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First published on March 18, 2005; DOI: 10.1124/dmd.104.003392

0090-9556/05/3306-862-865$20.00
DMD 33:862-865, 2005

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MINIPIG CYTOCHROME P450 2E1: COMPARISON WITH HUMAN ENZYME

Jana Baranová, Eva Anzenbacherová, Pavel Anzenbacher, and Pavel Soucek

Institute of Pharmacology (J.B., P.A.) and Institute of Medical Chemistry and Biochemistry (E.A.), Faculty of Medicine, Palacky University, Olomouc; and National Institute of Public Health, Prague (P.S.), Czech Republic

Cytochrome P450 2E1 was isolated from minipig liver microsomes. The protein has been cloned and the respective cDNA sequenced (GenBank Accession Number AY581116). Minipig CYP2E1 is two residues shorter than its human ortholog. The only difference between pig and minipig sequence is the presence of aspartic acid residue in position 346 contrary to valine in the pig enzyme. Minipig CYP2E1 was shown to be able to convert two prototypical substrates of human CYP2E1, chlorzoxazone and p-nitrophenol, to the respective metabolites. The experiments performed with both the liver microsomal fraction and reconstituted systems with human or minipig CYP2E1 confirmed the similarity of both enzymes. Inhibition with diethyldithiocarbamate gave comparable Ki values for minipig as well as for the human CYP2E1. The results indicate that the systems containing minipig CYP2E1 may be used to model the respective CYP2E1-catalyzed reactions of drug metabolism in humans.

Address correspondence to: Dr. Pavel Anzenbacher, Institute of Pharmacology, Faculty of Medicine, Palacky University, Hnevotinska 3, CZ-775 15 Olomouc, Czech Republic. E-mail anzen{at}tunw.upol.cz




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