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Engineering of a peptide α-N-methyltransferase to methylate non-proteinogenic amino acids
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dc.contributor.author | Song, Haigang | |
dc.contributor.author | Burton, Antony J. | |
dc.contributor.author | Shirran, Sally L. | |
dc.contributor.author | Fahrig-Kamarauskaitė, Jūratė | |
dc.contributor.author | Kaspar, Hannelore | |
dc.contributor.author | Muir, Tom W. | |
dc.contributor.author | Künzler, Markus | |
dc.contributor.author | Naismith, James H. | |
dc.date.accessioned | 2021-05-18T15:30:01Z | |
dc.date.available | 2021-05-18T15:30:01Z | |
dc.date.issued | 2021-04-15 | |
dc.identifier | 273831370 | |
dc.identifier | eec6ec6b-4936-4369-8061-4abc04933843 | |
dc.identifier | 85105794574 | |
dc.identifier | 000651092700001 | |
dc.identifier.citation | Song , H , Burton , A J , Shirran , S L , Fahrig-Kamarauskaitė , J , Kaspar , H , Muir , T W , Künzler , M & Naismith , J H 2021 , ' Engineering of a peptide α-N-methyltransferase to methylate non-proteinogenic amino acids ' , Angewandte Chemie International Edition , vol. Early View . https://doi.org/10.1002/anie.202100818 | en |
dc.identifier.issn | 1433-7851 | |
dc.identifier.other | RIS: urn:1C894111AFD79DE29EA08215DE2EFDBB | |
dc.identifier.other | ORCID: /0000-0003-3516-3507/work/94291571 | |
dc.identifier.uri | https://hdl.handle.net/10023/23217 | |
dc.description | Funding: This work was supported by grants to M.K. (CTI/Innosuisse 25951.2) and J.H.N. (BBSRC BB/R018189/1 and ERC 339367). A.J.B. isa Damon Runyon Fellow of the Damon Runyon Cancer Research Foundation (DRG-2283-17). | en |
dc.description.abstract | Introduction of α-N-methylated non-proteinogenic amino acids into peptides can improve their biological activities, membrane permeability and proteolytic stability. This is commonly achieved, in nature and in the lab, by assembling pre-methylated amino acids. The more appealing route of methylating amide bonds is challenging. Biology has evolved an α-N-automethylating enzyme, OphMA, which acts on the amide bonds of peptides fused to its C-terminus. Due to the ribosomal biosynthesis of its substrate, the activity of this enzyme towards peptides with non-proteinogenic amino acids has not been addressed. An engineered OphMA, intein-mediated protein ligation and solid-phase peptide synthesis have allowed us to demonstrate the methylation of amide bonds in the context of non-natural amides. This approach may have application in the biotechnological production of therapeutic peptides. | |
dc.format.extent | 6 | |
dc.format.extent | 1826355 | |
dc.language.iso | eng | |
dc.relation.ispartof | Angewandte Chemie International Edition | en |
dc.subject | Cyclic peptide | en |
dc.subject | RiPPs | en |
dc.subject | α-N-methylation | en |
dc.subject | Non-proteinogenic amino acids | en |
dc.subject | Split intein | en |
dc.subject | QD Chemistry | en |
dc.subject | T-NDAS | en |
dc.subject.lcc | QD | en |
dc.title | Engineering of a peptide α-N-methyltransferase to methylate non-proteinogenic amino acids | en |
dc.type | Journal article | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.1002/anie.202100818 | |
dc.description.status | Peer reviewed | en |
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