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Bottom: three-dimensional structure of the enzyme with the domains identified by color. The bound substrate NADPH (red) and cofactors FAD and FMN (yellow) are indicated. , 2004a. Electron transfer by diflavin reductases. Biochem. Biophys. , 1993). The housefly P450 reductase gene codes for a protein of 671 amino acids, and was mapped to chromosome III. The P450 reductases of other insects are very similar to the housefly enzyme – 82% identity for the D. , 2000), and 75% identity for the A. , 2003).

P450 at 82 kDa and adrenodoxin at 73 kDa) was also a surprising feature of that study. , 1993). Weirich et al. (1996) compared the apparent Km and specific activities of the mitochondrial and microsomal E20MO activities of Manduca sexta larval midgut. They concluded that at physiological ecdysone titers, despite a higher specific activity, the mitochondrial E20MO would contribute less than one-eighth the activity of the microsomal form. The probable existence of several genes encoding P450s with E20MO activity was suggested (Feyereisen, 1999).

The housefly P450 reductase gene codes for a protein of 671 amino acids, and was mapped to chromosome III. The P450 reductases of other insects are very similar to the housefly enzyme – 82% identity for the D. , 2000), and 75% identity for the A. , 2003). The insect, mammalian, and yeast enzymes are functionally interchangeable in reconstituted systems of the purified proteins or in heterologous expression systems. However, no detailed study has documented how well a mammalian or yeast P450 reductase can support the activity of an insect P450 when compared to the cognate insect P450 reductase.

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