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
-
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
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Crystallization
Crystallization on EC 1.13.12.2 - lysine 2-monooxygenase
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purified recombinant His-tagged wild-type and SeMet-labeled enzymes, sitting-drop vapor diffusion method, mixing of 0.001 ml of protein solution, consisting of 20 mg/mL protein in 20 mM HEPES-NaOH, pH 7.6, and 0.001 ml of reservoir solution, consisting of 8% PEG 4000 and 0.1 M Na-acetate, pH 4.6, Se-Met substituted crystals are obtained using reservoir solution consisting of 16% PEG 3350, 0.02 M citric acid, and 0.08 M bis-Tris propane-HCl, pH 8.8, 20°C, X-ray diffraction structure determination and analysis at 1.90 and 2.20 A resolution respectively
structures of L-AAO/MOG complexed with L-Lys, L-ornithine, and L-Arg. Residue Asp238 is located at the ceiling of a long hydrophobic pocket and forms a strong interaction with the terminal, positively charged group of the substrates. In the ligand-free structure, there are two channels connecting the active site and solvent, and a short region located at the dimer interface is disordered. In the L-Lys complex structure, a loop region is displaced to plug the channels