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  Rapid access to glycopeptide antibiotic precursor peptides coupled with cytochrome P450-mediated catalysis: towards a biomimetic synthesis of glycopeptide antibiotics

Brieke, C., Kratzig, V., Haslinger, K., Winkler, A., & Cryle, M. (2015). Rapid access to glycopeptide antibiotic precursor peptides coupled with cytochrome P450-mediated catalysis: towards a biomimetic synthesis of glycopeptide antibiotics. Organic & Biomolecular Chemistry, 13(7), 2012-2021. doi:10.1039/c4ob02452d.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-D2BA-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-A15E-C
Genre: Journal Article

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Brieke, Clara1, Author              
Kratzig, Veronika1, Author              
Haslinger, Kristina1, Author              
Winkler, Andreas1, Author              
Cryle, Max1, 2, 3, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Cytochrome P450, Max Planck Institute for Medical Research, Max Planck Society, Jahnstrasse 29, 69120 Heidelberg, DE, ou_1497697              
3Heme and Flavin Enzymes, Max Planck Institute for Medical Research, Max Planck Society, Jahnstrasse 29, 69120 Heidelberg, DE, ou_1497715              

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 Abstract: Understanding the mechanisms underpinning glycopeptide antibiotic biosynthesis is key to the future ability to reinvent these compounds. For effective in vitro characterization of the crucial later steps of the biosynthesis, facile access to a wide range of substrate peptides as their Coenzyme A (CoA) conjugates is essential. Here we report the development of a rapid route to glycopeptide precursor CoA conjugates that affords both high yields and excellent purities. This synthesis route is applicable to the synthesis of peptide CoA-conjugates containing racemization-prone arylglycine residues: such residues are hallmarks of non-ribosomal peptide synthesis and have previously been inaccessible to peptide synthesis using Fmoc-type chemistry. We have applied this route to generate glycopeptide precursor peptides in their carrier protein-bound form as substrates to explore the specificity of the first oxygenase enzyme from vancomycin biosynthesis (OxyBvan). Our results indicate that OxyBvan is a highly promiscuous catalyst for phenolic coupling of diverse glycopeptide precursors that accepts multiple carrier protein substrates, even on carrier protein domains from alternate glycopeptide biosynthetic machineries. These results represent the first important steps in the development of an in vitro biomimetic synthesis of modified glycopeptide aglycones

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Language(s): eng - English
 Dates: 2014-11-212014-12-032015-02-04
 Publication Status: Published in print
 Pages: 10
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 Rev. Type: Peer
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Title: Organic & Biomolecular Chemistry
  Other : Organic and Biomolecular Chemistry
  Abbreviation : Org. Biomol. Chem.
Source Genre: Journal
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Publ. Info: Cambridge : Royal Society of Chemistry
Pages: - Volume / Issue: 13 (7) Sequence Number: - Start / End Page: 2012 - 2021 Identifier: ISSN: 1477-0520
CoNE: https://pure.mpg.de/cone/journals/resource/954925269322