消除酰化作用的分子机制，一种新发现的翻译后修饰。
Molecular mechanism for eliminylation, a newly discovered post-translational modification.
机构信息
Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131, USA.
出版信息
J Am Chem Soc. 2011 Jul 27;133(29):11103-5. doi: 10.1021/ja204378q. Epub 2011 Jun 30.
Abstract
The newly discovered bacterial phosphothreonine lyases perform a post-translational modification of host cell signaling proteins through a novel catalytic mechanism that irreversibly removes the phosphate group from a phosphorylated threonine via β-elimination. This "eliminylation" reaction is shown by ab initio QM/MM studies to proceed via an E1cB-like pathway, in which the carbanion intermediate is stabilized by an enzyme oxyanion hole provided by Lys104 and Tyr158 of SpvC.
摘要
新发现的细菌磷酸苏氨酸裂解酶通过一种新颖的催化机制对宿主细胞信号蛋白进行翻译后修饰，该机制通过β-消除不可逆地从磷酸苏氨酸上去除磷酸基团。从头计算 QM/MM 研究表明，这种“消除反应”通过 E1cB 样途径进行，其中碳阴离子中间体由 SpvC 的 Lys104 和 Tyr158 提供的酶氧阴离子穴稳定。
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