A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates.
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.
Leavy
Tanya M
TM
Department of Chemistry, Howard Hughes Medical Institute, University of California, Berkeley 94720, USA.
Bertozzi
Carolyn R
CR
D002942:Circular Dichroism; D016384:Consensus Sequence; D004797:Enzyme-Linked Immunosorbent Assay; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D010455:Peptides; D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase