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  Cytochrome P450 OxyBtei catalyzes the first phenolic coupling step in teicoplanin biosynthesis

Haslinger, K., Maximowitsch, E., Brieke, C., Koch, A., & Cryle, M. (2014). Cytochrome P450 OxyBtei catalyzes the first phenolic coupling step in teicoplanin biosynthesis. ChemBioChem: A European Journal of Chemical Biology, 15(18), 2719-2728. doi:10.1002/cbic.201402441.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-D2C1-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-D2C2-C
Genre: Journal Article

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ChemBioChem_15_2014_2719.pdf (Any fulltext), 2MB
 
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 Creators:
Haslinger, Kristina1, Author              
Maximowitsch, Eglé1, Author              
Brieke, Clara1, Author              
Koch, Alexa1, 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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Free keywords: biocatalysis; cytochromes; peptide biosynthesis; secondary metabolism; teicoplanin
 Abstract: Bacterial cytochrome P450s form a remarkable clade of the P450 superfamily of oxidative hemoproteins, and are often involved in the biosynthesis of complex natural products. Those in a subgroup known as "Oxy enzymes" play a crucial role in the biosynthesis of glycopeptide antibiotics, including vancomycin and teicoplanin. The Oxy enzymes catalyze crosslinking of aromatic residues in the non-ribosomal antibiotic precursor peptide while it remains bound to the non-ribosomal peptide synthetase (NRPS); this crosslinking secures the three-dimensional structure of the glycopeptide, crucial for antibiotic activity. We have characterized OxyBtei , the first of the Oxy enzymes in teicoplanin biosynthesis. Our results reveal that OxyBtei possesses a structure similar to those of other Oxy proteins and is active in crosslinking NRPS-bound peptide substrates. However, OxyBtei displays a significantly altered activity spectrum against peptide substrates compared to its well-studied vancomycin homologue.

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Language(s): eng - English
 Dates: 2014-08-052014-10-302014-10-302014-12-15
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: Other: 8060
DOI: 10.1002/cbic.201402441
 Degree: -

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Title: ChemBioChem : A European Journal of Chemical Biology
  Other : ChemBioChem
Source Genre: Journal
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Publ. Info: Weinheim, Germany : Wiley-VCH
Pages: - Volume / Issue: 15 (18) Sequence Number: - Start / End Page: 2719 - 2728 Identifier: ISSN: 1439-4227
CoNE: https://pure.mpg.de/cone/journals/resource/110978984568897_1