1. Academic Validation
  2. β-Glucosidases

β-Glucosidases

  • Cell Mol Life Sci. 2010 Oct;67(20):3389-405. doi: 10.1007/s00018-010-0399-2.
James R Ketudat Cairns 1 Asim Esen
Affiliations

Affiliation

  • 1 Schools of Biochemistry and Chemistry, Institute of Science, Suranaree University of Technology, 111 University Avenue, Muang District, Nakhon Ratchasima, Thailand. cairns@sut.ac.th
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.

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