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

Abstract:

: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.

journal_name

Amino Acids

journal_title

Amino acids

authors

Bailey AJ

doi

10.1007/BF00813999

subject

Has Abstract

pub_date

1991-10-01 00:00:00

pages

293-306

issue

3

eissn

0939-4451

issn

1438-2199

journal_volume

1

pub_type

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