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dc.contributor.authorMelo Czekster, Clarissa
dc.contributor.authorGe, Ying
dc.contributor.authorNaismith, James H.
dc.identifier.citationMelo Czekster , C , Ge , Y & Naismith , J H 2016 , ' Mechanisms of cyanobactin biosynthesis ' Current Opinion in Chemical Biology , vol. 35 , pp. 80-88 .
dc.identifier.otherPURE: 245863580
dc.identifier.otherPURE UUID: 071c79df-38b2-408a-8c57-b8875e14e75f
dc.identifier.otherRIS: urn:F35E16F446E75CE8826153B584516BD9
dc.identifier.otherScopus: 84988372916
dc.descriptionThis work was supported by the European Research Council (339367), UK Biotechnology and Biological Sciences Research Council (K015508/1).en
dc.description.abstractCyanobactins are a diverse collection of natural products that originate from short peptides made on a ribosome. The amino acids are modified in a series of transformations catalyzed by multiple enzymes. The patellamide pathway is the most well studied and characterized example. Here we review the structures and mechanisms of the enzymes that cleave peptide bonds, macrocyclise peptides, heterocyclise cysteine (as well as threonine and serine) residues, oxidize five-membered heterocycles and attach prenyl groups. Some enzymes operate by novel mechanisms which is of interest and in addition the enzymes uncouple recognition from catalysis. The normally tight relationship between these factors hinders biotechnology. The cyanobactin pathway may be particularly suitable for exploitation, with progress observed with in vivo and in vitro approaches.
dc.relation.ispartofCurrent Opinion in Chemical Biologyen
dc.rights© 2016 Published by Elsevier Ltd. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at
dc.subjectQD Chemistryen
dc.titleMechanisms of cyanobactin biosynthesisen
dc.typeJournal itemen
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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