Ontology highlight
ABSTRACT:
SUBMITTER: de Oliveira JF
PROVIDER: S-EPMC6626659 | biostudies-literature | 2019 Jan
REPOSITORIES: biostudies-literature
de Oliveira Juliana Ferreira JF do Prado Paula Favoretti Vital PFV da Costa Silvia Souza SS Sforça Mauricio Luis ML Canateli Camila C Ranzani Americo Tavares AT Maschietto Mariana M de Oliveira Paulo Sergio Lopes PSL Otto Paulo A PA Klevit Rachel E RE Krepischi Ana Cristina Victorino ACV Rosenberg Carla C Franchini Kleber Gomes KG
Nature chemical biology 20181210 1
Ubiquitin-conjugating enzymes (E2) enable protein ubiquitination by conjugating ubiquitin to their catalytic cysteine for subsequent transfer to a target lysine side chain. Deprotonation of the incoming lysine enables its nucleophilicity, but determinants of lysine activation remain poorly understood. We report a novel pathogenic mutation in the E2 UBE2A, identified in two brothers with mild intellectual disability. The pathogenic Q93E mutation yields UBE2A with impaired aminolysis activity but ...[more]