Melanie Schoppet

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Department of Biomolecular Mechanisms, M Jahnstrasse 29, 69120 Heidelberg, Germany Interfaculty Institute of Microbiology Microbiology/Biotechnology, University of 72076 Tuebingen, Germany. E-mail: evi.steg EMBL Australia, Monash University, Clayto cryle@monash.edu The Monash Biomedicine Discovery Inst Molecular Biology, Monash University, Clay Institut für(More)
Halogenation plays a significant role in the activity of the glycopeptide antibiotics (GPAs), although up until now the timing and therefore exact substrate involved was unclear. Here, we present results combined from in vivo and in vitro studies that reveal the substrates for the halogenase enzymes from GPA biosynthesis as amino acid residues bound to(More)
Nonribosomal peptide synthetases (NRPSs) produce many important and structurally complex natural products. Because of their architectures, reprogramming NRPSs has long been attempted to access new bioactive compounds. However, detailed characterization of NRPS catalysis and substrate selectivity by adenylation (A) domains is needed to support such efforts.(More)
The biosynthesis of complex natural products by non-ribosomal peptide synthetases (NRPSs) and the related polyketide synthases (PKSs) represents a major source of important bioactive compounds. These large, multi-domain machineries are able to produce a fascinating range of molecules due to the nature of their modular architectures, which allows natural(More)
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