Structures and mechanisms of glycosyl hydrolases.
By G. Davies, Bernard Henrissat. 1995
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Citations in the corpus
- α-l-Arabinofuranosidases: the potential applications in biotechnology (2006, background): “This classification is useful to study evolutionary relationship, mechanistic information and structural features of these enzymes [25].”
- Carbohydrate metabolism in Bifidobacteria (2011, background): “Depending on the spatial position of these catalytic residues, hydrolysis occurs via overall retention or inversion of the anomeric configuration [15].”
- Cloning and Biochemical Characterization of BglC, a β-Glucosidase from the Cellulolytic Actinomycete Thermobifida fusca (2001, background): “BglC clearly belongs to glycosyl hydrolase family 1, which contains retaining enzymes employing a double displacement mechanism of catalysis [7, 25, 32].”
- Dissecting enzyme function with microfluidic-based deep mutational scanning (2015, background): “Bgl3 is a member of glycoside hydrolase family 1 (GH1), a large enzyme family accepting a broad range of glycosylated substrates (20, 21).”
- Plant Chitinases: Genetic Diversity and Physiological Roles (2012, background): “Glycosyl hydrolases are a group of enzymes that cleave the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety (Davies and Henrissat, 1995).”
- β-Xylosidases from filamentous fungi: an overview (2010, background): “3), a widespread group of enzymes that hydrolyze glycosidic bonds between two or more carbohydrates or between a carbohydrate and a noncarbohydrate moiety (Davies and Henrissat 1995).”
- Novel enzymes for the degradation of cellulose (2012, background): “In this sense these novel enzymes differ dramatically from classical glucanases, which need to position single chains in their active sites grooves, clefts or tunnels [48], and which normally are active on soluble oligosaccharides.”