Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases.

Abstract

The "high-mannose" glycosylated forms of aminopeptidase N (EC 3.4.11.2), maltase-glucoamylase (EC 3.2.1.20), and sucrase-isomaltase (EC 3.2.1.48, EC 3.2.1.10) have been purified. The high-mannose glycosylated form of sucrase-isomaltase was found to have a lower specific activity than the complex glycosylated form, whereas no difference was observed for the two other enzymes. The change in glycosylation from high-mannose to complex form thus seems to be of importance for the enzymatic activity of sucrase-isomaltase either by direct structural involvement or by a general stabilization effect on the protein conformation.