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Updated: Mar 15, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
How the glycosyltransferase OGT catalyzes amide bond cleavage
John Janetzko1,2, Sunia A Trauger3, Michael B Lazarus1,2
1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts, USA.
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.
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