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dc.contributor.authorKoehnke, Jesko Alexander Johannes Gunter
dc.contributor.authorBent, Andrew Frank
dc.contributor.authorHoussen, Wael E.
dc.contributor.authorMann, Greg
dc.contributor.authorJaspars, Marcel
dc.contributor.authorNaismith, Jim
dc.identifier.citationKoehnke , J A J G , Bent , A F , Houssen , W E , Mann , G , Jaspars , M & Naismith , J 2014 , ' The structural biology of patellamide biosynthesis ' , Current Opinion in Structural Biology , vol. 29 , pp. 112-121 .
dc.identifier.otherPURE: 158298025
dc.identifier.otherPURE UUID: 8c499744-bf70-4176-a983-3dbc15e24b64
dc.identifier.otherWOS: 000348016600016
dc.identifier.otherScopus: 84911940597
dc.descriptionThis work was supported by grants from the ERC339367 (JHN and MJ) and BBSRCBB/K015508/1 (JHN and MJ).en
dc.description.abstractThe biosynthetic pathways for patellamide and related natural products have recently been studied by structural biology. These pathways produce molecules that have a complex framework and exhibit a diverse array of activity due to the variability of the amino acids that are found in them. As these molecules are difficult to synthesize chemically, exploitation of their properties has been modest. The patellamide pathway involves amino acid heterocyclization, peptide cleavage, peptide macrocyclization, heterocycle oxidation and epimerization; closely related products are also prenylated. Enzyme activities have been identified for all these transformations except epimerization, which may be spontaneous. This review highlights the recent structural and mechanistic work on amino acid heterocyclization, peptide cleavage and peptide macrocyclization. This work should help in using the enzymes to produce novel analogs of the natural products enabling an exploitation of their properties.
dc.relation.ispartofCurrent Opinion in Structural Biologyen
dc.rights© 2014 Published by Elsevier Ltd. Open access under CC BY license (
dc.subjectQD Chemistryen
dc.titleThe structural biology of patellamide biosynthesisen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.description.statusPeer revieweden

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