ArticleThe Plant cell2010
Structure-function analyses of a caffeic acid O-methyltransferase from perennial ryegrass reveal the molecular basis for substrate preference.
Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 106 citations in OpenAlex.
- Structural insights into a dual-substrate O-methyltransferase reveal the enzymatic mechanism of parallel paeonol biosynthesis.Nature communications · 2026Article
- Integrated Metabolomics and Transcriptomics Provided Novel Insights into the Biosynthetic Regulation of Phenolic Compounds inFoods (Basel, Switzerland) · 2026Article
- Structural Elucidation and Engineering of the (S)-scoulerine 2-O-Methyltransferase Enabling Regioselective Epiberberine Biosynthesis in Coptis chinensis.Plant biotechnology journal · 2026Article
- Cell-Free Synthesis of Cannabistilbene I: A Dual Acting Anti-Inflammatory fromJournal of natural products · 2026Article
- Structural dynamics of the π-stacking network governing cofactor-substrate cooperativity of SbSOMT methyltransferase.Communications chemistry · 2026Article
- Structure-Guided Engineering of a Promiscuous O-Methyltransferase for a SAM Regeneration Biocatalysis Platform of Methylated Pharmaceuticals.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Comparative Genomic Analysis of COMT Family Genes in ThreePlants (Basel, Switzerland) · 2025Article
- How to Tell an N from an O: Controlling the Chemoselectivity of Methyltransferases.ACS catalysis · 2025Article
- Nutritional enhancement of animal feed and forage crops via genetic modification.Journal of the Royal Society of New Zealand · 2025Review
- Comparative transcriptome analysis provides novel insights into the seed germination of Panax japonicus, an endangered species in China.BMC plant biology · 2024Article
- Beyond pathways: Accelerated flavonoids candidate identification and novel exploration of enzymatic properties using combined mapping populations of wheat.Plant biotechnology journal · 2024Article
- Genome assembly ofFrontiers in plant science · 2024Article
- Structure of methyltransferase RedM that forms the dimethylpyrrolinium of the bisindole reductasporine.The Journal of biological chemistry · 2024Article
- Exogenous Methyl Jasmonate Mediated MiRNA-mRNA Network Improves Heat Tolerance of Perennial Ryegrass.International journal of molecular sciences · 2023Article
- Regioselective stilbene O-methylations in Saccharinae grasses.Nature communications · 2023Article
- Engineering of flavonoid 3'-O-methyltransferase for improved biosynthesis of chrysoeriol in Escherichia coli.Applied microbiology and biotechnology · 2023Article
- Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.Molecules (Basel, Switzerland) · 2022Review
- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
- Identification and Functional Analysis of the Caffeic Acid O-Methyltransferase (COMT) Gene Family in Rice (International journal of molecular sciences · 2022Article
- Molecular Characterisation of FlavanoneInternational journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lignin forms from the polymerization of phenylpropanoid-derived building blocks (the monolignols), whose modification through hydroxylation and O-methylation modulates the chemical and physical properties of the lignin polymer. The enzyme caffeic acid O-methyltransferase (COMT) is central to lignin biosynthesis. It is often targeted in attempts to engineer the lignin composition of transgenic plants for improved forage digestibility, pulping efficiency, or utility in biofuel production. Despite intensive investigation, the structural determinants of the regiospecificity and substrate selectivity of COMT remain poorly defined. Reported here are x-ray crystallographic structures of perennial ryegrass (Lolium perenne) COMT (Lp OMT1) in open conformational state, apo- and holoenzyme forms and, most significantly, in a closed conformational state complexed with the products S-adenosyl-L-homocysteine and sinapaldehyde. The product-bound complex reveals the post-methyl-transfer organization of COMT's catalytic groups with reactant molecules and the fully formed phenolic-ligand binding site. The core scaffold of the phenolic ligand forges a hydrogen-bonding network involving the 4-hydroxy group that anchors the aromatic ring and thereby permits only metahydroxyl groups to be positioned for transmethylation. While distal from the site of transmethylation, the propanoid tail substituent governs the kinetic preference of ryegrass COMT for aldehydes over alcohols and acids due to a single hydrogen bond donor for the C9 oxygenated moiety dictating the preference for an aldehyde.
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