Amino Acids

, Volume 1, Issue 3, pp 293–306 | Cite as

The chemistry of natural enzyme-induced cross-links of proteins

  • A. J. Bailey
Review Article

Summary

The cross-linking of protein molecules to form stable supramolecular aggregates capable of acting as protective and supporting structures is a common feature of organisms coping with the stresses of life. These new polymeric forms range from thick rigid structures to thin flexible membranes. The formation of such cross-links must be carefully controlled since more or less than optimal cross-linking could lead to malfunction or even death of the organism. The chemistry of the amino acids converted or directly involved in the formation of these cross-links is complex and a range of new amino acids has been identified. Di- and tri-tyrosines are formed by the action of peroxidases, quinones by catechol oxidases,γ glutamyl lysine iso-peptide bonds by glutamyl transferase and a complex series of lysine- aldehyde derived cross-links induced by lysyl oxidase. These cross-linking mechanisms provide an insight into the complex changes in tissue function during growth of the organism and their effects on the properties of foods.

Keywords

Amino acids Cross-links Peroxidases Catechol oxidase Glutamyl transferase Lysyl oxidase Resilin Fibrin Collagen 

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Copyright information

© Springer-Verlag 1991

Authors and Affiliations

  • A. J. Bailey
    • 1
  1. 1.Muscle & Collagen Research GroupUniversity of BristolLangford, BristolEngland

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