The Enzyme Database

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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, 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. [PMID: 2877456]
[EC 2.3.2.13 created 1978, modified 1981, modified 1983]
 
 


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