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Journal of Bacteriology, March 2002, p. 1234-1243, Vol. 184, No. 5
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.5.1234-1243.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Flavoprotein MrsD Catalyzes the Oxidative Decarboxylation Reaction Involved in Formation of the Peptidoglycan Biosynthesis Inhibitor Mersacidin

Florian Majer,¹ Dietmar G. Schmid,² Karsten Altena,^3, Gabriele Bierbaum,³ and Thomas Kupke^1*

Mikrobielle Genetik, Universität Tübingen, Auf der Morgenstelle 15, Verfügungsgebäude,¹ Institut für Organische Chemie, Universität Tübingen, Auf der Morgenstelle 18, 72076 Tübingen,² Institut für Medizinische Mikrobiologie und Immunologie, Universität Bonn, 53105 Bonn, Germany³

Received 27 August 2001/ Accepted 26 November 2001

The lantibiotic mersacidin inhibits peptidoglycan biosynthesis by binding to the peptidoglycan precursor lipid II. Mersacidin contains an unsaturated thioether bridge, which is proposed to be synthesized by posttranslational modifications of threonine residue +15 and the COOH-terminal cysteine residue of the mersacidin precursor peptide MrsA. We show that the flavoprotein MrsD catalyzes the oxidative decarboxylation of the COOH-terminal cysteine residue of MrsA to an aminoenethiol residue. MrsD belongs to the recently described family of homo-oligomeric flavin-containing Cys decarboxylases (i.e., the HFCD protein family). Members of this protein family include the bacterial Dfp proteins (which are involved in coenzyme A biosynthesis), eukaryotic salt tolerance proteins, and further oxidative decarboxylases such as EpiD. In contrast to EpiD and Dfp, MrsD is a FAD and not an FMN-dependent flavoprotein. HFCD enzymes are characterized by a conserved His residue which is part of the active site. Exchange of this His residue for Asn led to inactivation of MrsD. The lantibiotic-synthesizing enzymes EpiD and MrsD have different substrate specificities.

Present address: Abteilung Biotechnik, Pharma-Zentrale GmbH, 58313 Herdecke, Germany.

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