Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry Q88QV1 for Pseudomonas putida KT2440 davB
Massively Parallel Fitness Profiling Reveals Multiple Novel Enzymes in Pseudomonas putida Lysine Metabolism.
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DavB oxidizes L-lysine to 5-aminopentanamide in the initial Dav-pathway step.
"the oxidation of lysine to 5-aminopentanamide by DavB and its subsequent deamination to 5AVA by DavA"
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DavA and DavB abundance responds most strongly to L-lysine.
"The initial two enzymes from l-lysine metabolism, DavA and DavB, were most highly expressed in the presence of l-lysine"
Multiple and interconnected pathways for L-lysine catabolism in Pseudomonas putida KT2440.
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Mutations in either KT2440 lysine-catabolic pathway impair use of L-lysine.
"Mutants with mutations in either pathway failed to use L-lysine as the sole carbon and nitrogen source"
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The study identifies davB and davA as the first two aminovalerate-pathway genes.
"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."
Enzymatic production of 5-aminovalerate from L-lysine using L-lysine monooxygenase and 5-aminovaleramide amidohydrolase.