Abstract
The glycosidases are a class of enzymes that are responsible for the hydrolysis of glycosidic bonds. Such glycosidic linkages occur in a wide range of contexts, including polysaccharides, oligosaccharides, glycolipids, glycoproteins, lipopolysaccharides, proteoglycans, saponins, and a range of other glycoconju-gates. Corresponding to this diverse collection of substrates there is a very large assortment of glycosidases responsible for their selective hydrolysis. Amino acid sequences are now available for well over 2000 of these enzymes, and these have been arranged into families on the basis of sequence similarities (1–4). At the last count (November 1999) there were 76 such families, and a regularly updated list of these is readily available at the URL http://afmb.cnrs-mrs.fr/ R~pedro/CAZY/db.html. A large amount of effort has been expended on structural studies of these enzymes in the past 10 yr with the result that three-dimensional X-ray crystal structures are now available for representatives of at least 27 of these families (4–6). These structures are remarkably diverse, with monomer sizes ranging from approx 14,000 to 170,000 Daltons, and compositions ranging from essentially completely α-helical to almost exclusively β-sheet. The reasons for this diversity are probably twofold; the diverse nature of the substrates themselves, and different evolutionary pathways to the construction of an active site.
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Vocadlo, D.J., Withers, S.G. (2000). Identification of Active Site Residues in Glycosidases by Use of Tandem Mass Spectrometry. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:203
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DOI: https://doi.org/10.1385/1-59259-045-4:203
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