Glycan Phosphorylases in Multi-Enzyme Synthetic Processes

Protein Pept Lett. 2017;24(8):696-709. doi: 10.2174/0929866524666170811125109.

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.

Keywords: Phosphorylase; biofuel; cellodextrin; disaccharide; high-value products; α-glucan.

Publication types

  • Review

MeSH terms

  • Biofuels / supply & distribution
  • Carbohydrate Conformation
  • Cellulose / analogs & derivatives*
  • Cellulose / chemistry
  • Cellulose / metabolism
  • Chemistry Techniques, Synthetic*
  • Dextrins / chemistry*
  • Dextrins / metabolism
  • Disaccharides / chemistry*
  • Disaccharides / metabolism
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Glucans / chemistry*
  • Glucans / metabolism
  • Glycosylation
  • Kinetics
  • Phosphorylases / chemistry*
  • Phosphorylases / metabolism
  • Plants / enzymology
  • Plants / genetics
  • Starch / chemistry
  • Starch / metabolism
  • Substrate Specificity

Substances

  • Biofuels
  • Dextrins
  • Disaccharides
  • Glucans
  • Cellulose
  • Starch
  • cellodextrin
  • Phosphorylases