DavB is the flavin-dependent lysine 2-monooxygenase that initiates the bacterial Dav pathway by oxidatively decarboxylating L-lysine to 5-aminopentanamide. DavA then hydrolyzes this intermediate to 5-aminovalerate.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Correct but uninformative oxidoreductase parent. Reason: The substrate-specific lysine 2-monooxygenase term captures the core activity. |
| GO:0050067 L-lysine 2-monooxygenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct enzyme-specific activity for the DavB reaction. Reason: Purified KT2440 DavB directly oxidizes L-lysine to 5-aminopentanamide, supporting an experimental evidence upgrade beyond the current IEA row despite the conflicting automated UniProt product name. Supporting Evidence: PMID:25012259 DavB is a FAD-dependent monooxygenase that catalyzes oxidative decarboxylation of l-lysine PMID:31064836 the oxidation of lysine to 5-aminopentanamide by DavB and its subsequent deamination to 5AVA by DavA |
| GO:0019477 L-lysine catabolic process | IMP PMID:16237033 Multiple and interconnected pathways for L-lysine catabolism... | NEW | Summary: Add the genetically established Dav-pathway biological process. Reason: KT2440 mutant analysis identifies davB in the aminovalerate pathway required for use of L-lysine as sole carbon and nitrogen source. Supporting Evidence: PMID:16237033 Mutants with mutations in either pathway failed to use L-lysine as the sole carbon and nitrogen source PMID:16237033 New genes were identified in both pathways, including the davB and davA genes that encode the enzymes involved in the oxidation of L-lysine to delta-aminovaleramide and the hydrolysis of the latter to delta-aminovalerate, respectively. |
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Download this section (compressed HTML)Q: Which active-site determinants distinguish DavB lysine 2-monooxygenases from tryptophan 2-monooxygenases?
Experiment: Measure purified DavB turnover with L-lysine and L-tryptophan, identify the flavin cofactor, and test davB complementation during growth on L-lysine.
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