Literature summary 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 .
Application
EC Number |
Application |
Comment |
Organism |
---|
1.13.12.2 |
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)
EC Number |
Cloned (Comment) |
Organism |
---|
1.13.12.2 |
gene davB, recombinant expression of His-tagged enzyme DavB in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase |
Pseudomonas putida |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.13.12.2 |
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)
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 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.13.12.2 |
Pseudomonas putida |
Q88QV1 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.13.12.2 |
recombinant His-tagged enzyme DavB from Escherichia coli by ncikel affinity chromatography |
Pseudomonas putida |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
1.13.12.2 |
6.1 |
- |
purified recombinant enzyme, pH 7.0, 30°C |
Pseudomonas putida |
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 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.13.12.2 |
? |
x * 62400, recombinant His-tagged enzyme, SDS-PAGE |
Pseudomonas putida |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.13.12.2 |
davB |
- |
Pseudomonas putida |
1.13.12.2 |
L-lysine monooxygenase |
- |
Pseudomonas putida |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.13.12.2 |
30 |
- |
assay at |
Pseudomonas putida |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.13.12.2 |
7 |
- |
assay at |
Pseudomonas putida |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.13.12.2 |
FAD |
DavB is a FAD-dependent monooxygenase |
Pseudomonas putida |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.13.12.2 |
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 |
1.13.12.2 |
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 |