Haniu M, Yanagibashi K, Hall P F, Shively J E
Arch Biochem Biophys. 1987 Apr;254(1):380-4. doi: 10.1016/0003-9861(87)90115-9.
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.
肾上腺微粒体21-羟化酶对于各种甾体激素的生物合成或代谢至关重要。通过对几组蛋白水解片段进行序列分析,确定了来自猪肾上腺的这种细胞色素P-450的完整氨基酸序列。成熟蛋白由492个氨基酸残基组成,分子量为55,484。九个半胱氨酸残基中的七个位于分子的氨基末端一半。羧基末端一半仅含有两个半胱氨酸,其中一个位于所有细胞色素P-450中提出的高度保守的血红素结合区域。21-羟化酶和17α-羟化酶之间的结构比较表明,在羧基末端区域存在序列同源性优势。这些研究表明,猪肾上腺中甾体21-羟化酶表达的是单一基因产物。