Protein-Oligosaccharide Interactions: Lysozyme, Phosphorylase, Amylases

  • L. N. Johnson
  • J. Cheetham
  • P. J. McLaughlin
  • K. R. Acharya
  • D. Barford
  • D. C. Phillips
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 139)


Polysaccharides have many diverse biological roles. They comprise the insoluble structural and supportive elements of bacterial and plant cell walls. They serve as storage macromolecules (e.g., glycogen and starch) to provide fuel for cells, and they form important components in the heteromacromolecules, proteoglycans and glycoproteins, which are involved in the structural elements of connective tissue, in the lubrication of skeletal joints, in cell-cell adhesion and in cell-surface recognition. The enzymes that catalyze the biosynthesis and degradation of these polysaccharides are highly specific, resulting, in the case of biosynthesis, in polymers of defined constitution and sequence and, in the case of degradation in the cleavage of specific linkages. In this article we describe the X-ray structural results for three of these enzymes: lysozyme, glycogen phosphorylase, and amylase. Each catalyzes a specific step in the degradation of different polysaccharides. (To date there are no structural data on any of the biosynthetic enzymes.) Lysozyme catalyzes the hydrolysis of a β-(1–4) linkage of bacterial cell wall polysaccharides; glycogen phosphorylase catalyzes the reversible phosphorylation of α-(1–4) linkages of glycogen and amylase catalyzes the hydrolysis of α-(1–4) linkages in starch. We use these results in an attempt to draw together some general principles that appear to be important in generating a protein-oligosaccharide recognition site and compare these features with protein monosaccharide sites.


Catalytic Site Storage Site Glycogen Phosphorylase Pyranose Ring Oligosaccharide Binding 
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Copyright information

© Springer-Verlag Berlin · Heidelberg 1988

Authors and Affiliations

  • L. N. Johnson
    • 1
  • J. Cheetham
    • 1
  • P. J. McLaughlin
    • 1
  • K. R. Acharya
    • 1
  • D. Barford
    • 1
  • D. C. Phillips
    • 1
  1. 1.Laboratory of Molecular BiophysicsOxfordUK

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