Noshiro M, Okuda K
Department of Biochemistry, School of Dentistry, Hiroshima University, Japan.
FEBS Lett. 1990 Jul 30;268(1):137-40. doi: 10.1016/0014-5793(90)80992-r.
A complete cDNA clone encoding human cholesterol 7 alpha-hydroxylase has been isolated using a rat P-450ch7 alpha cDNA insert [(1989) FEBS Lett. 257, 97-100] as a probe and totally sequenced. The cDNA contained 1512-base pair open reading frame encoding 504 amino acid residues (Mr 57,630), 39-base pair 5'-untranslated region 1322-base pair 3'-ultranslated region including 20 nucleotides of poly A tail in the total length of 2873 base pairs. The deduced amino acid sequence showed 82% similarity to rat P-450ch7 alpha. Unique amino acid residues were observed in putative binding domains for heme and steroid which are highly conserved in most steroidogenic P-450s.
利用大鼠P-450ch7α cDNA插入片段[(1989年)《欧洲生物化学学会联合会快报》257, 97 - 100]作为探针,分离出了编码人胆固醇7α-羟化酶的完整cDNA克隆,并进行了全序列测定。该cDNA包含1512个碱基对的开放阅读框,编码504个氨基酸残基(分子量57,630),5'非翻译区为39个碱基对,3'非翻译区为1322个碱基对,包括20个聚腺苷酸尾核苷酸,全长2873个碱基对。推导的氨基酸序列与大鼠P-450ch7α的相似性为82%。在大多数类固醇生成性P-450中高度保守的血红素和类固醇推定结合结构域中观察到了独特的氨基酸残基。