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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

General Information

General Information on EC 1.13.12.2 - lysine 2-monooxygenase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the bifunctional enzyme L-AAO/MOG belongs to the MAO family of enzymes
malfunction
metabolism
physiological function
the enzyme produces 5-aminovalerate, a metabolite of L-lysine catabolism through the aminovalerate pathway in Pseudomonas putida. L-Lysine monooxygenase (DavB) and 5-aminovaleramide amidohydrolase (DavA, EC 3.5.1.30) play key roles in the biotransformation of L-lysine into 5-aminovalerate
additional information
three-dimensional structure of L-AAO/MOG, overview. The key residue for the activity conversion of L-AAO/MOG, Cys254, is located near the aromatic cage (Trp418, Phe473, and Trp516). Cys254 is not directly involved in the substrate binding, but the chemical modification by 4-chloromercuribenzoate or C254I mutation has significant impact on the substrate binding via the side chain of Trp516. A slight difference of the binding position of a substrate dictates the activity of this type of enzyme as oxidase or monooxygenase