Bypassing the proline/thiazoline requirement of the macrocyclase PatG
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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.
Oueis , E , Stevenson , H , Jaspars , M , Westwood , N J & Naismith , J H 2017 , ' Bypassing the proline/thiazoline requirement of the macrocyclase PatG ' Chemical Communications , vol 53 , no. 91 , pp. 12274-12277 . DOI: 10.1039/C7CC06550G
© 2017 the Authors. Open Access Article. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
DescriptionThis work was supported by the European Research Council (339367), UK Biotechnology and Biological Sciences Research Council (K015508/1), the Wellcome Trust (TripleTOF 5600 mass spectrometer (094476), the MALDI TOF-TOF Analyser (079272AIA), 700 NMR) and the EPSRC UK National Mass Spectrometry Facility at Swansea University. J.H.N. is a Royal Society Wolfson Merit Award Holder and 1000 talent scholar at Sichuan University
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