1 research outputs found
Biocatalytic Characterization of Human FMO5: Unearthing Baeyer–Villiger Reactions in Humans
Flavin-containing mono-oxygenases
are known as potent drug-metabolizing
enzymes, providing complementary functions to the well-investigated
cytochrome P450 mono-oxygenases. While human FMO isoforms are typically
involved in the oxidation of soft nucleophiles, the biocatalytic activity
of human FMO5 (along its physiological role) has long remained unexplored.
In this study, we demonstrate the atypical <i>in vitro</i> activity of human FMO5 as a Baeyer–Villiger mono-oxygenase
on a broad range of substrates, revealing the first example to date
of a human protein catalyzing such reactions. The isolated and purified
protein was active on diverse carbonyl compounds, whereas soft nucleophiles
were mostly non- or poorly reactive. The absence of the typical characteristic
sequence motifs sets human FMO5 apart from all characterized Baeyer–Villiger
mono-oxygenases so far. These findings open new perspectives in human
oxidative metabolism