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J. Biol. Chem., Vol. 276, Issue 13, 9606-9612, March 30, 2001

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Cloning and Expression of a Pig Liver Taurochenodeoxycholic Acid 6-Hydroxylase (CYP4A21)
A NOVEL MEMBER OF THE CYP4A SUBFAMILY^*

Kerstin Lundell, Ronnie Hansson, and Kjell Wikvall

From the Division of Biochemistry, Department of Pharmaceutical Biosciences, University of Uppsala, Box 578, Uppsala S-751 23, Sweden

A cytochrome P450 expressed in pig liver was cloned by polymerase chain reaction using oligonucleotide primers based on amino acid sequences of the purified taurochenodeoxycholic acid 6-hydroxylase. This enzyme catalyzes a 6-hydroxylation of chenodeoxycholic acid, and the product hyocholic acid is considered to be a primary bile acid specific for the pig. The cDNA encodes a protein of 504 amino acids. The primary structure of the porcine taurochenodeoxycholic acid 6-hydroxylase, designated CYP4A21, shows about 75% identity with known members of the CYP4A subfamily in rabbit and man. Transfection of the cDNA for CYP4A21 into COS cells resulted in the synthesis of an enzyme that was recognized by antibodies raised against the purified pig liver enzyme and catalyzed 6-hydroxylation of taurochenodeoxycholic acid. The hitherto known CYP4A enzymes catalyze hydroxylation of fatty acids and prostaglandins and have frequently been referred to as fatty acid hydroxylases. A change in substrate specificity from fatty acids or prostaglandins to a steroid nucleus among CYP4A enzymes is notable. The results of mutagenesis experiments indicate that three amino acid substitutions in a region around position 315 which is highly conserved in all previously known CYP4A and CYP4B enzymes could be involved in the altered catalytic activity of CYP4A21.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AJ278474 SSC278474.

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