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dc.contributor.authorHong, Huien
dc.contributor.authorSamborsky, Markiyanen
dc.contributor.authorLindner, Fredericken
dc.contributor.authorLeadlay, Peteren
dc.date.accessioned2015-11-04T17:19:56Z
dc.date.available2015-11-04T17:19:56Z
dc.date.issued2015-12-02en
dc.identifier.citationHong et al. Angewandte Chemie International Edition (2015) Vol. 55, pp. 1118-1123. doi:10.1002/anie.201509300en
dc.identifier.issn1433-7851
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/252521
dc.description.abstractDesertomycin A is an aminopolyol polyketide containing a macrolactone ring. We have proposed that desertomycin A and similar compounds (marginolactones) are formed by polyketide synthases primed not with gamma-aminobutanoyl-CoA but with 4- guanidinylbutanoyl-CoA, to avoid facile cyclization of the starter unit. This hypothesis requires that there be final-stage de-amidination of the corresponding guanidino-substituted natural product, but no such enzyme has been described. We have now identified candidate amidinohydrolase genes within the desertomycin and primycin clusters. Deletion of the putative desertomycin amidinohydrolase gene dstH in Streptomyces macronensis led to accumulation of desertomycin B, the guanidino- form of the antibiotic. Also, purified DstH efficiently catalyzed the in vitro conversion of desertomycin B into the A form. Hence this amidinohydrolase furnishes the missing link in the proposal of a naturally-evolved example of protective group chemistry
dc.description.sponsorshipWe gratefully acknowledge BBSRC (project grants BB/J007250/1 and BB/K002341/1 to P.F.L.), Shilo Dickens and colleagues (Nextgen Sequencing Facility, Department of Biochemistry, University of Cambridge) for help with genome sequencing, and Prof. Dr. Wolfgang Wohlleben, University of Tübingen, for the gift of Streptomyces olivaceus Tü4018. P.F.L. is an International Research Awardee of the Alexander von Humboldt Foundation.
dc.languageEnglishen
dc.language.isoenen
dc.publisherWiley
dc.rightsCreative Commons Attribution 4.0 International License
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.titleA novel amidinohydrolase provides the missing link in biosynthesis of amino-marginolactone antibiotics*en
dc.typeArticle
dc.description.versionThis is the final version of the article. It was first available from Wiley via http://dx.doi.org/10.1002/anie.201509300en
prism.endingPage1123
prism.publicationDate2015en
prism.publicationNameAngewandte Chemie International Editionen
prism.startingPage1118
prism.volume55en
dc.rioxxterms.funderBBSRC
dc.rioxxterms.projectidBB/J007250/1
dc.rioxxterms.projectidBB/K002341/1
rioxxterms.versionofrecord10.1002/anie.201509300en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-12-02en
dc.contributor.orcidLeadlay, Peter [0000-0002-3247-509X]
dc.identifier.eissn1521-3773
rioxxterms.typeJournal Article/Reviewen


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Except where otherwise noted, this item's licence is described as Creative Commons Attribution 4.0 International License