The cytochrome P450 system of animals comprises many individual cytochromes
P450 in addition to a single cytochrome P450 reductase and cytochrome b(5)
. Although individual genes of the cytochrome P450 superfamily are highly d
iverged, the P450 reductase and cytochrome b(5) remain more conserved acros
s taxa. Here, we describe the transformation of Drosophila melanogaster wit
h a house-fly-specific cytochrome P450, CYP6D1. Functional activity of ecto
pically expressed cytochromes P450 requires successful interaction between
the transgenic P450 and the requisite coenzymes of the host organism. Trans
formed Drosophila, but not controls, contained CYP6D1 protein as identified
by protein immunoblotting, elevated total P450 and elevated CYP6D1 enzymat
ic activity. These data demonstrate that house-fly CYP6D1 can interact with
low to moderate efficiency with Drosophila P450 reductase and cytochrome b
(5).