Journal of Veterinary Medical Science · 2010 · 10 citations · 15 references
MedicineBiochemistryPharmacologyCellular MetabolismDrug MetabolismMetabolismCytochrome P450 EnzymesCytochrome P450-mediated MetabolismDrug-metabolizing EnzymesHepatic Drug MetabolismHepatic MetabolismSpecies Differences In Drug MetabolismCdna CloningCyp2d6 Drug MetabolismCytochrome P450 2D6Cytochrome P450 Enzyme ActivityCytochrome P450 Metabolic PathwaysOpen Reading Frame AnnotationOpen Reading Frame IdentificationSpecies Differences In Xenobiotic Metabolism
Cytochrome P450 2D (CYP2D) is one of the major metabolizing enzymes for drugs in humans and other mammals. Although domestic cats (Felis catus) are the most common companion animal in many countries, the properties of their drug-metabolizing system are largely unknown. We determined the complete cDNA sequence of the CYP2D open reading frame (1,500 bp) with both 5'- and 3'-untranslated regions in domestic cats. Feline CYP2D consists of 500 deduced amino acids and shows high homology with CYP2Ds of primates and rodents, particularly with the canine CYP2D homologue, and was designated as CYP2D6 based on its genomic structure. CYP2D6 transcripts were expressed predominantly in the liver and to a much lesser in the testis, suggesting the role of xenobiotic metabolism in the liver.
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David R. Nelson · Human Genomics · 2009 · 1K citations · Full text
Nomenclature for human CYP2D6 alleles
Ann K. Daly, Jürgen Brockmöller, Franck Broly et al. · Pharmacogenetics · 1996 · 400 citations
Robin E. Pearce, Denise Greenway, Andrew Parkinson · Archives of Biochemistry and Biophysics · 1992 · 189 citations
Medicine, Biochemistry, Pharmacology +16