ArticleScientific reports2018
Identification of a unique Radical SAM methyltransferase required for the sp
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 48 citations in OpenAlex.
- Substrate-driven phage community structure and phage-host dynamics in anaerobic digesters.Environmental microbiome · 2026Article
- Insights into the stereochemical mechanism of the BCommunications biology · 2026Article
- Novel chemistry and structural perspectives in vitamin BChemical science · 2026Review
- Atomic resolution structures of the methane-activating enzyme in anaerobic methanotrophy reveal extensive post-translational modifications.Nature communications · 2025Article
- Radical Fluoromethylation Enabled by Cobalamin-Dependent Radical SAM Enzymes.ACS bio & med chem Au · 2025Article
- Article
- Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024Article
- Physiological and transcriptomic response to methyl-coenzyme M reductase limitation inApplied and environmental microbiology · 2024Article
- Genomic remnants of ancestral methanogenesis and hydrogenotrophy in Archaea drive anaerobic carbon cycling.Science advances · 2022Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (Basel, Switzerland) · 2022Review
- Expression of divergent methyl/alkyl coenzyme M reductases from uncultured archaea.Communications biology · 2022Article
- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- A Cobalamin-Dependent Radical SAM Enzyme Catalyzes the Unique CAngewandte Chemie (International ed. in English) · 2022Article
- A Structural View of Alkyl-Coenzyme M Reductases, the First Step of Alkane Anaerobic Oxidation Catalyzed by Archaea.Biochemistry · 2022Review
- The Atypical Cobalamin-DependentJournal of the American Chemical Society · 2022Article
- Crystallographic snapshots of a BNature · 2022Article
- Overview of Diverse Methyl/Alkyl-Coenzyme M Reductases and Considerations for Their Potential Heterologous Expression.Frontiers in microbiology · 2022Review
- Overall Retention of Methyl Stereochemistry during BBiochemistry · 2021Article
- Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications.Microorganisms · 2021Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biological formation of methane (methanogenesis) is a globally important process, which is exploited in biogas technology, but also contributes to global warming through the release of a potent greenhouse gas into the atmosphere. The last and methane-releasing step of methanogenesis is catalysed by the enzyme methyl-coenzyme M reductase (MCR), which carries several exceptional posttranslational amino acid modifications. Among these, a 5-C-(S)-methylarginine is located close to the active site of the enzyme. Here, we show that a unique Radical S-adenosyl-L-methionine (SAM) methyltransferase is required for the methylation of the arginine residue. The gene encoding the methyltransferase is currently annotated as "methanogenesis marker 10" whose function was unknown until now. The deletion of the methyltransferase gene ma4551 in Methanosarcina acetivorans WWM1 leads to the production of an active MCR lacking the C-5-methylation of the respective arginine residue. The growth behaviour of the corresponding M. acetivorans mutant strain and the biophysical characterization of the isolated MCR indicate that the methylated arginine is important for MCR stability under stress conditions.
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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.