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- W2897783063 abstract "P. putida lysine metabolism can produce multiple commodity chemicals, conferring great biotechnological value. Despite much research, the connection of lysine catabolism to central metabolism in P. putida remained undefined. Here, we used random barcode transposon sequencing to fill the gaps of lysine metabolism in P. putida . We describe a route of 2-oxoadipate (2OA) catabolism, which utilizes DUF1338-containing protein P. putida 5260 (PP_5260) in bacteria. Despite its prevalence in many domains of life, DUF1338-containing proteins have had no known biochemical function. We demonstrate that PP_5260 is a metalloenzyme which catalyzes an unusual route of decarboxylation of 2OA to d -2-hydroxyglutarate ( d -2HG). Our screen also identified a recently described novel glutarate metabolic pathway. We validate previous results and expand the understanding of glutarate hydroxylase CsiD by showing that can it use either 2OA or 2KG as a cosubstrate. Our work demonstrated that biological novelty can be rapidly identified using unbiased experimental genetics and that RB-TnSeq can be used to rapidly validate previous results." @default.
- W2897783063 created "2018-10-26" @default.
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- W2897783063 date "2019-06-25" @default.
- W2897783063 modified "2023-10-10" @default.
- W2897783063 title "Massively Parallel Fitness Profiling Reveals Multiple Novel Enzymes in <i>Pseudomonas putida</i> Lysine Metabolism" @default.
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- W2897783063 doi "https://doi.org/10.1128/mbio.02577-18" @default.
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- W2897783063 hasPublicationYear "2019" @default.
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