Cellular and Molecular Life Sciences

, Volume 67, Issue 20, pp 3389–3405



DOI: 10.1007/s00018-010-0399-2

Cite this article as:
Ketudat Cairns, J.R. & Esen, A. Cell. Mol. Life Sci. (2010) 67: 3389. doi:10.1007/s00018-010-0399-2


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 functionStructureSubstrate-specificityGlycoside hydrolaseGlycosidesStructure–function relationships

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© Springer Basel AG 2010

Authors and Affiliations

  1. 1.Schools of Biochemistry and Chemistry, Institute of ScienceSuranaree University of TechnologyNakhon RatchasimaThailand
  2. 2.Department of Biological SciencesVirginia Polytechnic Institute and State UniversityBlacksburgUSA