8-9.0 [Flashner74]


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sat Aug 29, 2015, BIOCYC14A.