title: Enzymatic characterization of recombinant enzymes of O-GlcNAc cycling.
abstract: The dynamic addition of O-GlcNAc to target proteins is now recognized as a major signaling paradigm impacting phosphorylation, protein turnover, gene expression, and other posttranslational modifications influencing epigenetics. Here we describe the production of and methods for assay of the recombinant enzymes of O-GlcNAc cycling: O-linked GlcNAc Transferase (OGT) and O-GlcNAcase (OGA).
authors.affiliation: Laboratory Cell Biochemistry and Biology, NIDDK, National Institutes of Health, Bethesda, MD, USA.
authors.forename: Eun Ju
authors.initials: EJ
authors.lastname: Kim
authors.forename: John A
authors.initials: JA
authors.lastname: Hanover
mesh_terms: D000818:Animals; D003001:Cloning, Molecular / Q000379:methods; D057075:Enzyme Assays / Q000379:methods*; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D017351:N-Acetylglucosaminyltransferases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase