Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli:: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli:: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
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DOI：
10.1021/ja042428u
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发表时间：
2005-03-09
影响因子：
15
通讯作者：
Booker, SJ
中科院分区：
文献类型：
--
作者：
Cicchillo, RM;Booker, SJ
硫辛酰合成酶催化硫辛酰辅因子从头生物合成的最后一步，即将两个硫原子插入辛酰链中，辛酰链以酰胺键与硫辛酰接受蛋白上的保守赖氨酸结合。我们在本文中表明，硫辛酰辅因子中的硫原子来自硫辛酰合酶本身，并且每个硫辛酰合酶多肽将两个硫原子贡献给完整的辅因子。
Lipoyl synthase catalyzes the final step in the de novo biosynthesis of the lipoyl cofactor, which is the insertion of two sulfur atoms into an octanoyl chain that is bound in an amide linkage to a conserved lysine on a lipoyl-accepting protein. We show herein that the sulfur atoms in the lipoyl cofactor are derived from lipoyl synthase itself, and that each lipoyl synthase polypeptide contributes both of the sulfur atoms to the intact cofactor.