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.
authors.affiliation: Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131, USA.
authors.forename: Zhihong
authors.initials: Z
authors.lastname: Ke
authors.forename: Gregory K
authors.initials: GK
authors.lastname: Smith
authors.forename: Yingkai
authors.initials: Y
authors.lastname: Zhang
authors.forename: Hua
authors.initials: H
authors.lastname: Guo
mesh_terms: D019757:Carbon-Oxygen Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D008958:Models, Molecular; D009154:Mutation; D011499:Protein Processing, Post-Translational; D019779:Salmonella enterica / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism
chemical_list: D019757:Carbon-Oxygen Lyases; C527194:phosphothreonine lyase, Salmonella enterica