Dissemin is shutting down on January 1st, 2025

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Portland Press, Biochemical Journal, 3(457), p. 497-502, 2014

DOI: 10.1042/bj20131272

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Bisubstrate UDP–peptide conjugates as human O-GlcNAc transferase inhibitors

Journal article published in 2014 by Vladimir S. Borodkin, Daan M. F. vanAalten, Daan Mf F. van Aalten, Marianne Schimpl ORCID, Mehmet Gundogdu, Karim Rafie, Helge Christian Dorfmueller ORCID, Daan M. F. van Aalten, David A. Robinson
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation. We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring. Goblin1 co-crystallizes with OGT, revealing an ordered C3 linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.