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Publication Abstract from PubMed

The sesaminol triglucoside (STG)-hydrolyzing beta-glucosidase from Paenibacillus sp. (PSTG1), which belongs to glycoside hydrolase family 3 (GH3), is a promising catalyst for the industrial production of sesaminol. We determined the X-ray crystal structure of PSTG1 with bound glycerol molecule in the putative active site. PSTG1 monomer contained typical three domains of GH3 with the active site in domain 1 (TIM barrel). In addition, PSTG1 contained an additional domain (domain 4) at the C-terminus that interacts with the active site of the other protomer as a lid in the dimer unit. Interestingly, the interface of domain 4 and the active site forms a hydrophobic cavity probably for recognizing the hydrophobic aglycone moiety of substrate. The short flexible loop region of TIM barrel was found to be approaching the interface of domain 4 and the active site. We found that n-heptyl-beta-D-thioglucopyranoside detergent acts as an inhibitor for PSTG1. Thus, we propose that the recognition of hydrophobic aglycone moiety is important for PSTG1-catalyzed reactions. Domain 4 might be a potential target for elucidating the aglycone recognition mechanism of PSTG1 as well as for engineering PSTG1 to create a further excellent enzyme to degrade STG more efficiently to produce sesaminol.

Structural insights into a bacterial beta-glucosidase capable of degrading sesaminol triglucoside to produce sesaminol: toward the understanding of the aglycone recognition mechanism by the C-terminal lid domain.,Yanai T, Takahashi Y, Katsumura E, Sakai N, Takeshita K, Imaizumi R, Matsuura H, Hongo S, Waki T, Takahashi S, Yamamoto M, Kataoka K, Nakayama T, Yamashita S J Biochem. 2023 Sep 29;174(4):335-344. doi: 10.1093/jb/mvad048. PMID:37384427^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.