还原性乙酰辅酶A途径：来自嗜热栖热梭菌的活性甲基四氢叶酸：类咕啉/铁硫蛋白甲基转移酶的序列与异源表达
The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum.
作者信息
Roberts D L, Zhao S, Doukov T, Ragsdale S W
机构信息
Department of Biochemistry, University of Nebraska, Lincoln 68583-0718.
出版信息
J Bacteriol. 1994 Oct;176(19):6127-30. doi: 10.1128/jb.176.19.6127-6130.1994.
Abstract
The methyltransferase (MeTr) from Clostridium thermoaceticum transfers the N5-methyl group of (6S)-methyltetrahydrofolate to the cobalt center of a corrinoid/iron-sulfur protein in the acetyl coenzyme A pathway. MeTr was purified to homogeneity and shown to lack metals. The acsE gene encoding MeTr was sequenced and actively expressed in Escherichia coli at a level of 9% of cell protein. Regions in the sequence of MeTr and the E. coli cobalamin-dependent methionine synthase were found to share significant homology, suggesting that they may represent tetrahydrofolate-binding domains.
摘要
来自热醋梭菌的甲基转移酶（MeTr）将（6S）-甲基四氢叶酸的N5-甲基基团转移至乙酰辅酶A途径中类咕啉/铁硫蛋白的钴中心。MeTr被纯化至同质且显示不含金属。对编码MeTr的acsE基因进行了测序，并在大肠杆菌中以细胞蛋白9%的水平进行了活性表达。发现MeTr序列与大肠杆菌钴胺素依赖性甲硫氨酸合酶序列中的区域具有显著同源性，这表明它们可能代表四氢叶酸结合结构域。
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