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Protein Modifications catalysed by Transglutaminase

Abstract

WORK from this laboratory has shown that transglutaminase catalyses the hydrolysis of the amide group of protein-bound glutamine, and its exchange with primary amines1. In addition, preliminary evidence indicated that the ε-amino group of protein-bound lysine may act as a replacing amine2. Therefore, by the action of transglutaminase, various proteins can be modified and the new protein species may have properties unlike those of the original protein; for example, proteins may acquire novel antigenic properties as shown by proteins in which the ε-amino group of lysine had been modified by substitution with polyamino-acids by chemical means3,4. Modifications produced enzymatically by the linkage of two proteins to each other through the γ-carboxyl group of protein-bound glutamic acid and the ε-amino group of protein-bound lysine are of particular interest.

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KORNGUTH, S., WAELSCH, H. Protein Modifications catalysed by Transglutaminase. Nature 198, 188–189 (1963). https://doi.org/10.1038/198188a0

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