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  1. IPB Halle
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    • Research Mission and Profile
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    • Molecular Signal Processing
      • Secretariat & All Staff
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      • Research Groups
        • Nutrient Sensing
        • Symbiosis Signaling
        • Jasmonate Signaling
    • Bioorganic Chemistry
      • Secretariat & All Staff
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        • Bioactives
        • Natural Products & Metabolomics
        • Biotechnology
        • Biofunctional Synthesis
        • Computational Chemistry
        • Data & Resources
    • Biochemistry of Plant Interactions
      • Secretariat & All Staff
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      • Research Groups
        • Calcium-dependent Protein Kinases
        • Cellular Signaling
        • Metabolite-based Defense Mechanisms
        • Nuclear Processes in Plant Defense
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      • Secretariat & All Staff
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Püllmann, P.; Weissenborn, M. J.; Pilzliche Peroxygenasen: der Schlüssel zu C-H-Hydroxylierungen und mehr? BIOspektrum 25 572-574 (2019) DOI: 10.1007/s12268-019-1090-2
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Fungal peroxygenases represent an exciting new enzyme class for stereo-selective hydroxylation reactions. They are capable of the oxyfunctionalisation of a large, diverse scope of substrates including alkanes and steroids as well as the heteroatoms sulfur and nitrogen. The outstanding activities and stabilities as well as their reliance on hydrogen peroxide as co-substrate renders it a highly interesting biocatalyst.

Publications

Kammel, M.; Knorrscheidt, A.; Püllmann, P.; Weissenborn, M. J.; Tackling the numbers problem: Entwicklung nicht-nativer Enzymreaktionen BIOspektrum 23 830-832 (2017) DOI: 10.1007/s12268-017-0876-3
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The screening effort of large protein variant libraries renders the probability of coincidental discovering a new enzyme with non-natural activity to almost zero - the so-called numbers problem. Insights into the origin of life, evolution and enzymatic promiscuity, combined with the inspiration of methods from organic chemistry, offer solutions for this problem. With the newly discovered enzymes synthetic micro production units shall be established in a Leibniz Research Cluster where engineering and biotechnology are combined.

Publications

Berger, R.; Bornscheuer, U.; Liese, A.; Schwaneberg, U.; Syldatk, C.; Wessjohann, L.; Biotechnologie von Morgen: DECHEMA/VAAM-Fachgruppe „Biotransformationen“ BIOspektrum 19 208-210 (2013) DOI: 10.1007/s12268-013-0291-3
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0

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Wessjohann, L.; Vogt, T.; Kufka, J.; Klein, R.; Prenyl- und Methyltransferasen in Natur und Synthese BIOspektrum 18 22-25 (2012) DOI: 10.1007/s12268-012-0137-4
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Late stage enzymatic prenylation and methylation are means to diversify (natural) compounds and to specify their functions. In eukaryotes and microbes, these steps are performed by large enzyme families, the prenyl and methyl transferases, which modify various types of small molecules, like isoprenoids, phenolics or alkaloids, but also DNA and proteins. We investigate the theoretical basis of these processes and possible commercial applications in synthetic chemistry.

Publications

Dissmeyer, N.; CDK-Phosphorylierung in Zellzyklus und Stress: artspezifische Unterschiede BIOspektrum 751-753 (2010)
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  • RIS

In Arabidopsis, deactivation of cyclin-dependent kinases via phosphorylation has no function in cell proliferation, growth, and stress response. In other eukaryotes, however, this is mandatorily required for maintaining genomic integrity.

Publications

Wessjohann, L. A.; Rivera, D. G.; Vercillo, O. E.; Multiple Multicomponent Macrocyclizations (MiBs): A Strategic Development Toward Macrocycle Diversity Chem. Rev. 109 796-814 (2009) DOI: 10.1021/cr8003407
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0

Publications

Spengler, J.; Böttcher, C.; Albericio, F.; Burger, K.; Hexafluoroacetone as Protecting and Activating Reagent: New Routes to Amino, Hydroxy, and Mercapto Acids and Their Application for Peptide and Glyco- and Depsipeptide Modification Chem. Rev. 106 4728-4746 (2006) DOI: 10.1021/cr0509962
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0

Publications

Wessjohann, L. A.; Brandt, W.; Thiemann, T.; Biosynthesis and Metabolism of Cyclopropane Rings in Natural Compounds Chem. Rev. 103 1625-1648 (2003) DOI: 10.1021/cr0100188
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0

Publications

Feussner, I.; Porzel, A.; Wasternack, C.; Kühn, H.; Quantitative Analyse von Lipoxygenase-Metaboliten in Lipiden durch NMR-Spektroskopie BIOspektrum 3 54-58 (1997)
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