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Literature summary extracted from

  • Takeda, H.; Yamamoto, S.; Kojima, Y.; Hayaishi, O.
    Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase (1969), J. Biol. Chem., 244, 2935-2941.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.12.2 2,2'-dipyridyl
-
Pseudomonas fluorescens
1.13.12.2 Mersalyl
-
Pseudomonas fluorescens
1.13.12.2 o-Iodosobenzoate
-
Pseudomonas fluorescens
1.13.12.2 p-chloromercuribenzoate
-
Pseudomonas fluorescens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.12.2 191000
-
sedimentation velocity experiments Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.2 Pseudomonas fluorescens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.2 L-arginine + O2
-
Pseudomonas fluorescens 4-guanidinobutyramide + CO2 + H2O
-
?
1.13.12.2 L-lysine + electron acceptor anaerobic conditions, electron acceptors are methylene blue, toluylene blue, phenol blue or thymol indophenol Pseudomonas fluorescens ?
-
?
1.13.12.2 L-lysine + O2 monooxygenase activity Pseudomonas fluorescens 5-aminopentanamide + CO2 + H2O
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.12.2 49
-
inactivation above Pseudomonas fluorescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.2 9.5
-
-
Pseudomonas fluorescens

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.13.12.2 7 8 4°C, several weeks, retains almost full activity Pseudomonas fluorescens

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.2 FAD contains 2 mol of FAD per mol of enzyme Pseudomonas fluorescens