3.2.1.186	dimer	1 * 54000 + 1 * 58000, SDS-PAGE	722251	
3.2.1.186	monomer	1 * 66573, sequence calculation, 1 * 80700, native enzyme, SDS-PAGE, 1 * 140000, glycosylated recombinant His-tagged enzyme, SDS-PAGE, 1 * 70000, deglycosylated recombinant His-tagged enzyme, SDS-PAGE	755023	
3.2.1.186	monomer	1 * 80700, SDS-PAGE	723361	
3.2.1.186	additional information	the enzyme has a quaternary protein structure of a three-dimensionally radiated assembly of long fibrillae. It is assembled by linear stacking of hollow trimeric units and the resulting fibril has a long central tunnel connecting to the outer medium via regularly distributed side fenestrations. The enzyme active sites are located within the central tunnel. This unique multimer assembly increases enzyme affinity to avenacosides, in vivo substrates, and may function to discriminate avenacosides from many other kinds of beta-glucoside in oat. The fibrillar multimer of oat beta-glucosidase is a novel quaternary protein structure for enzyme supramolecular assembly that may have a functional role in the regulation of enzyme affinity	666175	
3.2.1.186	multimer	x * 60000, the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof	723436