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

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

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)11103-11105
Number of pages3
JournalJournal of the American Chemical Society
Volume133
Issue number29
DOIs
StatePublished - Jul 27 2011

Fingerprint

Phosphothreonine
Cell signaling
Lyases
Threonine
Post Translational Protein Processing
Phosphates
Enzymes
Proteins

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Molecular mechanism for eliminylation, a newly discovered post-translational modification. / Ke, Zhihong; Smith, Gregory K.; Zhang, Yingkai; Guo, Hua.

In: Journal of the American Chemical Society, Vol. 133, No. 29, 27.07.2011, p. 11103-11105.

Research output: Contribution to journalArticle

@article{89a904e2e0754678b6aabdfba19fd27a,
title = "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 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.",
author = "Zhihong Ke and Smith, {Gregory K.} and Yingkai Zhang and Hua Guo",
year = "2011",
month = "7",
day = "27",
doi = "10.1021/ja204378q",
language = "English (US)",
volume = "133",
pages = "11103--11105",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "29",

}

TY - JOUR

T1 - Molecular mechanism for eliminylation, a newly discovered post-translational modification

AU - Ke, Zhihong

AU - Smith, Gregory K.

AU - Zhang, Yingkai

AU - Guo, Hua

PY - 2011/7/27

Y1 - 2011/7/27

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=79960593151&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79960593151&partnerID=8YFLogxK

U2 - 10.1021/ja204378q

DO - 10.1021/ja204378q

M3 - Article

C2 - 21710993

AN - SCOPUS:79960593151

VL - 133

SP - 11103

EP - 11105

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 29

ER -