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J. Biol. Chem., Vol. 266, Issue 12, 7774-7778, 04, 1991
Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis
JJ Cali and DW Russell
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
The enzyme sterol 27-hydroxylase catalyzes the first step in the oxidation
of the side chain of sterol intermediates in the bile acid synthesis
pathway. Human sterol 27-hydroxylase cDNAs were isolated from a liver cDNA
library by cross-hybridization with a previously cloned rabbit cDNA probe.
DNA sequence analysis of hybridization-positive clones predicted a human
sterol 27-hydroxylase consisting of a 33-amino- acid mitochondrial signal
sequence followed by a mature protein of 498 amino acids. RNA blotting
experiments demonstrated sterol 27- hydroxylase mRNAs of approximately 1.8
to 2.2 kilobases in liver and fibroblast cells. The steady state levels of
the mRNA did not change when cultured cells were grown in the presence or
absence of sterols. Introduction of the sterol 27-hydroxylase cDNA into
Simian COS cells resulted in the expression of active enzyme capable of
catalyzing multiple oxidation reactions (R-CH3----R-CH2OH----R-COOH) at
carbon 27 of sterol intermediates of the bile acid synthesis pathway.

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Copyright © 1991 by the American Society for Biochemistry and Molecular Biology.
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