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

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Received for publication December 17, 2004.
Revised March 16, 2005.
Accepted for publication March 16, 2005.

Minipig cytochrome P450 2E1: comparison with human enzyme

Jana Baranova 1, Eva Anzenbacherova 1, Pavel Anzenbacher 1*, Pavel Soucek 2

1 Palacky University, Olomouc, CZ 2 Natl Inst Publ Health, Prague, CZ

* Address correspondence to: E-mail: anzen{at}tunw.upol.cz

Abstract

Cytochrome P450 2E1 was isolated from minipig liver microsomes. The protein has been cloned and the respective cDNA sequenced (GenBank Accession No AY581116). Minipig CYP2E1 is two residues shorter than its human orthologue. 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 as well with 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 man.


Key words: CYP2E, cytochrome P450, cytochrome P450 function, cytochrome P450 isoforms, cytochrome P450 structure, human CYP enzymes, liver microsomes


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