Bypassing the proline/thiazoline requirement of the macrocyclase PatG
MetadataShow full item record
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.
This 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
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.