Post-secretional modification of exo-1,3-beta-D-glucanases from Saccharomyces cerevisiae.
Exo-1,3-beta-D-glucanase secreted by Saccharomyces cerevisiae undergoes extracellular modifications in its carbohydrate moiety that change the affinity towards the lectin concanavalin A. The transition of negatively reacting enzyme form into positively reacting one depends on temperature. Results from experiments with glucono-delta-lactone and from treatments in vitro with hydrolases suggest a glycosidase-mediated mechanism.
D003208:Concanavalin A / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D043326:Glucan 1,3-beta-Glucosidase; D005947:Glucose / Q000378:metabolism; D005959:Glucosidases / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism; D011523:Protoplasts / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013696:Temperature; D000520:alpha-Glucosidases / Q000378:metabolism; D001617:beta-Glucosidase / Q000378:metabolism*
D003208:Concanavalin A; D005959:Glucosidases; D000520:alpha-Glucosidases; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase; D005947:Glucose; D008358:Mannose