The biosynthesis of albicidins
Albicidins, produced by the sugarcane pathogenic bacterium Xanthomonas albilineans, are potent inhibitors of the bacterial DNA gyrase with Ic50values in nM ranges [1].The structure of albicidins remained unclear for more than three decades after their first description by Birch et al. [2]. After the identification and sequencing of three gene islands, responsible for the albicidin biosynthesis, a PKS-NRPS hybrid, build up by three enzymes, Alb01, Alb05and Alb09 was proposed for the albicidin assembly [3, 4].Most recently we were able to solve the hitherto unknown structure of the main albicidin [5,6] and post NRPS modified derivatives, revealing a unique polyaromatic oligopeptide mainly composed of p-amino benzoic acids. Our in-vitro studies of the non-ribosomal albicidin assembly line and tailoring enzymes provide detailed insights into the biosynthetic machinery of albicidins. Together with our bioinformatic investigations we are able to propose a comprehensive biochemical assembly, expanding the non-ribosomal code of adenylation domains with p-amino benzoic acid derivatives. Furthermore our study revealed a new type of dehydratase domain responsible for the in situ formation and incorporation of cyano-alanine [6]. (Texte intégral)
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dig-cirad-fr-5791482016-02-26T13:53:36Z http://agritrop.cirad.fr/579148/ http://agritrop.cirad.fr/579148/ The biosynthesis of albicidins. Petras Daniel, Hempel Benjamin, Kerwat Dennis, Mainz Andi, Cociancich Stéphane, Royer Monique, Süssmuth Roderich. 2015. . Francfort : DECHEMA, Résumé, 1 p. European Conference on Natural Products. 2, Francfort, Allemagne, 6 Septembre 2015/9 Septembre 2015.http://www.dechema.de/en/ECNP2015.html <http://www.dechema.de/en/ECNP2015.html> Researchers The biosynthesis of albicidins Petras, Daniel Hempel, Benjamin Kerwat, Dennis Mainz, Andi Cociancich, Stéphane Royer, Monique Süssmuth, Roderich eng 2015 DECHEMA H20 - Maladies des plantes Albicidins, produced by the sugarcane pathogenic bacterium Xanthomonas albilineans, are potent inhibitors of the bacterial DNA gyrase with Ic50values in nM ranges [1].The structure of albicidins remained unclear for more than three decades after their first description by Birch et al. [2]. After the identification and sequencing of three gene islands, responsible for the albicidin biosynthesis, a PKS-NRPS hybrid, build up by three enzymes, Alb01, Alb05and Alb09 was proposed for the albicidin assembly [3, 4].Most recently we were able to solve the hitherto unknown structure of the main albicidin [5,6] and post NRPS modified derivatives, revealing a unique polyaromatic oligopeptide mainly composed of p-amino benzoic acids. Our in-vitro studies of the non-ribosomal albicidin assembly line and tailoring enzymes provide detailed insights into the biosynthetic machinery of albicidins. Together with our bioinformatic investigations we are able to propose a comprehensive biochemical assembly, expanding the non-ribosomal code of adenylation domains with p-amino benzoic acid derivatives. Furthermore our study revealed a new type of dehydratase domain responsible for the in situ formation and incorporation of cyano-alanine [6]. (Texte intégral) conference_item info:eu-repo/semantics/conferenceObject Conference info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/579148/9/comm_579148.pdf text Cirad license info:eu-repo/semantics/restrictedAccess https://agritrop.cirad.fr/mention_legale.html http://www.dechema.de/en/ECNP2015.html info:eu-repo/semantics/altIdentifier/purl/http://www.dechema.de/en/ECNP2015.html |
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H20 - Maladies des plantes H20 - Maladies des plantes Petras, Daniel Hempel, Benjamin Kerwat, Dennis Mainz, Andi Cociancich, Stéphane Royer, Monique Süssmuth, Roderich The biosynthesis of albicidins |
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Albicidins, produced by the sugarcane pathogenic bacterium Xanthomonas albilineans, are potent inhibitors of the bacterial DNA gyrase with Ic50values in nM ranges [1].The structure of albicidins remained unclear for more than three decades after their first description by Birch et al. [2]. After the identification and sequencing of three gene islands, responsible for the albicidin biosynthesis, a PKS-NRPS hybrid, build up by three enzymes, Alb01, Alb05and Alb09 was proposed for the albicidin assembly [3, 4].Most recently we were able to solve the hitherto unknown structure of the main albicidin [5,6] and post NRPS modified derivatives, revealing a unique polyaromatic oligopeptide mainly composed of p-amino benzoic acids. Our in-vitro studies of the non-ribosomal albicidin assembly line and tailoring enzymes provide detailed insights into the biosynthetic machinery of albicidins. Together with our bioinformatic investigations we are able to propose a comprehensive biochemical assembly, expanding the non-ribosomal code of adenylation domains with p-amino benzoic acid derivatives. Furthermore our study revealed a new type of dehydratase domain responsible for the in situ formation and incorporation of cyano-alanine [6]. (Texte intégral) |
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conference_item |
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H20 - Maladies des plantes |
author |
Petras, Daniel Hempel, Benjamin Kerwat, Dennis Mainz, Andi Cociancich, Stéphane Royer, Monique Süssmuth, Roderich |
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Petras, Daniel Hempel, Benjamin Kerwat, Dennis Mainz, Andi Cociancich, Stéphane Royer, Monique Süssmuth, Roderich |
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Petras, Daniel |
title |
The biosynthesis of albicidins |
title_short |
The biosynthesis of albicidins |
title_full |
The biosynthesis of albicidins |
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The biosynthesis of albicidins |
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The biosynthesis of albicidins |
title_sort |
biosynthesis of albicidins |
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DECHEMA |
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http://agritrop.cirad.fr/579148/ http://agritrop.cirad.fr/579148/9/comm_579148.pdf |
work_keys_str_mv |
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