| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1373457 | Bioorganic & Medicinal Chemistry Letters | 2007 | 4 Pages |
Abstract
O-GlcNAc transferase (OGT) catalyzes the addition of N-acetylglucosamine (O-GlcNAc) onto a diverse array of intracellular proteins. Although hundreds of proteins are known to be modified by O-GlcNAc, a strict amino acid consensus sequence for OGT has not been identified. In this study, we describe the development of a high-throughput assay for OGT and use it to profile the specificity of the enzyme among a panel of peptide substrates.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Tanya M. Leavy, Carolyn R. Bertozzi,