EC - Protein-glutamine γ-glutamyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
protein-glutamine γ-glutamyltransferase
Other names:
R-glutaminyl-peptide:amine γ-glutamyl transferase
Factor XIIIa
fibrin stabilizing factor
glutaminylpeptide γ-glutamyltransferase
polyamine transglutaminase
tissue transglutaminase
Systematic name:
protein-glutamine:amine γ-glutamyltransferase




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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00473
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003810
CAS Registry Number: 80146-85-6
UniProtKB/Swiss-Prot: (50) [show] [UniProt]


  1. Folk, J.E. and Chung, S.I.
    Molecular and catalytic properties of transglutaminases.
    Adv. Enzymol. Relat. Areas Mol. Biol. 38: 109-191 (1973). [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: 5518-5525 (1966). [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: 1-133 (1977). [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: 8019-8023 (1986). [PMID: 2430312]

[EC created 1978, modified 1981, modified 1983]