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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.13.12.2 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
3.5.1.30 synthesis the enzyme is useful to produce the nylon-5 monomer 5-aminovalerate from L-lysine in large scale Pseudomonas putida
3.5.1.30 synthesis 2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are coexpressed 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)

EC Number Cloned (Comment) Organism
1.13.12.2 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
1.13.12.2 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
3.5.1.30 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
3.5.1.30 gene davA, coexpression with gene davB from construct pETDuet-DavAB in Escherichia coli strain BL21(DE3) Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.2 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
3.5.1.30 additional information lysine 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. Then, 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, strain optimization for large scale production, overview. Overexpression of transport proteins improves the production of 5-aminovalerate from L-lysine in Escherichia coli. The optimum catalytic conditions are determined to be reaction temperature 30°C, substrate concentration 40 g/l, and biocatalyst concentration 60 OD600nm Pseudomonas putida

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.12.2 L-lysine + O2 Pseudomonas putida
-
 5-aminopentanamide + CO2 + H2O
-
 ?
3.5.1.30 5-aminopentanamide + H2O Pseudomonas putida
-
 5-aminopentanoate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.2 Pseudomonas putida
-
-
-
1.13.12.2 Pseudomonas putida Q88QV1
-
-
3.5.1.30 Pseudomonas putida Q88QV2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.2 L-lysine + O2
-
 Pseudomonas putida 5-aminopentanamide + CO2 + H2O
-
 ?
3.5.1.30 5-aminopentanamide + H2O
-
 Pseudomonas putida 5-aminopentanoate + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.2 davB
-
 Pseudomonas putida
3.5.1.30 DavA
-
 Pseudomonas putida
3.5.1.30 delta-aminovaleramidase
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.12.2 30
-
-
 Pseudomonas putida
3.5.1.30 30
-
 in vivo activity Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.13.12.2 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
3.5.1.30 metabolism 5-aminovalerate, produced by the enzyme DavA, is an intermediate of L-lysine catabolism that is called aminovalerate pathway in Pseudomonas putida Pseudomonas putida