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The existence of several genes encoding P450s with E20MO activity could account for the dual localization and complex regulation of the enzyme’s activity. On the other hand, alternative splicing or post-translational modifications of a single gene product could also lead to the microsomal and mitochondrial forms, and this seems more likely, given the unusual N-terminal sequences of CYP314A1 proteins (see below). Interestingly, both microsomal and mitochondrial activities of the Spodoptera littoralis fat body E20MO were reported to be reversibly activated by phosphorylation (Hoggard and Rees, 1988; Hoggard et al., 1989). Cases of post-translational modifications of P450 enzymes by reversible phosphorylation are not very common, and this observation would suggest that the S. littoralis fat body E20MOs are products of the same gene.