Structural modeling of glucanase-substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-beta-D-glucanases.

Glycosyl hydrolase family 16 (GHF16) truncated Fibrobacter succinogenes (TFs) and GHF17 barley 1,3-1,4-beta-D-glucanases (beta-glucanases) possess different structural folds, beta-jellyroll and (beta/alpha)8, although they both catalyze the specific hydrolysis of beta-1,4 glycosidic bonds adjacent to beta-1,3 linkages in mixed beta-1,3 and beta-1,4 beta-D-glucans or lichenan. Differences in the active site region residues of TFs beta-glucanase and barley beta-glucanase create binding site topographies that require different substrate conformations. In contrast to barley beta-glucanase, TFs beta-glucanase possesses a unique and compact active site. The structural analysis results suggest that the tyrosine residue, which is conserved in all known 1,3-1,4-beta-D-glucanases, is involved in the recognition of mixed beta-1,3 and beta-1,4 linked polysaccharide.