Cellular and Molecular Life Sciences

, Volume 67, Issue 20, pp 3389-3405

First online:


  • James R. Ketudat CairnsAffiliated withSchools of Biochemistry and Chemistry, Institute of Science, Suranaree University of Technology Email author 
  • , Asim EsenAffiliated withDepartment of Biological Sciences, Virginia Polytechnic Institute and State University

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β-Glucosidases ( are found in all domains of living organisms, where they play essential roles in the removal of nonreducing terminal glucosyl residues from saccharides and glycosides. β-Glucosidases function in glycolipid and exogenous glycoside metabolism in animals, defense, cell wall lignification, cell wall β-glucan turnover, phytohormone activation, and release of aromatic compounds in plants, and biomass conversion in microorganisms. These functions lead to many agricultural and industrial applications. β-Glucosidases have been classified into glycoside hydrolase (GH) families GH1, GH3, GH5, GH9, and GH30, based on their amino acid sequences, while other β-glucosidases remain to be classified. The GH1, GH5, and GH30 β-glucosidases fall in GH Clan A, which consists of proteins with (β/α)8-barrel structures. In contrast, the active site of GH3 enzymes comprises two domains, while GH9 enzymes have (α/α)6 barrel structures. The mechanism by which GH1 enzymes recognize and hydrolyze substrates with different specificities remains an area of intense study.


Biological function Structure Substrate-specificity Glycoside hydrolase Glycosides Structure–function relationships