Glycan Phosphorylases in Multi-Enzyme Synthetic Processes.

Giulia Pergolizzi, Sakonwan Kuhaudomlarp, Eeshan Kalita, Robert A Field

Journal: Protein and peptide letters 2017;24(8):696-709

PMID: 28799504

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Abstract

Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by glycosylation with concomitant release of inorganic phosphate. The equilibrium position of such reactions can render them of limited synthetic utility, unless coupled with a secondary enzymatic step where the reaction lies heavily in favour of product. This article surveys recent works on the combined use of glycan phosphorylases with other enzymes to achieve synthetically useful processes.

Address: Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH. United Kingdom.

DOI: 10.2174/0929866524666170811125109

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MeSH Terms: Biofuels, Carbohydrate Conformation, Cellulose, Chemistry Techniques, Synthetic, Dextrins, Disaccharides, Escherichia coli, Glucans, Glycosylation, Kinetics, Phosphorylases, Plants, Starch, Substrate Specificity