羊毛硫肽生物合成酶的结构与机制。
Structure and mechanism of lanthipeptide biosynthetic enzymes.
作者信息
van der Donk Wilfred A, Nair Satish K
机构信息
Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; The Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
出版信息
Curr Opin Struct Biol. 2014 Dec;29:58-66. doi: 10.1016/j.sbi.2014.09.006. Epub 2014 Oct 14.
Abstract
Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.
摘要
羊毛硫肽是核糖体合成及翻译后修饰肽（RiPP）天然产物家族的成员。它们含有硫醚交联键，该交联键由丝氨酸（Ser）和苏氨酸（Thr）残基脱水后形成，随后半胱氨酸（Cys）残基的巯基加成到脱氢氨基酸上。最近的研究揭示了翻译后修饰的意外机制，并且结构研究已开始为修饰酶识别肽底物提供见解。
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