ArticleThe Plant cell2002
Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase.
Article in The Plant cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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Who cites it
96 citing papers in PubMed, 243 citations in OpenAlex.
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- Structural insights into a dual-substrate O-methyltransferase reveal the enzymatic mechanism of parallel paeonol biosynthesis.Nature communications · 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
- Integrated analysis of transcriptome and metabolome reveals the mechanism of lignin biosynthesis in fruit abscission of Chinese bayberry (Myrica rubra).BMC plant biology · 2025Article
- Developing a highly efficient whole-cell biotransformation of 3,4-dihydroxyacetophenone into Apocynin by engineered Escherichia coli expressing caffeic acid O-methyltransferase.World journal of microbiology & biotechnology · 2025Article
- How to Tell an N from an O: Controlling the Chemoselectivity of Methyltransferases.ACS catalysis · 2025Article
- Cloning and bioinformatics analysis of key gene ShOMT3 of podophyllotoxin biosynthesis pathway in Sinopodophyllum hexandrum.PloS one · 2025Article
- Identification of GiOMT gene family in Glycyrrhiza inflata bat and expression analysis under UV-B stresses.BMC genomics · 2024Article
- Lr34/Yr18/Sr57/Pm38 confers broad-spectrum resistance to fungal diseases via sinapyl alcohol transport for cell wall lignification in wheat.Plant communications · 2024Article
- Systematic Identification and Characterization ofInternational journal of molecular sciences · 2024Article
- Methylation Modification in Ornamental Plants: Impact on Floral Aroma and Color.International journal of molecular sciences · 2024Review
- Beyond pathways: Accelerated flavonoids candidate identification and novel exploration of enzymatic properties using combined mapping populations of wheat.Plant biotechnology journal · 2024Article
- Structure of methyltransferase RedM that forms the dimethylpyrrolinium of the bisindole reductasporine.The Journal of biological chemistry · 2024Article
- Article
- 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
- Article
- Lignocellulose molecular assembly and deconstruction properties of lignin-altered rice mutants.Plant physiology · 2023Article
- Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.Molecules (Basel, Switzerland) · 2022Review
- Identification and Functional Analysis of the Caffeic Acid O-Methyltransferase (COMT) Gene Family in Rice (International journal of molecular sciences · 2022Article
36 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase (COMT) from alfalfa is an S-adenosyl-L-Met-dependent O-methyltransferase involved in lignin biosynthesis. COMT methylates caffeoyl- and 5-hydroxyferuloyl-containing acids, aldehydes, and alcohols in vitro while displaying a kinetic preference for the alcohols and aldehydes over the free acids. The 2.2-A crystal structure of COMT in complex with S-adenosyl-L-homocysteine (SAH) and ferulic acid (ferulate form), as well as the 2.4-A crystal structure of COMT in complex with SAH and 5-hydroxyconiferaldehyde, provide a structural understanding of the observed substrate preferences. These crystal structures identify residues lining the active site surface that contact the substrates. Structurally guided site-directed mutagenesis of active site residues was performed with the goal of altering the kinetic preferences for physiological substrates. The kinetic parameters of the COMT mutants versus wild-type enzyme are presented, and coupled with the high-resolution crystal structures, they will serve as a starting point for the in vivo manipulation of lignin monomers in transgenic plants. Ultimately, this structurally based approach to metabolic engineering will allow the further alteration of the lignin biosynthetic pathway in agronomically important plants. This approach will lead to a better understanding of the in vivo operation of the potential metabolic grid for monolignol biosynthesis.
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