Functional Characterization of the Recombinant N-Methyltransferase Domain from the Multienzyme Enniatin Synthetase (pages 1048–1054)
Till Hornbogen, Sean-Patrick Riechers, Bianka Prinz, Jeffrey Schultchen, Christine Lang, Sebastian Schmidt, Clemens Mügge, Suada Turkanovic, Roderich D. Süssmuth, Eva Tauberger and Rainer Zocher
Version of Record online: 30 APR 2007 | DOI: 10.1002/cbic.200700076
The heart of the matter: The N-methyltransferase domain of enniatin synthetase (ENMT) from Fusarium scirpi was functionally expressed. The recombinant protein was found to be active by using S-adenosyl methionine (AdoMet) as methyl donor in cross-linking experiments and saturation transfer difference NMR spectroscopy studies (see scheme). Methyl group transfer was demonstrated by using aminoacyl-N-acetylcysteamine thioesters as substrates.