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1.13.12.2: lysine 2-monooxygenase

This is an abbreviated version!
For detailed information about lysine 2-monooxygenase, go to the full flat file.

Word Map on EC 1.13.12.2

Reaction

L-lysine
+
O2
=
5-Aminopentanamide
 +
CO2
 +
H2O

Synonyms

davB, L-AAO/MOG, L-amino acid oxidase/monooxygenase, L-LOX/MOG, L-lysine 2-monooxygenase, L-lysine monooxygenase, L-lysine oxidase/monooxygenase, L-lysine-2-monooxygenase, lysine monooxygenase, lysine oxygenase

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
                1.13.12.2 lysine 2-monooxygenase

Crystallization

Crystallization on EC 1.13.12.2 - lysine 2-monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and SeMet-labeled enzymes, sitting-drop vapor diffusion method, mixing of 0.001 ml of protein solution, consisting of 20 mg/mL protein in 20 mM HEPES-NaOH, pH 7.6, and 0.001 ml of reservoir solution, consisting of 8% PEG 4000 and 0.1 M Na-acetate, pH 4.6, Se-Met substituted crystals are obtained using reservoir solution consisting of 16% PEG 3350, 0.02 M citric acid, and 0.08 M bis-Tris propane-HCl, pH 8.8, 20°C, X-ray diffraction structure determination and analysis at 1.90 and 2.20 A resolution respectively
structures of L-AAO/MOG complexed with L-Lys, L-ornithine, and L-Arg. Residue Asp238 is located at the ceiling of a long hydrophobic pocket and forms a strong interaction with the terminal, positively charged group of the substrates. In the ligand-free structure, there are two channels connecting the active site and solvent, and a short region located at the dimer interface is disordered. In the L-Lys complex structure, a loop region is displaced to plug the channels