Ontology highlight
ABSTRACT:
SUBMITTER: Ke Z
PROVIDER: S-EPMC3140633 | biostudies-literature | 2011 Jul
REPOSITORIES: biostudies-literature
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]