A new variant allele CYP2D6*62 (g.4044C>T; R441C) of the drugmetabolizing cytochrome P450 (P450) CYP2D6 was identified in a person with reduced sparteine oxidation phenotype, which was unexpected based on a genetic CYP2D6*1A/*41 background. The recombinantly expressed variant protein had no activity toward propafenone as a result of missing heme incorporation. Sequence alignment revealed that t...

A new variant allele CYP2D6*62 (g.4044C>T; R441C) of the drugmetabolizing cytochrome P450 (P450) CYP2D6 was identified in a person with reduced sparteine oxidation phenotype, which was unexpected based on a genetic CYP2D6*1A/*41 background. The recombinantly expressed variant protein had no activity toward propafenone as a result of missing heme incorporation. Sequence alignment revealed that t...

A new variant allele CYP2D6*62 (g.4044C>T; R441C) of the drugmetabolizing cytochrome P450 (P450) CYP2D6 was identified in a person with reduced sparteine oxidation phenotype, which was unexpected based on a genetic CYP2D6*1A/*41 background. The recombinantly expressed variant protein had no activity toward propafenone as a result of missing heme incorporation. Sequence alignment revealed that t...

Dog CYP2A13 and CYP2A25 were coexpressed with dog NADPHcytochrome P450 reductase (OR) in baculovirus-infected Sf9 insect cells. CYP2A13 effectively catalyzed 7-ethoxycoumarin (7EC) deethylation and coumarin hydroxylation with apparent Km values of 4.8 and 2.1 M, respectively, similar to those observed using dog liver microsomes (7.5 and 0.75 M, respectively). CYP2A25 exhibited much lower affini...

Mammalian flavin-containing monooxygenase (FMO) enzymes catalyze oxidation at nucleophilic, heteroatom centers and are important for drug, xenobiotic, and endogenous substrate metabolism. In human liver, human FMO3 (hFMO3) is the most abundant FMO isoform and is known to contribute to the hepatic clearance of a variety of clinical drugs. The purpose of the current study was to express and compa...

Mammalian flavin-containing monooxygenase (FMO) enzymes catalyze oxidation at nucleophilic, heteroatom centers and are important for drug, xenobiotic, and endogenous substrate metabolism. In human liver, human FMO3 (hFMO3) is the most abundant FMO isoform and is known to contribute to the hepatic clearance of a variety of clinical drugs. The purpose of the current study was to express and compa...

Mammalian flavin-containing monooxygenase (FMO) enzymes catalyze oxidation at nucleophilic, heteroatom centers and are important for drug, xenobiotic, and endogenous substrate metabolism. In human liver, human FMO3 (hFMO3) is the most abundant FMO isoform and is known to contribute to the hepatic clearance of a variety of clinical drugs. The purpose of the current study was to express and compa...

Dog CYP2A13 and CYP2A25 were coexpressed with dog NADPHcytochrome P450 reductase (OR) in baculovirus-infected Sf9 insect cells. CYP2A13 effectively catalyzed 7-ethoxycoumarin (7EC) deethylation and coumarin hydroxylation with apparent Km values of 4.8 and 2.1 M, respectively, similar to those observed using dog liver microsomes (7.5 and 0.75 M, respectively). CYP2A25 exhibited much lower affini...

Dog CYP2A13 and CYP2A25 were coexpressed with dog NADPHcytochrome P450 reductase (OR) in baculovirus-infected Sf9 insect cells. CYP2A13 effectively catalyzed 7-ethoxycoumarin (7EC) deethylation and coumarin hydroxylation with apparent Km values of 4.8 and 2.1 M, respectively, similar to those observed using dog liver microsomes (7.5 and 0.75 M, respectively). CYP2A25 exhibited much lower affini...

Dog CYP2A13 and CYP2A25 were coexpressed with dog NADPHcytochrome P450 reductase (OR) in baculovirus-infected Sf9 insect cells. CYP2A13 effectively catalyzed 7-ethoxycoumarin (7EC) deethylation and coumarin hydroxylation with apparent Km values of 4.8 and 2.1 M, respectively, similar to those observed using dog liver microsomes (7.5 and 0.75 M, respectively). CYP2A25 exhibited much lower affini...