Corning® Supersomes™ Human CYP2D6*1 (Val374) + Oxidoreductase, 0.5 enzyme prepared from insect cells infected with baculovirus containing desired cDNAs
CYP2D6 is responsible for a common human genetic defect in the oxidation of many drugs, termed the debrisoquine or sparteine polymorphism. There are on the order of 70 allelic variants of CYP2D6, many resulting in inactive protein or diminished activity. Roughly 10% of Caucasians are poor metabolizers (PM) and lack functional CYP2D6 protein. The CYP2D6 enzyme accounts for the metabolism of roughly 30% of all prescribed medications.
Substrates of CYP2D6 include bufuralol, debrisoquine, sparteine, dextromethorphan, nortriptyline, propanalol, and numerous other drugs. Bufuralol 1′-hydroxylation and dextromethorphan N-demethylation are probe substrate for in vitro activity testing. Quinidine is a potent selective inhibitor of the CYP2D6. CYP2D6 is also capable of activating the tobacco smoke-derived procarcinogen, NNK.
One of the most common allelic variants of CYP2D6 is CYP2D6*10. This allele is quite common in Asian populations and contains two amino acid substitutions relative to the wild type CYP2D6*1 (Pro34Ser and Ser486Thr). CYP2D6*10 has diminished catalytic activity relative to CYP2D6*1.