Cellular and Molecular Life Sciences

, Volume 67, Issue 20, pp 3389–3405 | Cite as

β-Glucosidases

Review

Abstract

β-Glucosidases (3.2.1.21) 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.

Keywords

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

Notes

Acknowledgments

Rodjana Opassiri and three anonymous reviewers are thanked for useful comments on the manuscript. JRKC was supported by Suranaree University of Technology and the Thailand Research Fund.

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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

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