A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates

Bioorg Med Chem Lett. 2007 Jul 15;17(14):3851-4. doi: 10.1016/j.bmcl.2007.05.008. Epub 2007 May 10.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Circular Dichroism
  • Consensus Sequence
  • Enzyme-Linked Immunosorbent Assay
  • N-Acetylglucosaminyltransferases / metabolism*
  • Peptides / chemistry
  • Peptides / metabolism*
  • Substrate Specificity

Substances

  • Peptides
  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase