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Journal of Biochemistry 2006 139(5):865-872; doi:10.1093/jb/mvj093
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© 2006 The Japanese Biochemical Society.

Regular Paper

Cynomolgus Monkey Cytochrome P450 2C43: cDNA Cloning, Heterologous Expression, Purification and Characterization

Maori Mitsuda1, Masahiko Iwasaki1,* and Satoru Asahi2

1 Department of Biology, Graduate School of Science, Osaka University, 2-17-85, Jusohonmachi, Yodogawa-ku, Osaka 532-8686; and 2 Development Research Center, Pharmaceutical Research Division, Takeda Pharmaceutical Company Ltd., 2-17-85, Jusohonmachi, Yodogawa-ku, Osaka 532-8686

* To whom correspondence should be addressed. Tel: +81-6-6300-6076, Fax: +81-6-6300-6306, E-mail: Iwasaki_Masahiko{at}takeda.co.jp

The cDNA of cytochrome P450 (CYP) 2C43 was cloned from cynomolgus monkey liver by RT-PCR. The deduced amino acid sequence showed 93% and 91% identity to human CYP2C9 and CYP2C19, respectively. The cDNA was expressed in Escherichia coli and purified by a series of chromatography steps, yielding a specific content of 11.5 nmol P450/mg protein. The substrate specificity of the purified CYP2C43 was examined in a reconstitution system comprising NADPH-P450 reductase, lipid, cytochrome b5 and CYP2C marker substrates. The purified CYP2C43 showed high activity for testosterone 17-oxidation and progesterone 21-hydroxylation, which were also observed for CYP2C19 but not CYP2C9. In addition, CYP2C43 showed activity for (S)-mephenytoin 4'-hydroxylation, a marker reaction for CYP2C19. With CYP2C9 marker substrates, CYP2C43 exhibited low activity for diclofenac 4'-hydroxylation and no activity for tolbutamide p-methylhydroxylation. Therefore, in terms of substrate specificity, our results indicate that CYP2C43 is similar to CYP2C19, rather than CYP2C9.


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