Isolation and amino acid sequence analysis of bovine adrenal 3 beta-hydroxysteroid dehydrogenase/steroid isomerase.
Isolation and amino acid sequence analysis of bovine adrenal 3 beta-hydroxysteroid dehydrogenase/steroid isomerase.
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牛肾上腺3β-羟基类固醇脱氢酶/类固醇异构酶的分离和氨基酸序列分析。
DOI：
10.1021/bi00247a003
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发表时间：
1991
期刊：
影响因子：
2.9
通讯作者：
Shively,JE
中科院分区：
文献类型：
--
作者：
Rutherfurd,KJ;Chen,SA;Shively,JE
1991年3月27日接收的修订版Mandarin pt摘要：3 j8-羟基类固醇脱氢酶/类固醇异构酶已从牛肾上腺中纯化至均一。分离到一个分子量为42090 ±40的蛋白质，该蛋白质同时具有两种酶的活性。牛肾上腺3/3-羟基类固醇脱氢酶/类固醇异构酶的大约86%的氨基酸序列已经通过用胰蛋白酶和赖氨酰内肽酶对从牛肾上腺素分离的肽进行测序以及用溴化氰进行化学裂解而获得。获得的序列与牛卵巢3/S-羟基类固醇脱氢酶/类固醇异构酶的推导氨基酸序列相同[Zhao et al. 04 The Dog（1989）259，153-157]，除了牛卵巢序列中发现的N-末端甲硫氨酸残基不存在于成熟的牛肾上腺素酶中。的基础上的一级structureand与其他NAD+结合蛋白的比较，我们提出了一个结构模型的牛肾上腺3/3-羟基类固醇脱氢酶/类固醇异构酶定位的NAD+结合位点以及膜锚定段。3/3-羟基类固醇脱氢酶和类固醇异构酶催化连续步骤的类固醇激素的生物合成途径，即，转换的双烯醇酮孕酮。3/3-羟基-5-烯类固醇脱氢酶和5-烯-4-烯类固醇异构酶的酶活性被认为是由哺乳动物组织中的单一蛋白质催化的（福特和恩格尔，1974;石井-大场等人，1986 a，B，1987; Lorence et
Revised Manuscript Received March 27, 1991 abstract: 3j8-Hydroxysteroid dehydrogenase/steroid isomerase has been purified to homogeneity from bovine adrenal glands. A single protein of molecular weight 42 090±40 containing both enzyme activities has been isolated. Approximately 86% of the amino acid sequence of the bovine adrenal 3/3-hydroxysteroid dehydrogenase/steroid isomerasehas been obtained by sequencing peptides isolated from digests with trypsin and lysyl endopeptidase and by chemical cleavage with CNBr. The sequence obtained is identical with that of the deduced amino acid sequence of the bovine ovarian 3/S-hydroxysteroid dehydrogenase/steroid isomerase [Zhao et al.(1989) FEBS Lett. 259, 153-157], with the exception that the N-terminal methionineresidue found in the bovine ovarian sequence is not present in the mature bovine adrenalenzyme. On the basis of the primary structureand comparisons with other NAD+ binding proteins, we propose a structural model of the bovine adrenal 3/3-hydroxysteroid dehydrogenase/steroid isomerase localizing the NAD+ binding site as well as the membrane-anchoring segment.3/3-Hydroxysteroid dehydrogenase and steroid isomerase catalyze consecutive steps in the steroid hormone biosynthesis pathway, namely, the conversion of pregnenolone to progesterone. The enzyme activities of 3/3-hydroxy-5-ene steroid dehydrogenase and 5-ene-4-ene steroid isomerase are thought to be catalyzed by a single protein in mammalian tissues (Ford & Engel, 1974; Ishii-Ohba et al., 1986a, b, 1987; Lorence et
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