A unique enzyme catalyzing the formation of 4-hydroxyaniline from 4-amino-benzoic acid in Agaricus bisporus.
A unique enzyme that catalyzes the formation of 4-hydroxyaniline from 4-aminobenzoic acid was found in the homogenate of Agaricus bisporus. The enzyme was prepared from the homogenate by (NH4)2SO4 fractionation, gel filtration and ion-exchange chromatography. The products formed from 4-aminobenzoic acid by the enzyme were shown to be 4-hydroxyaniline and CO2. The reaction required FAD, NAD(P)H and O2. These results indicate that the enzyme is a new FAD-dependent monooxygenase.
D010129:4-Aminobenzoic Acid / Q000378:metabolism*; D062365:Aminobenzoates / Q000378:metabolism*; D000627:Aminophenols / Q000378:metabolism*; D001487:Basidiomycota / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D007700:Kinetics; D013058:Mass Spectrometry; D009243:NAD / Q000378:metabolism; D010100:Oxygen
D062365:Aminobenzoates; D000627:Aminophenols; D009243:NAD; D005182:Flavin-Adenine Dinucleotide; D010100:Oxygen; D010129:4-Aminobenzoic Acid