Cellular transglutaminases in neural development

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Abstract
Enzymes of the transglutaminase family catalyze the Ca2+-dependent covalent cross-linking of peptide-bound glutamine residues of proteins and glycoproteins to the ε-amino group of lysine residues to create inter- or intramolecular isopeptide bonds. Transglutaminases can also covalently link a variety of primary amines to peptide-bound glutamine residues giving rise to two possibilities; firstly, where the primary amine has two or more amine groups, further catalysis can result in the formation of cross-linked bridges between glutamine residues, and secondly, where the primary amine is a monoamine, glutamine residues are rendered inert to further modification. The products are therefore in the main, homo- or heterodimers, or extensive, metabolically-stable multimeric complexes or matrices.