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Originally published In Press as doi:10.1074/jbc.M004273200 on August 1, 2000

J. Biol. Chem., Vol. 275, Issue 41, 31838-31846, October 13, 2000
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Molecular Characterization of Lantibiotic-synthesizing Enzyme EpiD Reveals a Function for Bacterial Dfp Proteins in Coenzyme A Biosynthesis*

Thomas KupkeDagger §, Michael Uebele, Dietmar Schmid, Günther Jung, Michael Blaesse||, and Stefan Steinbacher||

From the Dagger  Lehrstuhl für Mikrobielle Genetik, Universität Tübingen, Auf der Morgenstelle 15, Verfügungsgebäude, 72076 Tübingen, the  Institut für Organische Chemie, Universität Tübingen, Auf der Morgenstelle 18, 72076 Tübingen, and the || Abteilung für Strukturforschung, MPI für Biochemie, 82152 Planegg-Martinsried, Germany

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 suggested that they catalyze a similar reaction like EpiD and/or may have similar substrates and are homododecameric flavoproteins. We demonstrate that the N-terminal domain of the Escherichia coli Dfp protein catalyzes the decarboxylation of (R)-4'-phospho-N-pantothenoylcysteine to 4'-phosphopantetheine. This reaction is essential for coenzyme A biosynthesis.

* This work was supported by Deutsche Forschungsgemeinschaft Grant KU869/4-1 and the University of Tübingen Strukturfond (to T. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence and reprint requests should be addressed. E-mail: Thomas.Kupke@t-online.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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