Literature summary for 1.13.12.2 extracted from

Li, Z.; Xu, J.; Jiang, T.; Ge, Y.; Liu, P.; Zhang, M.; Su, Z.; Gao, C.; Ma, C.; Xu, P.
Overexpression of transport proteins improves the production of 5-aminovalerate from L-lysine in Escherichia coli (2016), Sci. Rep., 6, 30884 .

Search for more literature for 1.13.12.2

Application

Application	Comment	Organism
synthesis	2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are co-expressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine. PP2911 (4-aminobutyrate transporter in Pseudomonas putida) and LysP (the lysine specific permease in Escherichia coli) are overexpressed to promote 5-aminovalerate production using whole cells of recombinant Escherichia coli. The constructed Escherichia coli strain overexpressing transport proteins exhibits good 5-aminovalerate production performance and might serve as a promising biocatalyst for 5-aminovalerate production from L-lysine. This strategy not only shows an efficient process for the production of nylon monomers but also might be used in production of other chemicals	Pseudomonas putida

Cloned(Commentary)

Cloned (Comment)	Organism
2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are coexpressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine	Pseudomonas putida
gene davB, recombinant expression in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, lysine specific permease LysP, and PP2911, a 4-aminobutyrate transporter, since Escherichia coli is unable to assimilate L-lysine and to secrete 5-aminovalerate	Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
additional information	recombinant expression of gene davB in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, lysine specific permease LysP, and PP2911, a 4-aminobutyrate transporter, since Escherichia coli is unable to assimilate L-lysine and to secrete 5-aminovalerate, reconstitution of Pseudomonas putida 5-aminovalerate pathway for production of 5-aminovalerate from L-lysine in Escherichia coli, biocatalysis conditions and method optimization, overview. Optimal temperature is 30°C	Pseudomonas putida

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasm	-	Pseudomonas putida	5737	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-lysine + O2	Pseudomonas putida	-	5-aminopentanamide + CO2 + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-
Pseudomonas putida	Q88QV1	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
davB	-	Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	-	Pseudomonas putida

General Information

General Information	Comment	Organism
metabolism	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)	Pseudomonas putida

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)