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Literature summary extracted from

  • Poulsen, L.L.; Ziegler, D.M.
    The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies (1979), J. Biol. Chem., 254, 6449-6455.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.8 64000
-
SDS-PAGE Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.8 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.8 N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O ordered ter-bi mechanism with an irreversible step between the second and third substrate, NADPH is added first, followed by O2 and the oxidizable organic substrate last Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.8 liver
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.8 N,N-dimethylaniline + NADPH + O2
-
Sus scrofa N,N-dimethylaniline N-oxide + NADP+ + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.14.13.8 ? x * 64000, SDS-PAGE, active enzyme exists as aggregating units of the monomer, amino acid composition Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.8 8.4
-
-
Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.8 FAD flavoprotein Sus scrofa