Transglutaminase enzyme (TG (commonly used); TG2 (for tissue transglutaminase, a prominent member of the family))

Transglutaminases are a family of enzymes that catalyze post-translational modification of proteins by forming covalent cross-links between lysine and glutamine residues, creating resilient isopeptide bonds. These enzymes are widely distributed in nature, with at least eight members encoded in the human genome. Their activities are involved in diverse biological functions including stabilization of the extracellular matrix, regulation of cell adhesion and motility, wound healing, apoptosis, and blood clotting. Transglutaminases—especially tissue transglutaminase (TG2)—are implicated in diseases such as cancer, neurodegeneration, and autoimmunity (notably celiac disease, as TG2 is a major autoantigen). In food technology, microbial transglutaminase is used for protein cross-linking, known as "meat glue." Therapeutic targeting of transglutaminase enzymatic activity is an active area of research for autoimmune and fibrotic diseases, but is challenged by their multifunctional roles and widespread biological importance[1][2][3][4][5][6][9][10].

Other names

TGTissue transglutaminase (for TG2)Protein-glutamine-γ-glutamyltransferaseMeat glue (in food industry)

Inhibition of cross-linking enzymatic activity (blocking isopeptide bond formation) Inhibition of post-translational modification or deamidation of glutamine residues Blocking protein-protein cross-linking may reduce tissue fibrosis or autoantigen generation