title: A human cytochrome P-450 characterized by inhibition studies as the sparteine-debrisoquine monooxygenase.
abstract: The present study compares the debrisoquine monooxygenase and the sparteine monooxygenase activities of human liver microsomes. In the presence of 14 competitive inhibitors, apparent inhibition constants (Ki) as determined by these two activities ranged over four orders of magnitude with a correlation coefficient 0.99. These in vitro results represent the strongest evidence to date that the debrisoquine monooxygenase and the sparteine monooxygenase are identical and involve a single isozyme of cytochrome P-450.
mesh_terms: D019389:Cytochrome P-450 CYP2D6; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D003647:Debrisoquin / Q000378:metabolism*; D006801:Humans; D007546:Isoquinolines / Q000378:metabolism*; D008862:Microsomes, Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000037:antagonists & inhibitors*; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000037:antagonists & inhibitors*; D013034:Sparteine / Q000378:metabolism*
chemical_list: D007546:Isoquinolines; D013034:Sparteine; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D010105:Oxygenases; D019389:Cytochrome P-450 CYP2D6; D003647:Debrisoquin