Carbohydrates are structurally and functionally diverse materials including polysaccharides, and marine organisms are known to have many enzymes for the breakdown of complex polysaccharides. Here, we identified an α-l-fucosidase enzyme from the marine bacterium Vibrio sp. strain EJY3 (VejFCD) that has dual α-1,4-glucosidic and β-1,4-galactosidic specificities. We determined the crystal structure of VejFCD and provided the structural basis underlying the dual α- and β-glycosidase activities of the enzyme. Unlike other three-domain FCDs, in VejFCD, carbohydrate-binding module-B (CBM-B) with a novel β-sandwich fold tightly contacts with the CatD/CBM-B main body and provides key residues for the β-1,4-glycosidase activity of the enzyme. The phylogenetic tree analysis suggests that only a few FCDs from marine microorganisms have the key structural features for dual α-1,4- and β-1,4-glycosidase activities. This study provides the structural insights into the mechanism underlying the novel glycoside hydrolase activities and could be applied for more efficient utilization in the hydrolysis of complex carbohydrates in biotechnological applications.
Bibliographical noteFunding Information:
This work was supported by the Basic Science Research Program (NRF2020R1A4A1018332) and the Mid-career Researcher Program (2020R1A2B5B02002631) through the National Research Foundation of Korea (NRF) funded by the Korea government (MSIT).
© 2021 American Chemical Society.
- Vibrio sp. strain EJY3
- dual α-1,4- and β-1,4-glycosidase: carbohydrate-binding module
- marine microorganism
- α- l -fucosidase
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)