Albicidin
Feglymycin
Class II Lanthipeptides
Class III Lanthipeptides
CDPs
Paenilamicin
Abyssomicin
Salmochelin
Skyllamycin
MembraTech



Cyclodepsipeptides (CDPs)

 


Coworkers: Dr. Agnes Mühlenweg, Annette Poch, Charlotte Steiniger, Simon Boecker

Keywords: Nonribosomal peptide synthetases, Cyclodepsipeptides, protein engineering, combinatorial biosynthesis, chemoenzymatics

Cooperation: Prof. Vera Meyer, TU Berlin


 

 



Nonribosomal peptide synthetases (NRPS) gained from bacteria and fungi are multifunctional enzymes with a large product diversity of pharmacological relevant peptides. These Enzymes contain different modules, which catalyze the activation of their specific substrates, such as amino acids and hydroxy acids, respectively. In some enzymes the substrate specificity is expanded (Müller et al. (2009); Feifel et al. (2007)). The modules consist of at least a minimum of three domains responsible for condensation, activation and thiolation (CAT). These domain complexes are optional expandable (e.g. epimerisation, N-methylation) and exchangeable. This leads to a high variability of synthesized products as a result of just one enzyme complex. The wide range of therapeutic uses comprises antibiotic, anticancer and immunosuppressive effects. Classic clinical applications are Cyclosporin (immunosuppressant), Vancomycin („antibiotic of the last resort“) and one example of the work in our group is the insecticide Enniatin B. Recently, we were able to establish different heterologous hosts for the production of Enniatin B: Aspergillus niger is able to produce Enniatin B in high amounts (up to 4.5 g/L) (Richter et al. (2014)), whereas Bacillus subtilis secretes the product to the medium (Zobel et al. (2014)).