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Molecular Mechanism for Eliminylation, a Newly Discovered Post-Translational Modification
- Source :
- Journal of the American Chemical Society. 133:11103-11105
- Publication Year :
- 2011
- Publisher :
- American Chemical Society (ACS), 2011.
-
Abstract
- The newly discovered bacterial phosphothreonine lyases perform a post-translational modification of host cell signaling proteins employing 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 the E1cB-like pathway, in which the carbanion intermediate is stabilized by an enzyme oxyanion hole provided by Lys104 and Tyr158 of SpvC.
- Subjects :
- Models, Molecular
chemistry.chemical_classification
Stereochemistry
Carbon-Oxygen Lyases
Ab initio
Salmonella enterica
General Chemistry
Biochemistry
Article
Catalysis
Colloid and Surface Chemistry
Enzyme
chemistry
Catalytic Domain
Mutation
Phosphorylation
Phosphothreonine
Oxyanion hole
Threonine
Protein Processing, Post-Translational
Carbanion
Subjects
Details
- ISSN :
- 15205126 and 00027863
- Volume :
- 133
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....0b08ae2c8dd5c64e280f8df5e0456a30