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Literature summary for 1.13.12.2 extracted from

  • Matsui, D.; Im, D.H.; Sugawara, A.; Fukuta, Y.; Fushinobu, S.; Isobe, K.; Asano, Y.
    Mutational and crystallographic analysis of L-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 Interconversion between oxidase and monooxygenase activities (2014), FEBS Open Bio, 4, 220-228 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene laao/mog, recombinant expression of His-tagged wild-type enzyme L-amino acid oxidase/monooxygenase in Escherichia coli strain BL21(DE3), selenomethionine-labeled enzyme is expressed in Escherichia coli strain BL21 CodonPlus (DE3)-RIL-X Pseudomonas sp. AIU 813

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Pseudomonas sp. AIU 813

Protein Variants

Protein Variants Comment Organism
C254A site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254D site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254E site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254F site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254G site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254H site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
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 Pseudomonas sp. AIU 813
C254L site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254L site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254M site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254N site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254P site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254Q site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254R site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254S site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254T site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254V site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254W site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254W site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813
C254Y site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type Pseudomonas sp. AIU 813

Inhibitors

Inhibitors Comment Organism Structure
additional information 4-chloromercuribenzoate inhibits only the oxidase activity of the bifunctional enzyme, while the monooxygenase activity is not affected Pseudomonas sp. AIU 813

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine + O2 Pseudomonas sp. AIU 813
-
5-aminopentanamide + CO2 + H2O
-
?
additional information Pseudomonas sp. AIU 813 bifunctional L-amino acid oxidase, EC 1.4.3.2, of Pseudomonas sp. AIU813, renamed as L-amino acid oxidase/monooxygenase (L-AAO/MOG), exhibits L-lysine 2-monooxygenase as well as oxidase activity ?
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. AIU 813 W6JQJ6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and and SeMet-labeled enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, anion exchange chromatography, and gel filtration Pseudomonas sp. AIU 813

Reaction

Reaction Comment Organism Reaction ID
L-lysine + O2 = 5-aminopentanamide + CO2 + H2O a slight difference of the binding position of a substrate dictates the activity of this type of enzyme as oxidase or monooxygenase, residue C254 is involved Pseudomonas sp. AIU 813

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.108
-
purified recombinant enzyme, pH 7,0, 30°C, substrate L-arginine Pseudomonas sp. AIU 813
0.146
-
purified recombinant enzyme, pH 7,0, 30°C, substrate L-ornithine Pseudomonas sp. AIU 813
0.532
-
purified recombinant enzyme, pH 7,0, 30°C, substrate L-lysine Pseudomonas sp. AIU 813

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine + O2
-
Pseudomonas sp. AIU 813 4-guanidinobutanamide + CO2 + H2O
-
?
L-lysine + O2
-
Pseudomonas sp. AIU 813 5-aminopentanamide + CO2 + H2O
-
?
L-lysine + O2 preferred substrate Pseudomonas sp. AIU 813 5-aminopentanamide + CO2 + H2O
-
?
L-ornithine + O2
-
Pseudomonas sp. AIU 813 4-aminobutanamide + CO2 + H2O
-
?
additional information bifunctional L-amino acid oxidase, EC 1.4.3.2, of Pseudomonas sp. AIU813, renamed as L-amino acid oxidase/monooxygenase (L-AAO/MOG), exhibits L-lysine 2-monooxygenase as well as oxidase activity Pseudomonas sp. AIU 813 ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure of L-AAO/MOG, overview. The key residue for the activity conversion of L-AAO/MOG, Cys-254, is located near the aromatic cage (Trp418, Phe473, and Trp516) Pseudomonas sp. AIU 813

Synonyms

Synonyms Comment Organism
L-AAO/MOG
-
Pseudomonas sp. AIU 813
L-amino acid oxidase/monooxygenase
-
Pseudomonas sp. AIU 813
L-lysine 2-monooxygenase
-
Pseudomonas sp. AIU 813

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Pseudomonas sp. AIU 813

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Pseudomonas sp. AIU 813

Cofactor

Cofactor Comment Organism Structure
FAD
-
Pseudomonas sp. AIU 813

General Information

General Information Comment Organism
evolution the bifunctional enzyme L-AAO/MOG belongs to the MAO family of enzymes Pseudomonas sp. AIU 813
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 Pseudomonas sp. AIU 813