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- W2293897411 abstract "Disaccharide phosphorylases are interesting enzymes for use in glycoside synthesis since they pose a number of advantages over glycoside hydrolases and glycosyltransferases, enzymes more traditionally used for this purpose: they require no expensive nucleotide-activated substrates and catalyze a reversible reaction. In this dissertation we describe the successful cloning, expression, purification, crystallization and the determination of the 3-dimensional structure of two disaccharide phosphorylases in the absence and the presence of ligands binding in the active site. Trehalose phosphorylase from Thermoanaerobacter sp. (EC 2.4.1.64) is the second 3-dimensional structure reported in the CAZy family GH65 and the first representative with this activity. The enzyme is shown to be a dimer displaying a characteristic fold comprising 4 domains. In addition, a partial kinetic characterization is presented which reveals the enzyme likely acts according to a ternary complex mechanism whereby trehalose binds before phosphate and D-glucose and β-D-glucose 1-phosphate are released in that order. Cellobiose phosphorylase from Cellulomonas uda (EC 2.4.1.20) belongs to GH family 94, together with cellodextrin phosphorylase and chitobiose phosphorylase. Its 3-dimensional structure, together with the structure of a mutant C. uda cellobiose phosphorylase with altered substrate specificity, is reported. Differences between both structures show cellobiose phosphorylase is a dynamic structure which undergoes conformational changes upon substrate binding. The potential mechanistic consequences are discussed." @default.
- W2293897411 created "2016-06-24" @default.
- W2293897411 creator A5029013198 @default.
- W2293897411 date "2010-01-01" @default.
- W2293897411 modified "2023-09-23" @default.
- W2293897411 title "Structure-functional studies of bacterial glycoside phosphorylases" @default.
- W2293897411 hasPublicationYear "2010" @default.
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