Transglutaminases: crosslinking enzymes with pleiotropic functions
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nrm1014.pdf
Reference150 articles.
1. Sarkar, N. K., Clarke, D. D. & Waelsch, H. An enzymically catalyzed incorporation of amines into proteins. Biochim. Biophys. Acta 25, 451–452 (1957). This is the first report of the discovery of a transglutaminase.
2. Cariello, L., et al. Probing the transglutaminase-mediated, posttranslational modification of proteins during development. Biochemistry 29, 5103–5108 (1990).
3. Nemes, Z., Marekov, L. N., Fesus, L. & Steinert, P. M. A novel function for transglutaminase 1: attachment of long-chain ω-hydroxyceramides to involucrin by ester bond formation. Proc. Natl Acad. Sci. USA 96, 8402–8407 (1999). This article reports the identification of the previously unrecognised potential of TGs to catalyse post-translational protein modification by linking long-chain fatty acids (ceramides) through an ester bond (see reaction d in Fig. 1).
4. Shan, L. et al. Structural basis for gluten intolerance in celiac sprue. Science 297, 2218–2220 (2002). This article shows that in vitro treatment of proline-rich deamidated peptides with the enzyme prolylendopeptidase destroys their antigenic properties, offering perhaps a strategy for oral peptidase supplement therapy in lieu of a gluten-free diet in gluten sensitivity diseases.
5. Lorand, L., Campbell, L. & Robertson, B. in Biochemistry Vol. 11 (ed. Green, D) 434–438 (CRC Press, Boca Raton, USA, 1972).
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