• 2.13
  • Transglutaminases (EC 2.3.2.13) (TGase) [ PMID: 1974250 , PMID: 1683845 ] are calcium-dependent enzymes that catalyze the cross-linking of proteins by promoting the formation of isopeptide bonds between the gamma-carboxyl group of a glutamine in one polypeptide chain and the epsilon-amino group of a lysine in a second polypeptide chain. (ebi.ac.uk)
  • Transglutaminases (E.C. 2.3.2.13) are a family of calcium-dependent thiol enzymes which catalyze the covalent cross-linking of peptide-bound glutamine residues to a variety of primary amines, including the epsilonamino group of peptide-bound lysine residues (reviewed by Folk, 1980). (springer.com)
  • catalytic
  • The cellular form is a dimer of two identical subunits, FXIII-A, each consisting of an activation peptide that is cleaved upon activation, a β-sandwich domain, a catalytic transglutaminase domain and two β-barrel domains. (wikipedia.org)
  • Three-dimensional modeling of TG5 showed that G113C lies close to the catalytic domain, and, furthermore, that this glycine residue is conserved in all known transglutaminases, which is consistent with pathogenicity. (wikipedia.org)