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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons117984

Haslinger,  Kristina
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons117805

Maximowitsch,  Eglé
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons117956

Brieke,  Clara
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons117807

Koch,  Alexa
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons92561

Cryle,  Max
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-D2C1-E
Zusammenfassung
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.