Institute of Molecular Microbiology and Biotechnology

The Fetzner group (Institute of Molecular Microbiology and Biotechnology)

Prof. Susanne Fetzner is an expert in the area of microbial metabolic pathways and enzymology, with a focus on enzymes active toward aromatic and heterocyclic compounds. Major aims are to understand the physiological roles and catalytic mechanisms of the enzymes, and to modify and improve their activities for potential applications. This includes: (1) in vitro pathway reconstruction using isolated enzymes, (2) investigations of how enzymes recognize, bind and activate their substrate(s), (3) investigations of how enzymes perform catalysis, and (4) knowledge-based enzyme engineering.

Key findings are the elucidation of the reaction pathway of a cofactor-independent dioxygenase and of cofactor-independent O2 activation, and the detection of enzymes which specifically inactivate virulence-associated Pseudomonas aeruginosa quorum sensing molecules.

Susanne Fetzner has published >80 peer-reviewed papers with >1,800 citations; her h-index is 25 (Google Scholar). She was awarded the Research Prize of the University of Münster in 2010.

Recent top publications

  1. Drees, S.L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J. & Fetzner, S. (2016) PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291:6610-6624.
  2. Müller, C., Birmes, F.S., Rückert, C., Kalinowski, J. & Fetzner, S. (2015) Rhodococcus erythropolis BG43 genes mediating Pseudomonas aeruginosa quinolone signal degradation and virulence factor attenuation. Appl. Environ. Microbiol. 81:7720-7729.
  3. Drees, S.L. & Fetzner, S. (2015) PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22:611-618.
  4. Thierbach S, Bui N, Zapp J, Chhabra SR, Kappl R, Fetzner S. (2014) Substrate-assisted O2 activation in a cofactor-independent dioxygenase, Chem. Biol. 21:217-225. Referred to by: Bugg, T.D.H.: How to break the rules of dioxygen activation. Chem. Biol. 21:168-169.