Biochemical Approaches for Understanding Iron-Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis.
Biochemical Approaches for Understanding Iron-Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis.
复制标题
催化过程中大肠杆菌脂酰合酶中的铁硫簇再生的生化方法。
DOI：
10.1016/bs.mie.2018.06.006
复制
发表时间：
2018
影响因子：
--
通讯作者：
Booker SJ
中科院分区：
文献类型：
--
作者：
McCarthy EL;Booker SJ
硫辛酰合成酶（Lipoyl synthase，利帕）是一种S-腺苷甲硫氨酸（S-adenosylmethionine，SAM）自由基酶，催化硫辛酰辅因子的第二步生物合成：在辛酰侧链的C6和C8插入硫。除了作为自由基SAM（RS）酶特征的[4Fe-4S]簇外，利帕还含有第二个[4Fe-4S]簇，尽管存在争议，但已提出在周转期间降解以提供插入的硫原子。这种作用的结果是铁硫簇的破坏使酶处于非活性状态。最近，研究表明，大肠杆菌蛋白NfuA或IscU可以赋予大肠杆菌的催化特性。coli利帕的表达。本文介绍了利帕的体外表征和活性分析方法，并对大肠杆菌介导的利帕辅助簇的再生途径进行了研究。大肠杆菌铁硫载体蛋白NfuA。
Lipoyl synthase (LipA in bacteria) is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the second step of the de novo biosynthesis of the lipoyl cofactor: the insertion of sulfur at C6 and C8 of a pendant octanoyl chain. In addition to the [4Fe–4S] cluster that is characteristic of the radical SAM (RS) enzymes, LipA contains a second [4Fe–4S] cluster that, though controversial, has been the proposed to be degraded during turnover to supply the inserted sulfur atoms. A consequence of this proposed role is that the destruction of its iron-sulfur cluster renders the enzyme in an inactive state. Recently, it was shown that Escherichia coli proteins NfuA or IscU can confer catalytic properties to E. coli LipA in vitro. In this article, we present methods for characterizing LipA and analyzing its activity in vitro, and provide strategies to monitor the pathway for the regeneration of LipA’s auxiliary cluster by E. coli iron-sulfur carrier protein NfuA.
登录
查看更多内容
影响因子：
--
作者：
Blaszczyk AJ;Wang RX;Booker SJ
通讯作者：
Booker SJ
影响因子：
3.6
作者：
Py, Beatrice;Gerez, Catherine;Barras, Frederic
通讯作者：
Barras, Frederic
影响因子：
15
作者：
Cicchillo, RM;Booker, SJ
通讯作者：
Booker, SJ
影响因子：
4.1
作者：
Harmer, Jenny E.;Hiscox, Martyn J.;Roach, Peter L.
通讯作者：
Roach, Peter L.
影响因子：
2.9
作者：
Cicchillo, RM;Iwig, DF;Booker, SJ
通讯作者：
Booker, SJ