ArticlePloS one2017
Crystal Structure and Catalytic Mechanism of CouO, a Versatile C-Methyltransferase from Streptomyces rishiriensis.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Deciphering the Function and Structure of PA1216 as an S-Adenosyl-l-Methionine Binding Protein Using Differential Scanning Fluorimetry and Circular Dichroism.Protein science : a publication of the Protein Society · 2026Article
- S-Adenosyl-d-Methionine as a Non-Physiological Substrate for a Wide Range of SAM-Dependent Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- Context-Dependent Chemoselectivity of Aromatic C-Methyltransferases.Chembiochem : a European journal of chemical biology · 2026Article
- Utilizing a cell-free protein synthesis platform for the biosynthesis of a natural product, caffeine.Synthetic biology (Oxford, England) · 2023Article
- Biocatalytic Friedel-Crafts Reactions.ChemCatChem · 2022Review
- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
- Diversity of the reaction mechanisms of SAM-dependent enzymes.Acta pharmaceutica Sinica. B · 2021Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Friedel-Crafts alkylation of aromatic systems is a classic reaction in organic chemistry, for which regiospecific mono-alkylation, however, is generally difficult to achieve. In nature, methyltransferases catalyze the addition of methyl groups to a wide range of biomolecules thereby modulating the physico-chemical properties of these compounds. Specifically, S-adenosyl-L-methionine dependent C-methyltransferases possess a high potential to serve as biocatalysts in environmentally benign organic syntheses. Here, we report on the high resolution crystal structure of CouO, a C-methyltransferase from Streptomyces rishiriensis involved in the biosynthesis of the antibiotic coumermycin A1. Through molecular docking calculations, site-directed mutagenesis and the comparison with homologous enzymes we identified His120 and Arg121 as key functional residues for the enzymatic activity of this group of C-methyltransferases. The elucidation of the atomic structure and the insight into the catalytic mechanism provide the basis for the (semi)-rational engineering of the enzyme in order to increase the substrate scope as well as to facilitate the acceptance of SAM-analogues as alternative cofactors.
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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.