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Overview
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Background
Transglutaminases are a family of enzymes that catalyse the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains (Folk, J. E. and Cole, P. W., 1966). These enzymes catalyse the acyl transfer reaction between the γ-carboxyamide group of peptide-bound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine (Lorand L. et al., 1962). The resulting cross link is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation.
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Overview