Transglutaminases: multifunctional cross‐linking enzymes that stabilize tissues
@article{Greenberg1991TransglutaminasesMC, title={Transglutaminases: multifunctional cross‐linking enzymes that stabilize tissues}, author={Charles S. Greenberg and Paul J. Birckbichler and Robert H. Rice}, journal={The FASEB Journal}, year={1991}, volume={5}, pages={3071 - 3077} }
Transglutaminases catalyze the posttranslational modification of proteins by transamidation of available glutamine residues. This action results primarily in the formation of ∊‐(γ‐glutamyl)lysine cross‐links but includes the incorporation of polyamines into suitable protein substrates as well. The covalent isopeptide crosslink is stable and resistant to proteolysis, thereby increasing the resistance of tissue to chemical, enzymatic, and mechanical disruption. The plasma transglutaminase, factor…
946 Citations
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Data is reviewed on the properties of mammalian transglutaminases, particularly as regards their protein substrates and the relevance of transglUTaminase‐catalysed reactions in physiological and disease conditions.
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Transglutaminases (Tgases) are a widely distributed group of enzymes that catalyse the post-translational modification of proteins by the formation of isopeptide bonds. This occurs either through…
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A comprehensive review of recent insights into the pathophysiology of TGs related to their protein cross-linking activity is presented.
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