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
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1.13.12.2
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putida
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5-aminovalerate
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glutarate
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fed-batch
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nylon
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synthesis
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fluorescens
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semialdehyde
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1,5-pentanediol
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polyamides
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glutamicum
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flavoproteins
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corynebacterium
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l-pipecolate
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biotechnology
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4-aminobutyrate
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five-carbon
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amidohydrolase
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his6-tagged
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cadaverine
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biomass
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transaminase
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permease
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byproduct
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deamination
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putrescine
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bio-based
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feedstock
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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
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amidohydrolase
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his6-tagged
- cadaverine
- biomass
- transaminase
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permease
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byproduct
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deamination
- putrescine
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bio-based
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feedstock
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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
1.13.12.2 lysine 2-monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.12.2 - lysine 2-monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C254A
site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type
C254D
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254E
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254F
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254G
site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type
C254H
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254I
site-directed mutagenesis, the mutant enzyme shows 5times higher specific activity of oxidase activity compared to wild-type, while the lysine 2-monooxygenase activity is completely abolished
C254L
C254M
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254N
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254P
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254Q
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254R
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254S
site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type
C254T
site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type
C254V
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254W
C254Y
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
D238A
the interaction of Asp238 with the terminal, positively charged group of the substrates is critical for substrate binding but not for catalytic control between the oxidase/monooxygenase activities
D238F
mutant exhibits altered substrate specificity to long hydrophobic substrates
additional information
C254L
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254L
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254W
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254W
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
additional information
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engineering of a recombinant Escherichia coli strain expressing the davB and davA genes for bioconversion of L-lysine to 5-aminovaleric acid resulting in low levels of 5-aminovalerate. Development of metabolically engineered Corynebacterium glutamicum strains for enhanced fermentative production of 5-aminovalerate from glucose. Expression of the Corynebacterium glutamicum codon-optimized davA gene fused with His6-Tag at its N-terminus and the davB gene as an operon under a strong synthetic H36 promoter (plasmid p36davAB3) in Corynebacterium glutamicum strain BE (pJS38) enables the most efficient production of 5-aminovalerate. The construct containing the His6-tagged variant produces substantially more 5-aminovalerate compared to that produced using the construct lacking the His-tag, possibly because of the improved stability afforded by the 5'-modification, which results in higher expression of the davAB genes in the recombinant Corynebacterium glutamicum BE strain. Deletion of the gabT gene (EC 2.6.1.19), encoding 4-aminobutyrate aminotransferase, improves the 5-aminovalerate production
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
additional information
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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
additional information
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Escherichia coli strain WL3110, coexpressing genes davB and davA, is used as whole-cell-catalyst for production of 5-aminovalerate from L-lysine, method optimization, overview
additional information
generation of an optimized production system for 5-aminovalerate from L-lysine in Escherichia coli by overexpressing genes davA and davB, encoding 5-aminovaleramide amidohydrolase and L-lysine 2-monooxygenase, the effects of induction conditions, reaction temperature, metal ion additives, and cell permeability on the whole-cell biocatalyst system are evaluated to improve biocatalytic efficiency, overview. Presence of Mn2+ and Ca2+ enhances the activity of whole-cell BL-22A-RB-YB system. Increased permeabilization of Escherichia coli BL-22A-RB-YB cells following surfactant treatment with TritonX-100 results in improved L-lysine consumption and 5-aminovalerate synthesis rate
additional information
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installation of an expression system for production of 5-aminovalerate in Corynebacterium glutamicum strain LYS-12 by coexpressing gene davA, encoding 5-aminovaleramidase, and davB, encoding lysine monooxygenase, resulting in strains AVA-1-3. 5-Aminovalerate production is established. Related to the presence of endogenous genes coding for 5-aminovalerate transaminase (gabT) and glutarate semialdehyde dehydrogenase, 5-aminovalerate is partially converted to glutarate. Residual L-lysine is secreted as by-product. Putative gabT gene is deleted to enhance 5-aminovalerate production, method optimization and evaluation, overview
additional information
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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
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
additional information
-
engineering of a recombinant Escherichia coli strain expressing the davB and davA genes for bioconversion of L-lysine to 5-aminovaleric acid resulting in low levels of 5-aminovalerate. Development of metabolically engineered Corynebacterium glutamicum strains for enhanced fermentative production of 5-aminovalerate from glucose. Expression of the Corynebacterium glutamicum codon-optimized davA gene fused with His6-Tag at its N-terminus and the davB gene as an operon under a strong synthetic H36 promoter (plasmid p36davAB3) in Corynebacterium glutamicum strain BE (pJS38) enables the most efficient production of 5-aminovalerate. The construct containing the His6-tagged variant produces substantially more 5-aminovalerate compared to that produced using the construct lacking the His-tag, possibly because of the improved stability afforded by the 5'-modification, which results in higher expression of the davAB genes in the recombinant Corynebacterium glutamicum BE strain. Deletion of the gabT gene (EC 2.6.1.19), encoding 4-aminobutyrate aminotransferase, improves the 5-aminovalerate production
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