Human cytochrome P450 reductase has been used in a study to assess the biocatalytic synthesis and structure elucidation of cyclized metabolites of the deacetylase inhibitor panobinostat (LBH589). Human cytochrome P450 reductase has also been used in a study to investigate the effects of coupled motions on electrons along the human microsomal P450 chains.
This human, recombinant protein is isolated from insect cells infected with a baculovirus containing the cDNA for human cytochrome P450 reductase. It is purified by affinity chromatography.
The enzyme catalyses electron transfer to cytochrome P450. This system plays a major role in detoxification of drugs and xenobiotics, activation of carcinogens, and metabolism of endogenous substrates such as steroids.
