1.13.12.2	evolution	the bifunctional enzyme L-AAO/MOG belongs to the MAO family of enzymes	742530	
1.13.12.2	malfunction	wild-type Escherichia coli enzyme can not convert lysine to 5-aminovalerate, whereas recombinant Escherichia coli enzyme expressing the davBA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase produces 5-aminovalerate from lysine with a 64% conversion yield	-, 728239	
1.13.12.2	metabolism	L-lysine monooxygenase (DavB) and 5-aminovaleramide amidohydrolase (DavA) play key roles in the 5-aminovalerate pathway of various microorganisms. DavB catalyzes the oxidation of L-lysine to produce 5-aminovaleramide. DavA then catalyzes 5-aminovaleramide into 5-aminovalerate	746434	
1.13.12.2	metabolism	the enzyme is involved in the aminovalerate pathway, overview	-, 745704	
1.13.12.2	metabolism	the enzyme is involved in the aminovalerate pathway, overview. The transformation process is composed of two steps: oxidation of L-lysine into 5-aminovaleramide catalyzed by lysine 2-monooxygenase (DavB) and hydrolysis of 5-aminovaleramide into 5-aminovalerate catalyzed by delta-aminovaleramidase (DavA, EC 3.5.1.30)	746458	
1.13.12.2	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	742530	
1.13.12.2	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	746434