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

Zhihong Ke; Gregory K. Smith; Yingkai Zhang; Hua Guo

doi:10.1021/ja204378q

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

Zhihong Ke, Gregory K. Smith, Yingkai Zhang, Hua Guo

Chemistry

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	11103-11105
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	133
Issue number	29
DOIs	https://doi.org/10.1021/ja204378q
State	Published - Jul 27 2011

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja204378q

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AU - Guo, Hua

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AB - 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.

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

Abstract

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