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  Facile synthetic access to glycopeptide antibiotic precursor peptides for the investigation of cytochrome P450 action in glycopeptide antibiotic biosynthesis

Brieke, C., Kratzig, V., Peschke, M., & Cryle, M. J. (2016). Facile synthetic access to glycopeptide antibiotic precursor peptides for the investigation of cytochrome P450 action in glycopeptide antibiotic biosynthesis. In Nonribosomal Peptide and Polyketide Biosynthesis (pp. 85-102). New York: Springer.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-22F1-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-3AB6-0
Genre: Book Chapter

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MethMolBiol_1401_2016_85.pdf (Any fulltext), 648KB
 
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 Creators:
Brieke, Clara1, Author              
Kratzig, Veronika1, Author              
Peschke, Madeleine1, Author              
Cryle, Max J.1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Glycopeptide antibiotics Solid phase peptide synthesis Coenzyme A Bio-conjugation Nonribosomal peptide synthetase Cytochrome P450
 Abstract: The glycopeptide antibiotics are an important class of complex, medically relevant peptide natural products. Given that the production of such compounds all stems from in vivo biosynthesis, understanding the mechanisms of the natural assembly system—consisting of a nonribosomal-peptide synthetase machinery (NRPS) and further modifying enzymes—is vital. In order to address the later steps of peptide biosynthesis, which are catalyzed by Cytochrome P450s that interact with the peptide-producing nonribosomal peptide synthetase, peptide substrates are required: these peptides must also be in a form that can be conjugated to carrier protein domains of the nonribosomal peptide synthetase machinery. Here, we describe a practical and effective route for the solid phase synthesis of glycopeptide antibiotic precursor peptides as their Coenzyme A (CoA) conjugates to allow enzymatic conjugation to carrier protein domains. This route utilizes Fmoc-chemistry suppressing epimerization of racemization-prone aryl glycine derivatives and affords high yields and excellent purities, requiring only a single step of simple solid phase extraction for chromatographic purification. With this, comprehensive investigations of interactions between various NRPS-bound substrates and Cytochrome P450s are enabled.

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Language(s): eng - English
 Dates: 2016-02-02
 Publication Status: Published in print
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Nonribosomal Peptide and Polyketide Biosynthesis
Source Genre: Book
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Publ. Info: New York : Springer
Pages: - Volume / Issue: 1401 Sequence Number: - Start / End Page: 85 - 102 Identifier: ISBN: 978-1-4939-3373-0

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Title: Methods in Molecular Biology:
Source Genre: Series
 Creator(s):
Evans, Bradley S., Editor
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Publ. Info: Springer
Pages: - Volume / Issue: 1401 Sequence Number: - Start / End Page: 85 - 102 Identifier: ISSN: 1064-3745