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Title 

Versatile O-GlcNAc transferase assay for high-throughput identification of enzyme variants, substrates, and inhibitors

Authors 

E J KimL K AbramowitzM R BondD C LoveD W KangH F LeuckeJong Seog AhnJ A Hanover

Publisher 

American Chemical Society

Issue Date 

2014

Citation 

Bioconjugate Chemistry, vol. 25, no. 6, pp. 1025-1030

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.

ISSN 

1043-1802

Link 

http://dx.doi.org/10.1021/bc5001774

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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