Transglutaminase
（重定向自Transglutaminases）
![The upper reaction shows how a transaminase combines with a glutamine residue, releasing ammonia, and then the combination reacts with the amine group of a lysine residue of another protein, setting the enzyme free again.](/Images/godic/202502/17/Transamidation_and_deamidation_mechanisms_of_tissue_transglutaminase4040.jpg")
![Three bistro tenders being joined together with transglutaminase](/Images/godic/202502/17/GluedBistroTenders4040.jpg")
A transglutaminase is an enzyme that catalyzes the formation of an isopeptide bond between a free amine group (e.g., protein- or peptide-bound lysine) and the acyl group at the end of the side chain of protein- or peptide-bound glutamine. The reaction also produces a molecule of ammonia. Such an enzyme is classified as EC2.3.2.13. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis).