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Results 1 - 7 of 7
EC Number General Information Commentary Reference
Show all pathways known for 1.13.12.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.2evolution the bifunctional enzyme L-AAO/MOG belongs to the MAO family of enzymes 742530
Show all pathways known for 1.13.12.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.2malfunction 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
Show all pathways known for 1.13.12.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.2metabolism 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
Show all pathways known for 1.13.12.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.2metabolism the enzyme is involved in the aminovalerate pathway, overview -, 745704
Show all pathways known for 1.13.12.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.2metabolism 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
Show all pathways known for 1.13.12.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.2more 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
Show all pathways known for 1.13.12.2Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.2physiological 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
Results 1 - 7 of 7