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

被引：24

作者：

Ke, Zhihong ^{[1
]}

Smith, Gregory K. ^{[1
]}

Zhang, Yingkai ^{[2
]}

Guo, Hua ^{[1
]}

机构：

[1] Univ New Mexico, Dept Chem & Chem Biol, Albuquerque, NM 87131 USA

[2] NYU, Dept Chem, New York, NY 10003 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2011年 / 133卷 / 29期

关键词：

CATALYZED PROTON ABSTRACTION; CARBON ACIDS; ALPHA-PROTONS; ENZYME; SUPERFAMILY;

D O I：

10.1021/ja204378q

中图分类号：

O6 [化学];

学科分类号：

0703 ;

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 beta-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.

引用

页码：11103 / 11105

页数：3

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