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.

Autor: Yanai, Taro, Takahashi, Yukino, Katsumura, Eri, Sakai, Naoki, Takeshita, Kohei, Imaizumi, Riki, Matsuura, Hiroaki, Hongo, Shuntaro, Waki, Toshiyuki, Takahashi, Seiji, Yamamoto, Masaki, Kataoka, Kunishige, Nakayama, Toru, Yamashita, Satoshi
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Zdroj: Journal of Biochemistry; Oct2023, Vol. 174 Issue 4, p335-344, 10p
Abstrakt: The sesaminol triglucoside (STG)-hydrolyzing β-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-β-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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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