Historical Background
Transglutaminases (TGs) are a family of enzymes (EC 2.3.2.13) that catalyze the formation of amide bonds between proteins to form insoluble cross-linked protein aggregates that are resistant to chemicals, detergents, and proteases degradation (Griffin et al. 2002; Yokoyama et al. 2004).
TG activity was first observed in 1957 by Clarke et al. (1957), when they found an enzyme with transamidating properties extracted from guinea pig liver. Only in 1959 the name transglutaminase was assigned by Waelsch and collaborators (Mycek et al. 1959), in order to distinguish this enzymatic activity from that of other enzymes with similar activity.
TGs catalyzes posttranslational cross-link reactions between two substrates that can be two proteins or two residues of the same...
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Martins, I.M., Choupina, A. (2018). Protein-Glutamine Gamma-Glutamyltransferase. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101758
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