Protein Glutamine gamma Glutamyltransferases, also known as transglutaminases, are a group of enzymes that catalyze the formation of covalent bonds between proteins or peptides. These enzymes play a crucial role in various biological processes, including blood clotting, wound healing, and the formation of the skin's protective barrier.
Protein Glutamine gamma Glutamyltransferases are primarily involved in a post-translational modification known as protein crosslinking. They accomplish this by catalyzing the formation of an isopeptide bond between the side chains of glutamine residues and glutamate residues. This process is often referred to as transamidation or transglutamination.
The catalytic activity of Protein Glutamine gamma Glutamyltransferases is calcium-dependent. These enzymes possess a conserved catalytic triad consisting of cysteine, histidine, and aspartate residues, which are responsible for their enzymatic activity. Glutamine residues serve as the substrate for transamidation reactions, while glutamate residues act as the acyl acceptor.
The physiological functions of Protein Glutamine gamma Glutamyltransferases are diverse and tissue-specific. For instance, in the skin, these enzymes are responsible for the formation of the cornified envelope, a crucial component of the skin's barrier function. In the blood coagulation pathway, transglutaminases play a role in stabilizing fibrin clots.
Dysregulation of Protein Glutamine gamma Glutamyltransferases has been implicated in various diseases, including autoimmune disorders, neurological disorders, and certain cancers. Therefore, these enzymes are of great interest as potential therapeutic targets.
Overall, Protein Glutamine gamma Glutamyl
