Structural Biology of Biosynthetic Enzymes

This group is located at the Helmholtz Institute for Pharmaceutical Research Saarland (HIPS)

Natural agents have always been the best source of antibiotics. This is exemplified by success stories such as penicillin, streptomycin, erythromycin and rifamycin. But the potential of natural agents is not being tapped to the fullest extent yet. Often, this is related to the chemical synthesis being difficult and the yields of the purification of the agents from natural sources being low. Consequently, a large number of promising natural substances have been discovered, but were not developed further for clinical application, either because their chemical structure could not be changed sufficiently or because it was impossible to produce sufficient amounts of them.


Our Research

Organic synthesis of natural substances is often associated with difficult production conditions, such as toxic organic solvents and high temperatures. The fact that enzymes can catalyse complex chemical reactions in aqueous solutions and at room temperature makes them an interesting and environment-friendly alternative.

The junior research group, "Structural Biology of Biosynthetic Enzymes", seeks to understand how certain enzymes work in order to be able to use the conversion power of enzymes and gain fundamental insights into their basic biochemical principles. The improved understanding of the properties of an enzyme will then be used, e.g., to produce modified versions of interesting natural substances in order to further develop promising Antiinfectives or to improve the yield of a natural agent.

To attain this goal, we apply x-ray crystallography to elucidate the structures of interesting enzymes at atomic resolution. The structural data are then linked to biochemical or biophysical data to obtain an even more comprehensive picture. This facilitates subsequent specific and rational modification of the enzymes.


  • HIPS Infofilm (English)

    Resistance to antibiotics has become one of the major global challenges regarding infectious diseases. This is specifically the issue that is being tackled by the new Helmholtz-Institute for Pharmaceutical Research Saarland (HIPS).

  • Surface of the enzyme PurAH

    The surface of the enzyme PurAH with the two catalytic zinc ions (grey spheres) bound at the active site.

  • 3D model of the enzyme BotH

    In bottromycin, a potential antibiotic, bacteria build up a mirrored amino acid. In a study published in the journal Nature Chemical Biology, Jesko Köhnke, head of the junior research group "Structural Biology of Biosynthetic Enzymes" at the Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), describes the enzyme BotH which is necessary for this.

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