| EC |
2.3.2.13 |
| 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 |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 80146-85-6 |
| References: |
| 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. [DOI] [PMID: 2877456] |
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| [EC 2.3.2.13 created 1978, modified 1981, modified 1983] |
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