Title: Two Functionally Redundant Sfp‐Type 4′‐Phosphopantetheinyl Transferases Differentially Activate Biosynthetic Pathways in <i>Myxococcus xanthus</i>
Abstract: ChemBioChemVolume 9, Issue 10 p. 1549-1553 Communication Two Functionally Redundant Sfp-Type 4′-Phosphopantetheinyl Transferases Differentially Activate Biosynthetic Pathways in Myxococcus xanthus Peter Meiser, Peter Meiser Institut für Pharmazeutische Biotechnologie, Universität des Saarlandes, P. O. Box 151150, 66041 Saarbrücken (Germany), Fax: (+49) 681-3025473Search for more papers by this authorRolf Müller Prof. Dr., Rolf Müller Prof. Dr. [email protected] Institut für Pharmazeutische Biotechnologie, Universität des Saarlandes, P. O. Box 151150, 66041 Saarbrücken (Germany), Fax: (+49) 681-3025473Search for more papers by this author Peter Meiser, Peter Meiser Institut für Pharmazeutische Biotechnologie, Universität des Saarlandes, P. O. Box 151150, 66041 Saarbrücken (Germany), Fax: (+49) 681-3025473Search for more papers by this authorRolf Müller Prof. Dr., Rolf Müller Prof. Dr. [email protected] Institut für Pharmazeutische Biotechnologie, Universität des Saarlandes, P. O. Box 151150, 66041 Saarbrücken (Germany), Fax: (+49) 681-3025473Search for more papers by this author First published: 23 June 2008 https://doi.org/10.1002/cbic.200800077Citations: 24Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Graphical Abstract A liberal alliance. Two Sfp-type 4′-phosphopantetheinyl transferases (PPTases, MxPpt1 and MxPpt2) are encoded in the Myxococcus xanthus DK1622 genome. Disruption or over-expression led to significant changes in secondary metabolism, but production of known compounds was not abolished. Both PPTases thus apparently differ in their specificity for biosynthetic pathways by employing carrier proteins from polyketide synthases and nonribosomal peptide synthetases. Supporting Information Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2268/2008/z800077_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article. References 1R. H. Lambalot, A. M. Gehring, R. S. Flugel, P. Zuber, M. LaCelle, M. A. Marahiel, R. Reid, C. Khosla, C. T. Walsh, Chem. 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Publication Year: 2008
Publication Date: 2008-06-23
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 25
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