Accepted name: protein-glutamine γ-glutamyltransferase
Reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Other name(s): transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase
Systematic name: protein-glutamine:amine γ-glutamyltransferase
Comments: Requires Ca2+. The γ-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
1.  Folk, J.E. and Chung, S.I. Molecular and catalytic properties of transglutaminases. Adv. Enzymol. Relat. Areas Mol. Biol. 38 (1973) 109–191. [PMID: 4151471]
2.  Folk, J.E. and Cole, P.W. Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity. J. Biol. Chem. 241 (1966) 5518–5525. [PMID: 5928192]
3.  Folk, J.E. and Finlayson, J.S. The ε-(γ-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv. Protein Chem. 31 (1977) 1–133. [PMID: 73346]
4.  Takahashi, N., Takahashi, Y. and Putnam, F.W. Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc. Natl. Acad. Sci. USA 83 (1986) 8019–8023. [PMID: 2877456]
[EC created 1978, modified 1981, modified 1983]

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