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Molecular Mechanism for Eliminylation, a Newly Discovered Post-Translational Modification

机译:Eliminylation,新发现的翻译后修饰的分子机制

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摘要

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-eIimination. This "eliminylation" reaction is shown by ab initio QM/MM studies to proceed via an ElcB-like pathway, in which the carbanion intermediate is stabilized by an enzyme oxyanion hole provided by Lys104 and Tyrl58 of SpvC.
机译:新发现的细菌磷酸苏氨酸裂解酶通过一种新型催化机制对宿主细胞信号蛋白进行翻译后修饰,该催化机制通过β-消除作用不可逆地从磷酸化苏氨酸中除去磷酸基团。从头开始的QM / MM研究表明,这种“消除”反应是通过ElcB样途径进行的,其中碳负离子中间物由SpvC的Lys104和Tyrl58提供的酶氧阴离子孔稳定。

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  • 来源
    《Journal of the American Chemical Society》 |2011年第29期|p.11103-11105|共3页
  • 作者单位

    Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131, United States;

    Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131, United States;

    Department of Chemistry, New York University, New York, New York 10003, United States;

    Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131, United States;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
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