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Discovery of O-GlcNAc transferase inhibitors.

Journal of the American Chemical Society (2005-10-20)
Benjamin J Gross, Brian C Kraybill, Suzanne Walker
ABSTRACT

O-GlcNAcylation of serine and threonine residues is a dynamic and essential post-translational modification involved in signaling pathways in eukaryotes. Studies of O-GlcNAcylation would be aided by small-molecule inhibitors of O-GlcNAc transferase (OGT), the sole enzyme know to mediate this modification, but discovery of such molecules has been hampered by poor expression of cloned OGT and lack of suitable high-throughput screens. This Communication describes the development an expression system to access large amounts of the catalytic domain of OGT and the implementation of a fluorescence-based substrate analogue displacement assay that has led to the discovery of a set of OGT inhibitors. This work lays the foundation for both structural and functional analysis of the catalytic domain of OGT.

MATERIALS
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Product Description

Sigma-Aldrich
ST045849, ≥98% (HPLC)