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Prior to designation as distinct species, an appellation presently in question, the tobacco aphid, Myzus nicotianae Blackman (Homoptera: Aphididae), was classified as a tobacco‐feeding form of the green peach aphid, Myzus persicae (Sulzer). In this study, RAPD polymorphisms distinguished members of the Myzus persicae complex (M. persicae and M. nicotianae) from three outgroup Myzus species (M. cerasi (F.), M. hemerocallis Takahashi, and M. varians Davidson). Polymorphisms within the complex did not separate populations on the basis of host association (tobacco versus other host plants) or geographic origin (collections from the United States, Europe, and Japan). Similarly, while GC‐MS analysis of cuticular hydrocarbon profiles revealed both developmental and inter‐populational differences within the M. persicae complex, it did not separate populations of tobacco feeding aphids from those collected off non‐tobacco hosts. Finally, with the exception of their responses to a choice between lettuce and collards, the host preference behavior of a green peach aphid population, a red tobacco aphid population, and a green tobacco aphid population was indistinguishable in host preference experiments. These results add to a growing body of evidence suggesting M. nicotianae and M. persicae are conspecific.

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FMO5 encodes a protein of 533 amino acids with a predicted molecular weight of 60.0 kDa and 84.1% identity to human FMO5 and 83-84% identity to other FMO5 orthologs. Two GxGxxG putative pyrophosphate binding domains exist beginning at positions 9 and 191 for FMO1, and 10 and 192 for FMO5. Mouse FMO1 and FMO5 were expressed in E. coli and show similar mobility to the native proteins as determined by SDS-PAGE. The expressed FMO1 protein showed activity toward methimazole, and FMO5 was active toward noctylamine. In addition, FMO1 was shown to metabolize radiolabeled phorate, whereas FMO5 showed no activity toward phorate.