EC Number |
General Information |
Reference |
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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 | more |
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 |