Expression and activity of a house-fly cytochrome P450, CYP6D1, in Drosophila melanogaster

The cytochrome P450 system of animals comprises many individual cytochromes P450 in addition to a single cytochrome P450 reductase and cytochrome b5. Although individual genes of the cytochrome P450 superfamily are highly diverged, the P450 reductase and cytochrome b5 remain more conserved across ta...

Full description

Saved in:
Bibliographic Details
Published in:Insect molecular biology 2000-10, Vol.9 (5), p.441-449
Main Authors: Korytko, P. J., Maclntyre, R. J., Scott, J. G.
Format: Article
Language:English
Subjects:
activity
Animals
Animals, Genetically Modified
Aryl Hydrocarbon Hydroxylases - metabolism
Crosses, Genetic
CYP6D1 gene
CYP6D1 protein
cytochrome
cytochrome b
Cytochrome P-450 Enzyme System - genetics
Cytochrome P-450 Enzyme System - metabolism
Cytochrome P450 Family 6
cytochrome P450 monooxygenases
cytochrome P450 reductase
Cytochromes b5 - metabolism
DNA, Complementary
Drosophila
Drosophila melanogaster
Drosophila melanogaster - genetics
Drosophila melanogaster - metabolism
expression
Female
Genes, Insect
Hot Temperature
house fly
Houseflies - genetics
Houseflies - metabolism
Insect Proteins
Male
Microsomes - metabolism
NADPH-Ferrihemoprotein Reductase - metabolism
P450 reductase
Recombinant Proteins - metabolism
Transformation, Genetic
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The cytochrome P450 system of animals comprises many individual cytochromes P450 in addition to a single cytochrome P450 reductase and cytochrome b5. Although individual genes of the cytochrome P450 superfamily are highly diverged, the P450 reductase and cytochrome b5 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 b5.
ISSN:0962-1075
1365-2583
DOI:10.1046/j.1365-2583.2000.00207.x