Literature summary for 1.13.12.2 extracted from

Park, S.J.; Kim, E.Y.; Noh, W.; Park, H.M.; Oh, Y.H.; Lee, S.H.; Song, B.K.; Jegal, J.; Lee, S.Y.
Metabolic engineering of Escherichia coli for the production of 5-aminovalerate and glutarate as C5 platform chemicals (2013), Metab. Eng., 16, 42-47.

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinantly expressed in Escherichia coli. 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	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-lysine + O2	-	Pseudomonas putida	5-aminovaleramide + CO2 + H2O	-	?
L-lysine + O2	-	Pseudomonas putida ATCC 12633	5-aminovaleramide + CO2 + H2O	-	?

Synonyms

Synonyms	Comment	Organism
lysine monooxygenase	-	Pseudomonas putida

General Information

General Information	Comment	Organism
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	Pseudomonas putida

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Release 2023.1 (January 2023)