ArticleAngewandte Chemie (International ed. in English)2021
Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Expanding the genetic code: phage-driven evolution of pyrrolysyl-synthetase for site-specific incorporation of synthetic phenylalanine and tyrosine derivatives.Frontiers in molecular biosciences · 2026Article
- α-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.Protein science : a publication of the Protein Society · 2025Article
- Genome Mining and Biological Engineering of Type III Borosins from Bacteria.International journal of molecular sciences · 2024Article
- Methyltransferases from RiPP pathways: shaping the landscape of natural product chemistry.Beilstein journal of organic chemistry · 2024Review
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Bioconjugate Platform for Iterative BackboneACS catalysis · 2022Article
- Applying Promiscuous RiPP Enzymes to Peptide BackboneACS chemical biology · 2022Article
- Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids.Angewandte Chemie (International ed. in English) · 2021Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
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.
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Registered trials
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