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Molecular mechanism for eliminylation, a newly discovered post-translational modification.


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 ?-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.

SUBMITTER: Ke Z 

PROVIDER: S-EPMC3140633 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Molecular mechanism for eliminylation, a newly discovered post-translational modification.

Ke Zhihong Z   Smith Gregory K GK   Zhang Yingkai Y   Guo Hua H  

Journal of the American Chemical Society 20110630 29


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. ...[more]

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