Molecular cloning and sequence analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from the human parasite Schistosoma mansoni.
Molecular cloning and sequence analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from the human parasite Schistosoma mansoni.
复制标题
人类寄生虫曼氏血吸虫的 3-羟基-3-甲基戊二酰辅酶 A 还原酶的分子克隆和序列分析。
DOI：
10.1073/pnas.86.21.8217
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发表时间：
1989
影响因子：
11.1
通讯作者：
Rottman,FM
中科院分区：
文献类型：
--
作者：
Rajkovic,A;Simonsen,JN;Davis,RE;Rottman,FM
从曼氏血吸虫体内分离到编码3-羟基-3-甲基戊二酰辅酶A(HMG-CoA)还原酶[(S)-甲戊酸：NaDP+氧化还原酶(CoA-酰化)，EC 1.1.1.34]的基因。合成的3459个碱基对的cDNA序列包含一个2844个碱基对的开放阅读框，对应一个948个氨基酸的蛋白质。预测的曼氏链霉菌HMG-CoA还原酶蛋白含有一个疏水的氨基末端，由7个潜在的跨膜结构域组成，它们在结构上是保守的，但氨基酸序列与其他物种的HMG-CoA还原酶不同。然而，曼氏链霉菌HMG-CoA还原酶蛋白的亲水性羧基末端与其他HMG-CoA还原酶的羧基末端在包含催化结构域的区域有48-52%的序列同源性。在大肠杆菌中以融合蛋白的形式表达时，血吸虫蛋白的羧基末端结构域具有HMG-CoA还原酶活性。
cDNA clones encoding the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase [(S)-mevalonate:NADP+ oxidoreductase (CoA-acylating), EC 1.1.1.34] from the human parasite Schistosoma mansoni have been isolated and characterized. The composite 3459 base pairs of cDNA sequence contains a 2844-base-pair open reading frame corresponding to a protein of 948 amino acids. The predicted S. mansoni HMG-CoA reductase protein contains a hydrophobic amino terminus consisting of seven potential transmembrane domains that are structurally conservative but are not identical in amino acid sequence with HMG-CoA reductases from other species. The hydrophilic carboxyl terminus of the S. mansoni HMG-CoA reductase protein, however, shares 48-52% sequence identity with the carboxyl termini of other HMG-CoA reductases in a region that contains the catalytic domain. When expressed as a fusion protein in Escherichia coli, the carboxyl-terminal domain of the schistosome protein exhibits HMG-CoA reductase enzyme activity.