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Updated: Dec 21, 2025

Spectrophotometric Methods for the Study of Eukaryotic Glycogen Metabolism
Published on: August 19, 2021
O-GlcNAc Transferase: Structural Characteristics, Catalytic Mechanism and Small-Molecule Inhibitors
1Department of Science Education-Chemistry Major, Daegu University, Gyeongsan-si, GyeongBuk, 712-714, South Korea.
Abstract:
Modifications of nuclear and cytoplasmic proteins with a single sugar, N-acetylglucosamine (GlcNAc), play roles in a wide variety of fundamental cellular processes, and aberrant O-GlcNAc profiles are associated with pathological progression of several chronic diseases. O-GlcNAc transferase (OGT) is the only enzyme to catalyze the attachment of GlcNAc to intracellular protein substrates. Considering its biological significance, selective and potent OGT inhibitors are invaluable tools for enhancing our understanding of the precise biological functions of the enzyme, for revealing its unknown functions, and for validating OGT as a therapeutic target. In this minireview, human OGT (hOGT) inhibitors and their catalytic mechanisms will be explored. In addition, a brief overview of recent findings on the 3D structural characteristics of hOGT that have contributed greatly to the development of novel inhibitors of hOGT is provided.
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