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| Content Provider | Springer Nature Link |
|---|---|
| Author | Ketudat Cairns, James R. Esen, Asim |
| Copyright Year | 2010 |
| 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. |
| Starting Page | 3389 |
| Ending Page | 3405 |
| Page Count | 17 |
| File Format | |
| ISSN | 1420682X |
| Journal | Cellular and Molecular Life Sciences |
| Volume Number | 67 |
| Issue Number | 20 |
| e-ISSN | 14209071 |
| Language | English |
| Publisher | SP Birkhäuser Verlag Basel |
| Publisher Date | 2010-05-20 |
| Publisher Place | Basel |
| Access Restriction | Subscribed |
| Subject Keyword | Biological function Structure Substrate-specificity Glycoside hydrolase Glycosides Structure–function relationships Biochemistry Life Sciences Biomedicine general Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience |
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