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  Chlorinated glycopeptide antibiotic peptide precursors improve cytochrome P450-catalyzed cyclization cascade efficiency

Peschke, M., Brieke, C., Goode, R. J. A., Schittenhelm, R. B., & Cryle, M. (2017). Chlorinated glycopeptide antibiotic peptide precursors improve cytochrome P450-catalyzed cyclization cascade efficiency. Biochemistry, 56(9), 1239-1247. doi:10.1021/acs.biochem.6b01102.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-B6C4-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-B6C5-3
Genre: Journal Article

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 Creators:
Peschke, Madeleine1, Author              
Brieke, Clara1, Author              
Goode, Rob J. A., Author
Schittenhelm, Ralf B., Author
Cryle, Max1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: The activity of glycopeptide antibiotics (GPAs) depends upon important structural modifications to their precursor heptapeptide backbone: specifically, the cytochrome P450-catalyzed oxidative cross-linking of aromatic side chains as well as the halogenation of specific residues within the peptide. The timing of halogenation and its effect on the cyclization of the peptide are currently unclear. Our results show that chlorination of peptide precursors improves their processing by P450 enzymes in vitro, which provides support for GPA halogenation occurring prior to peptide cyclization during nonribosomal peptide synthesis. We could also determine that the activity of the second enzyme in the oxidative cyclization cascade, OxyA, remains higher for chlorinated peptide substrates even when the biosynthetic GPA product possesses an altered chlorination pattern, which supports the role of the chlorine atoms in orienting the peptide substrate in the active site of these enzymes.

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Language(s): eng - English
 Dates: 2017-02-162016-10-272017-02-202017-02-202017-03-07
 Publication Status: Published in print
 Pages: 9
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 Rev. Type: Peer
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 56 (9) Sequence Number: - Start / End Page: 1239 - 1247 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103