Protein-glutamine gamma-glutamyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13) is an enzyme that catalyzes the chemical reaction

protein glutamine + alkylamine $\rightleftharpoons$ protein N₅-alkylglutamine + NH₃

Thus, the two substrates of this enzyme are protein glutamine and alkylamine, whereas its two products are protein N5-alkylglutamine and NH₃.

This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is protein-glutamine:amine gamma-glutamyltransferase. Other names in common use include transglutaminase, Factor XIIIa, fibrinoligase, fibrin stabilizing factor, glutaminylpeptide gamma-glutamyltransferase, polyamine transglutaminase, tissue transglutaminase, and R-glutaminyl-peptide:amine gamma-glutamyl transferase. This enzyme participates in complement and coagulation cascades and huntington's disease. It employs one cofactor, calcium.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes 1EVU, 1EX0, 1F13, 1FIE, 1G0D, 1GGT, 1GGU, 1GGY, 1IU4, 1KV3, 1L9M, 1L9N, 1NUD, 1NUF, 1NUG, 1QRK, 1RLE, 1SGX, and 1VJJ.

[edit] References

IUBMB entry for 2.3.2.13
BRENDA references for 2.3.2.13 (Recommended.)
PubMed references for 2.3.2.13
PubMed Central references for 2.3.2.13
Google Scholar references for 2.3.2.13
Folk JE, Chung SI (1973). "Molecular and catalytic properties of transglutaminases". Adv. Enzymol. Relat. Areas. Mol. Biol. 38: 109–91. doi:10.1002/9780470122839.ch3. PMID 4151471.
Folk JE, Cole PW (1966). "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: 5518–25. PMID 5928192.
Folk JE, Finlayson JS (1977). "The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases". Adv. Protein. Chem. 31: 1–133. PMID 73346.
Takahashi N, Takahashi Y, Putnam FW (1986). "Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta". Proc. Natl. Acad. Sci. U. S. A. 83: 8019–23. doi:10.1073/pnas.83.21.8019. PMID 2877456.