“…In the GH32 enzymes, these three residues (including the nucleophilic Asp, the acid-base Glu, and an Asp residue acting as a transition state stabilizer) are located within three conserved sequences, referred to as the WMNDPNG (or -fructosidase), EC, and RDP motifs, respectively (19). Surrounding the catalytic site, a set of hydrophobic residues, sometimes termed as the hydrophobic pocket, is also important for the stable binding of the substrate, through van der Waals contacts and CHstacking between the aromatic side chains and the sugar rings (2,19,22). GH32 enzymes typically contain an additional Cterminal -sandwich domain, which is important for maintaining structural stability and may be involved in protein oligomerization in some cases (1,4).…”