1.13.12.2: lysine 2-monooxygenase
This is an abbreviated version!
For detailed information about lysine 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.2
-
1.13.12.2
-
putida
-
5-aminovalerate
-
glutarate
-
fed-batch
-
nylon
-
synthesis
-
fluorescens
-
semialdehyde
-
1,5-pentanediol
-
polyamides
-
glutamicum
-
flavoproteins
-
corynebacterium
-
l-pipecolate
-
biotechnology
-
4-aminobutyrate
-
five-carbon
-
amidohydrolase
-
his6-tagged
-
cadaverine
-
biomass
-
transaminase
-
permease
-
byproduct
-
deamination
-
putrescine
-
bio-based
-
feedstock
-
codon-optimized
- 1.13.12.2
- putida
- 5-aminovalerate
- glutarate
-
fed-batch
-
nylon
- synthesis
- fluorescens
- semialdehyde
- 1,5-pentanediol
- polyamides
- glutamicum
- flavoproteins
-
corynebacterium
- l-pipecolate
- biotechnology
- 4-aminobutyrate
-
five-carbon
-
amidohydrolase
-
his6-tagged
- cadaverine
- biomass
- transaminase
-
permease
-
byproduct
-
deamination
- putrescine
-
bio-based
-
feedstock
-
codon-optimized
Reaction
Synonyms
davB, L-AAO/MOG, L-amino acid oxidase/monooxygenase, L-LOX/MOG, L-lysine 2-monooxygenase, L-lysine monooxygenase, L-lysine oxidase/monooxygenase, L-lysine-2-monooxygenase, lysine monooxygenase, lysine oxygenase
ECTree
Advanced search results
General Information
General Information on EC 1.13.12.2 - lysine 2-monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
the bifunctional enzyme L-AAO/MOG belongs to the MAO family of enzymes
malfunction
metabolism
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
additional information
three-dimensional structure of L-AAO/MOG, overview. The key residue for the activity conversion of L-AAO/MOG, Cys254, is located near the aromatic cage (Trp418, Phe473, and Trp516). Cys254 is not directly involved in the substrate binding, but the chemical modification by 4-chloromercuribenzoate or C254I mutation has significant impact on the substrate binding via the side chain of Trp516. A slight difference of the binding position of a substrate dictates the activity of this type of enzyme as oxidase or monooxygenase
-
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
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
-
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
metabolism
-
the enzyme is involved in the aminovalerate pathway, overview
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)
metabolism
-
the enzyme is involved in the aminovalerate pathway, overview
-