Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis.

@article{Kupke2000MolecularCO,
  title={Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis.},
  author={Thomas Kupke and Michael Uebele and Daphn{\'e} Schmid and Gunther Jung and Michael Blaesse and Stefan Steinbacher},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 41},
  pages={
          31838-46
        }
}
The lantibiotic-synthesizing flavoprotein EpiD catalyzes the oxidative decarboxylation of peptidylcysteines to peptidyl-aminoenethiols. The sequence motif responsible for flavin coenzyme binding and enzyme activity is conserved in different proteins from all kingdoms of life. Dfp proteins of eubacteria and archaebacteria and salt tolerance proteins of yeasts and plants belong to this new family of flavoproteins. The enzymatic function of all these proteins was not known, but our experiments… CONTINUE READING
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