Bypassing the proline/thiazoline requirement of the macrocyclase PatG† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7cc06550g

نویسندگان

  • E. Oueis
  • H. Stevenson
  • M. Jaspars
  • N. J. Westwood
  • J. H. Naismith
چکیده

Biocatalysis is a fast developing field in which an enzyme's natural capabilities are harnessed or engineered for synthetic chemistry. The enzyme PatG is an extremely promiscuous macrocyclase enzyme tolerating both non-natural amino acids and non-amino acids within the substrate. It does, however, require a proline or thiazoline at the C-terminal position of the core peptide which means the final product must contain this group. Here, we show guided by structural insight we have identified two synthetic routes, triazole and a double cysteine, that circumvent this requirement. With the triazole, we show PatGmac can macrocyclise substrates that do not contain any amino acids in the final product.

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Watasemycin biosynthesis in Streptomyces venezuelae: thiazoline C-methylation by a type B radical-SAM methylase homologue† †Electronic supplementary information (ESI) available: Experimental procedures and additional tables, figures, chromatograms and results from biological assays. See DOI: 10.1039/c6sc03533g Click here for additional data file.

Department of Chemistry, University of War [email protected] Kitasato Institute for Life Sciences, Kitasato Tokyo, Japan Department of Molecular Microbiology, Joh E-mail: [email protected] † Electronic supplementary information ( and additional tables, gures, chromatogr See DOI: 10.1039/c6sc03533g ‡ These authors contributed equally. § Current address: Department of Bioeng Diego, USA. ...

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عنوان ژورنال:

دوره 53  شماره 

صفحات  -

تاریخ انتشار 2017