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Expression and activity of a house‐fly cytochrome P450, CYP6D1, in Drosophila melanogaster
Author(s) -
Korytko P. J.,
Maclntyre R. J.,
Scott J. G.
Publication year - 2000
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.2000.00207.x
Subject(s) - cytochrome p450 , drosophila melanogaster , biology , cytochrome p450 reductase , cytochrome b5 , drosophila (subgenus) , transgene , cytochrome , reductase , cytochrome b , gene , biochemistry , genetics , enzyme , phylogenetic tree
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 diverged, the P450 reductase and cytochrome b 5 remain more conserved across taxa. Here, we describe the transformation of Drosophila melanogaster with a house‐fly‐specific cytochrome P450, CYP6D1. Functional activity of ectopically expressed cytochromes P450 requires successful interaction between the transgenic P450 and the requisite coenzymes of the host organism. Transformed Drosophila , but not controls, contained CYP6D1 protein as identified by protein immunoblotting, elevated total P450 and elevated CYP6D1 enzymatic activity. These data demonstrate that house‐fly CYP6D1 can interact with low to moderate efficiency with Drosophila P450 reductase and cytochrome b 5 .