Rajkovic A, Simonsen J N, Davis R E, Rottman F M
Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
Proc Natl Acad Sci U S A. 1989 Nov;86(21):8217-21. doi: 10.1073/pnas.86.21.8217.
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.
已分离并鉴定出编码来自人类寄生虫曼氏血吸虫的3-羟基-3-甲基戊二酰辅酶A（HMG-CoA）还原酶[（S）-甲羟戊酸：NADP+氧化还原酶（辅酶A酰化），EC 1.1.1.34]的cDNA克隆。该cDNA序列全长3459个碱基对，包含一个2844个碱基对的开放阅读框，对应于一个948个氨基酸的蛋白质。预测的曼氏血吸虫HMG-CoA还原酶蛋白含有一个疏水的氨基末端，由七个潜在的跨膜结构域组成，这些结构域在结构上保守，但氨基酸序列与其他物种的HMG-CoA还原酶不同。然而，曼氏血吸虫HMG-CoA还原酶蛋白的亲水羧基末端在包含催化结构域的区域与其他HMG-CoA还原酶的羧基末端具有48-52%的序列同一性。当在大肠杆菌中作为融合蛋白表达时，血吸虫蛋白的羧基末端结构域表现出HMG-CoA还原酶活性。
