SkfB Abstracts a Hydrogen Atom from Cα on SkfA To Initiate Thioether Cross-Link Formation.
SkfB Abstracts a Hydrogen Atom from Cα on SkfA To Initiate Thioether Cross-Link Formation.
复制标题
SKFB在SKFA上从Cα上提取氢原子，以启动硫醚交联的形成。
DOI：
10.1021/acs.biochem.6b00598
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发表时间：
2016-08-02
期刊：
影响因子：
2.9
通讯作者：
Bandarian V
中科院分区：
文献类型：
--
作者：
Bruender NA;Bandarian V
含硫- α碳硫醚肽（sactipeptide）是具有杀菌活性的核糖体合成的翻译后修饰肽（RiPPs）。硫醚交联是生物活性所必需的，是由自由基s -腺苷-l-蛋氨酸（SAM）超家族成员在肽底物中安装的。本研究表明，自由基SAM酶SkfB利用SAM的还原裂解产生的5 ' -脱氧腺苷基自由基从底物SkfA中12位氨基酸的α-碳上提取一个氢原子，以启动硫醚交联的安装。这项工作的见解适用于所有自由基SAM肽成熟酶。
Sulfur to alpha carbon thioether-containing peptides (sactipeptides) are ribosomally synthesized post-translationally modified peptides (RiPPs) with bacteriocidal activities. The thioether crosslink, which is required for biological activity, is installed by a member of the radical S-adenosyl-l-methionine (SAM) superfamily in the peptide substrate. Herein we show that the radical SAM enzyme, SkfB, utilizes the 5′-deoxyadenosyl radical generated from the reductive cleavage of SAM to abstract a hydrogen atom from the α-carbon of the amino acid at position 12 in the substrate, SkfA, to initiate the installation of a thioether crosslink. The insights from this work are applicable to all radical SAM sactipeptide maturases.