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Literature summary for 1.13.12.2 extracted from

  • Liu, P.; Zhang, H.; Lv, M.; Hu, M.; Li, Z.; Gao, C.; Xu, P.; Ma, C.
    Enzymatic production of 5-aminovalerate from L-lysine using L-lysine monooxygenase and 5-aminovaleramide amidohydrolase (2014), Sci. Rep., 4, 5657 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.12.2

Application

Application Comment Organism
synthesis the enzyme can be used for production of 5-aminovalerate, a potential C5 platform chemical for synthesis of valerolactam, 5-hydroxyvalerate, glutarate, and 1,5-pentanediol. Escherichia coli is engineered for production of 5-aminovalerate from L-lysine by coupled reaction of recombinant DavB, L-lysine monooxygenase, and recombinant DavA, 5-aminovaleramidase. Because L-lysine is an industrial fermentation product, the two-enzyme coupled system presents a promising alternative for the production of 5-aminovalerate Pseudomonas putida

Cloned(Commentary)

Cloned (Comment) Organism
gene davB, recombinant expression of His-tagged enzyme DavB in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
additional information Escherichia coli is engineered for production of 5-aminovalerate from L-lysine by coupled reaction of recombinant DavB, L-lysine monooxygenase, and recombinant DavA, 5-aminovaleramidase, overview. Under optimal conditions, 20.8 g/l 5-aminovalerate is produced from 30 g/l L-lysine in 12 h. Hydrogen peroxide, which is produced during the process of L-lysine oxidization, will further oxidize 6-amino-2-ketocaproic acid to form 5-aminovalerate as the final product. Method optimization, overview Pseudomonas putida

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 Q88QV1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme DavB from Escherichia coli by ncikel affinity chromatography Pseudomonas putida

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.1
-
 purified recombinant enzyme, pH 7.0, 30°C Pseudomonas putida

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 62400, recombinant His-tagged enzyme, SDS-PAGE Pseudomonas putida

Synonyms

Synonyms Comment Organism
davB
-
 Pseudomonas putida
L-lysine monooxygenase
-
 Pseudomonas putida

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
FAD DavB is a FAD-dependent monooxygenase Pseudomonas putida

General Information

General Information Comment Organism
metabolism L-lysine monooxygenase (DavB) and 5-aminovaleramide amidohydrolase (DavA) play key roles in the 5-aminovalerate pathway of various microorganisms. DavB catalyzes the oxidation of L-lysine to produce 5-aminovaleramide. DavA then catalyzes 5-aminovaleramide into 5-aminovalerate Pseudomonas putida
physiological function the enzyme produces 5-aminovalerate, a metabolite of L-lysine catabolism through the aminovalerate pathway in Pseudomonas putida. L-Lysine monooxygenase (DavB) and 5-aminovaleramide amidohydrolase (DavA, EC 3.5.1.30) play key roles in the biotransformation of L-lysine into 5-aminovalerate Pseudomonas putida