title: Complete amino acid sequence of 21-hydroxylase cytochrome P-450 from porcine adrenal microsomes.
abstract: Adrenal microsomal 21-hydroxylase is essential for biosynthesis or metabolism of various steroid hormones. The complete amino acid sequence of this cytochrome P-450 from pig adrenal was determined by sequence analysis on several sets of proteolytic fragments. The mature protein consists of 492 amino acid residues, corresponding to a molecular weight of 55,484. Seven out of nine total cysteine residues are localized in the amino terminal half of the molecule. The carboxyl terminal half contains only two cysteines, one of which is located at the highly conserved heme-binding region proposed in all cytochromes P-450. A structural comparison between 21-hydroxylase and 17 alpha-hydroxylase reveals that there is a preponderance of sequence homology at the carboxyl terminal region. These studies indicate that a single gene product is expressed for steroid 21-hydroxylase in porcine adrenal glands.
mesh_terms: D000311:Adrenal Glands / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D008861:Microsomes / Q000201:enzymology; D013254:Steroid 17-alpha-Hydroxylase; D013255:Steroid 21-Hydroxylase / Q000235:genetics / Q000378:metabolism; D013250:Steroid Hydroxylases / Q000235:genetics / Q000378:metabolism; D013552:Swine
chemical_list: D013250:Steroid Hydroxylases; D013255:Steroid 21-Hydroxylase; D013254:Steroid 17-alpha-Hydroxylase