Transglutaminase main reaction: Crosslinking by William Bains смотреть онлайн

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CROSSLINKING OR TRANSAMIDATION

The major function of transglutaminases (TGs) is the covalent cross-linking of one protein chain via a glutamine residue to a lysine residue of another protein chain in a reaction termed transamidation (Elli 2009).

Transglutaminases catalyzes the formation of ε -(γ-glutamyl)lysine bonds between a selected glutamine residue of one protein and a lysine residue of another protein, leading to protein crosslinking (Remon Van Geel 1982).

BETWEEN GLUTAMINE AND LYSINE

Transglutaminases catalyzes post-translational cross-link reactions between two substrates that can be two proteins or two residues of the same protein, involving lysine and glutamine (Serafini-Fracassini and Del Duca 2008).

The transglutaminases are a family of structurally and functionally related enzymes which catalyze Ca2+-dependent post-translational modification of proteins by introducing a protein-protein crosslink between a specific glutamine and a lysine residue (Klöck et al. 2012)

Transglutaminase is an enzyme that catalyzes the formation of isopeptide cross-links between glutamine and lysine residues in a variety of proteins (Sugimura 2006).

RESULTING BOND; A COVALENT BOND TERMED "ISOPEPTIDE BOND":

The cross-link formed is called an ε-(γ-glutamyl)lysine isopeptide bond (Lantto 2007).

The TG catalyzes the formation of ε-( γ-glutamyl) lysine bonds (isopeptide bond) between peptide-bound glutamine residues and the primary amine group of various amines (Haroon 1999).

The ε-(γ-glutamyl)lysine isopeptide bond is highly resistant to proteolysis and denaturants and it gives stable, rigid and insoluble protein complexes (Sulic 2011).

The resulting bonds are covalent, stable, and resistant to proteolysis, thereby increasing the resistance of tissues to chemical, enzymatic, and physical degradation (Greenberg 1991).

These isopeptide bonds are stable and more resistant to proteolytic degradation than noncovalent linkages. The covalent cross-linking reaction increases the resistance of proteins to chemical, enzymatic, and physical disruption (Haroon 1999).


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