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Start Over Author "Bond, Michelle" Publisher american chemical society
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3. Versatile O-GlcNAc transferase assay for high-throughput identification of enzyme variants, substrates, and inhibitors.

Author

Kim EJ, Abramowitz LK, Bond MR, Love DC, Kang DW, Leucke HF, Kang DW, Ahn JS, and Hanover JA

Subjects
Dose-Response Relationship, Drug, Enzyme Inhibitors chemistry, Humans, Molecular Structure, Nickel chemistry, Organometallic Compounds chemistry, Structure-Activity Relationship, Substrate Specificity drug effects, beta-N-Acetylhexosaminidases antagonists & inhibitors, beta-N-Acetylhexosaminidases metabolism, Enzyme Assays, Enzyme Inhibitors pharmacology, N-Acetylglucosaminyltransferases antagonists & inhibitors, N-Acetylglucosaminyltransferases metabolism, Organometallic Compounds pharmacology
Abstract

The dynamic glycosylation of serine/threonine residues on nucleocytoplasmic proteins with a single N-acetylglucosamine (O-GlcNAcylation) is critical for many important cellular processes. Cellular O-GlcNAc levels are highly regulated by two enzymes: O-GlcNAc transferase (OGT) is responsible for GlcNAc addition and O-GlcNAcase (OGA) is responsible for removal of the sugar. The lack of a rapid and simple method for monitoring OGT activity has impeded the efficient discovery of potent OGT inhibitors. In this study we describe a novel, single-well OGT enzyme assay that utilizes 6 × His-tagged substrates, a chemoselective chemical reaction, and unpurified OGT. The high-throughput Ni-NTA Plate OGT Assay will facilitate discovery of potent OGT-specific inhibitors on versatile substrates and the characterization of new enzyme variants.

Published
2014
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