Commentary on: "Structural insights into a bacterial β-glucosidase capable of degrading sesaminol triglucoside to produce sesaminol: toward the understanding of the aglycone recognition mechanism by the C-terminal lid domain".

Abstract

Sesaminol is an organic compound which shows the strong antioxidant, anti-inflammatory, and neuroprotective properties. Sesaminol triglucoside (STG) is glycosylated form of sesaminol and abundantly exists in sesame seeds. However, typical β-glucosidases could not deglycosylate STG probably due to its bulky aglycone. PSTG1 and 2 are β-glucosidases lately isolated from Paenibacillis sp. KB0459 and have the capacity to deglycosylate STG. A recent report by Yanai et al. (J. Biochem. 2023; 174:335-344) revealed that the unique domain architecture of PSTG1. Apart from other β-glucosdasies in GH3 family, PSTG1 has novel accessary domain (domain 4) at the C-terminus. Domain 4 contributes the dimer formation and is located close to the active site. Interestingly, several hydrophobic residues are exposed, suggesting that this domain may recognize the hydrophobic aglycone of STG. The physiological functions of the non-catalytic domains in glyco-enzymes are sometimes overlooked. This paper shed light on the aglycone recognition by novel accessary domain.