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Literature summary for 1.4.3.14 extracted from

  • Trisrivirat, D.; Lawan, N.; Chenprakhon, P.; Matsui, D.; Asano, Y.; Chaiyen, P.
    Mechanistic insights into the dual activities of the single active site of L-lysine oxidase/monooxygenase from Pseudomonas sp. AIU 813 (2020), J. Biol. Chem., 295, 11246-11261 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.14

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. AIU 813
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Pseudomonas sp. AIU 813 W6JQJ6
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + O2 + H2O enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase Pseudomonas sp. AIU 813 6-amino-2-oxohexanoate + NH3 + H2O2
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 ?
L-lysine + O2 + H2O the mechanistic features are reported that are important for allowing the single active site of L-LOX/MOG to catalyze the two reactions of apparent monooxygenation and the oxidation of the flavoprotein oxidase Pseudomonas sp. AIU 813 6-amino-2-oxohexanoate + NH3 + H2O2
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 ?
L-ornithine + O2 + H2O the mechanistic features are reported that are important for allowing the single active site of L-LOX/MOG to catalyze the two reactions of apparent monooxygenation and the oxidation of the flavoprotein oxidase Pseudomonas sp. AIU 813 5-amino-2-oxopentanoic acid + NH3 + H2O2
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 ?
L-ornithine + O2 + H2O enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase Pseudomonas sp. AIU 813 5-amino-2-oxopentanoate + NH3 + H2O2
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 ?

Synonyms

Synonyms Comment Organism
L-LOX/MOG
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 Pseudomonas sp. AIU 813
L-lysine oxidase/monooxygenase
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 Pseudomonas sp. AIU 813

Cofactor

Cofactor Comment Organism Structure
FAD FAD-dependent oxidase Pseudomonas sp. AIU 813