title: The glycoprotein precursor of concanavalin A is converted to an active lectin by deglycosylation.
abstract: We have previously shown that concanavalin A is synthesized as a glycoprotein precursor that is unable to bind to sugars and is processed through six intermediate forms before assembly of the mature active lectin. Since processing involves removal of the N-glycan, four proteolytic steps and a religation, the precise event that leads to carbohydrate binding activity was not known. We have now purified the glycoprotein precursor from microsomal membranes and show that deglycosylation in vitro is sufficient alone to convert the precursor to an active carbohydrate binding protein. This is the first demonstration of a novel role for N-glycans and N-glycanases in the regulation of protein activity.
authors.affiliation: Centre for Plant Biochemistry and Biotechnology, University of Leeds, Great Britain.
authors.forename: P S
authors.initials: PS
authors.lastname: Sheldon
authors.forename: D J
authors.initials: DJ
authors.lastname: Bowles
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000378:metabolism; D006023:Glycoproteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D037121:Plant Lectins; D010946:Plants, Medicinal; D011498:Protein Precursors / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
chemical_list: D006023:Glycoproteins; D037121:Plant Lectins; D011498:Protein Precursors; C074083:pro-concanavalin A; D003208:Concanavalin A; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase