The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum.
The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum.
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还原乙酰辅酶 A 途径：来自热乙酸梭菌的活性甲基四氢叶酸：咕啉/铁硫蛋白甲基转移酶的序列和异源表达。
DOI：
10.1128/jb.176.19.6127-6130.1994
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发表时间：
1994
影响因子：
3.2
通讯作者：
Ragsdale,SW
中科院分区：
文献类型：
--
作者：
Roberts,DL;Zhao,S;Doukov,T;Ragsdale,SW
在乙酰辅酶a途径中，来自热醋酸梭菌的甲基转移酶（MeTr）将(6S)-甲基四氢叶酸的n5 -甲基转移到类椰碱/铁硫蛋白的钴中心。经纯化后，发现其不含金属。对编码MeTr的acsE基因进行了测序，并在大肠杆菌中以9%的细胞蛋白水平积极表达。MeTr和大肠杆菌钴胺依赖蛋氨酸合成酶的序列区域具有显著的同源性，表明它们可能代表四氢叶酸结合域。
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.