ArticleFEBS letters2012
Catalytic promiscuity of a bacterial α-N-methyltransferase.
Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Biosynthesis of 14-Membered Cyclopeptide Alkaloids via Nonheme Iron- and 2-Oxoglutarate-Dependent Oxidative Decarboxylation.Journal of the American Chemical Society · 2026Article
- Biosynthesis of 14-membered cyclopeptide alkaloids via non-heme-iron- and 2-oxoglutarate-dependent oxidative decarboxylation.bioRxiv : the preprint server for biology · 2026Article
- De novo design of ribosomally synthesized and post-translationally modified peptides.Nature chemistry · 2025Article
- Substrate Specificity of a Methyltransferase Involved in the Biosynthesis of the Lantibiotic Cacaoidin.Biochemistry · 2024Article
- Discovery and engineering of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products.RSC chemical biology · 2024Review
- Methyltransferases from RiPP pathways: shaping the landscape of natural product chemistry.Beilstein journal of organic chemistry · 2024Review
- Non-Native Site-Selective Enzyme Catalysis.Chemical reviews · 2023Review
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis.ACS chemical biology · 2018Article
- Substrate specificity of the cypemycin decarboxylase CypD.Synthetic and systems biotechnology · 2018Review
- Methyltransferases of gentamicin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Ribosomal Natural Products, Tailored To Fit.Accounts of chemical research · 2017Article
- Chimeric Leader Peptides for the Generation of Non-Natural Hybrid RiPP Products.ACS central science · 2017Article
- Methanobactin and the Link between Copper and Bacterial Methane Oxidation.Microbiology and molecular biology reviews : MMBR · 2016Review
- Biosynthetic investigation of phomopsins reveals a widespread pathway for ribosomal natural products in Ascomycetes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Insights into methyltransferase specificity and bioactivity of derivatives of the antibiotic plantazolicin.ACS chemical biology · 2015Article
- Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis.Journal of the American Chemical Society · 2014Article
- Synthesis of plantazolicin analogues enables dissection of ligand binding interactions of a highly selective methyltransferase.Organic letters · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The posttranslational methylation of N-terminal α-amino groups (α-N-methylation) is a ubiquitous reaction found in all domains of life. Although this modification usually occurs on protein substrates, recent studies have shown that it also takes place on ribosomally synthesized natural products. Here we report an investigation of the bacterial α-N-methyltransferase CypM involved in the biosynthesis of the peptide antibiotic cypemycin. We demonstrate that CypM has low substrate selectivity and methylates a variety of oligopeptides, cyclic peptides such as nisin and haloduracin, and the ε-amino group of lysine. Hence it may have potential for enzyme engineering and combinatorial biosynthesis. Bayesian phylogenetic inference of bacterial α-N-methyltransferases suggests that they have not evolved as a specific group based on the chemical transformations they catalyze, but that they have been acquired from various other methyltransferase classes during evolution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.