How the glycosyltransferase OGT catalyzes amide bond cleavage

Nat Chem Biol. 2016 Nov;12(11):899-901. doi: 10.1038/nchembio.2173. Epub 2016 Sep 12.

Abstract

The essential human enzyme O-linked β-N-acetylglucosamine transferase (OGT), known for modulating the functions of nuclear and cytoplasmic proteins through serine and threonine glycosylation, was unexpectedly implicated in the proteolytic maturation of the cell cycle regulator host cell factor-1 (HCF-1). Here we show that HCF-1 cleavage occurs via glycosylation of a glutamate side chain followed by on-enzyme formation of an internal pyroglutamate, which undergoes spontaneous backbone hydrolysis.

MeSH terms

  • Amides / chemistry*
  • Amides / metabolism*
  • Biocatalysis*
  • Host Cell Factor C1 / chemistry*
  • Host Cell Factor C1 / metabolism*
  • Humans
  • Hydrolysis
  • N-Acetylglucosaminyltransferases / metabolism*

Substances

  • Amides
  • HCFC1 protein, human
  • Host Cell Factor C1
  • N-Acetylglucosaminyltransferases