Ontology highlight
ABSTRACT:
SUBMITTER: Kapuria V
PROVIDER: S-EPMC4840301 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Kapuria Vaibhav V Röhrig Ute F UF Bhuiyan Tanja T Borodkin Vladimir S VS van Aalten Daan M F DM Zoete Vincent V Herr Winship W
Genes & development 20160407 8
In complex with the cosubstrate UDP-N-acetylglucosamine (UDP-GlcNAc),O-linked-GlcNAc transferase (OGT) catalyzes Ser/ThrO-GlcNAcylation of many cellular proteins and proteolysis of the transcriptional coregulator HCF-1. Such a dual glycosyltransferase-protease activity, which occurs in the same active site, is unprecedented and integrates both reversible and irreversible forms of protein post-translational modification within one enzyme. Although occurring within the same active site, we show he ...[more]