Two membrane preparation containing glucan synthase activity were obtained by lysis of regenerating sphaeroplasts (enzyme A) or mechanical breakage (enzyme B) of yeast (Candida albicans) cells. The reaction products of both enzymes (glucans A and B respectively) were characterized as linear beta-1,3-linked glucans on the basis of chemical and enzymic analysis. In addition, two pools of glucan could be distinguished in glucan A preparations on the basis of their susceptibility to an exoglucanase. In no case were the reaction products synthesized de novo; rather the radioactive chains were added to the non-reducing end of non-radioactive preformed glucan chains or to an acceptor of a different nature. At least some of the performed chains of glucan A, but not those of glucan B, showed a free reducing terminal. Glucan A preparations were endowed with endoglucanase activity, which, under appropriate conditions, released glucose, laminaribiose and laminaritriose. These sugars were also found in cell-wall autolysates. On the basis of the origin of both enzyme preparations it is suggested that glucan molecules are synthesized while they are bound to a non-glucan acceptor that is subsequently excised, presumably by cell-wall-associated glucanases.
Highlights from the Macromolecular X-ray Crystallography Facility at Pennsylvania State University (a) crystal structures of bacterial expansin in complex with cellohexoase and β-glucan (b) solution scattering and crystal structure of sorbitol dehydrogenase with a substrate (c) computation model of human Ron receptor with its juxta-membrane domain and (d) model of phospholipase a2 with procyanidins