ArticleThe Plant cell2010
Crystal structures of a Populus tomentosa 4-coumarate:CoA ligase shed light on its enzymatic mechanisms.
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 48 papers.
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48 citing papers in PubMed, 121 citations in OpenAlex.
- Molecular Cloning, Biochemical Characterization, and Structural Insights into a Flavonoid-Associated Class II 4-Coumarate:CoA Ligase fromJournal of microbiology and biotechnology · 2026Article
- Study on biosynthesis pathway and accumulation mechanism of the dihydrochalcones inHorticulture research · 2026Article
- A Scots pine 4-coumarate:CoA ligase with high cinnamic acid affinity is the primary candidate for pinosylvin biosynthesis.The Plant journal : for cell and molecular biology · 2026Article
- Comparative analysis of key flavonoid synthesis genes in the transcriptome of Cayratia Japonica and therapeutic target prediction for ulcerative colitis : Functional & integrative genomics.Functional & integrative genomics · 2025Article
- Algal origins of core land plant stress response subnetworks.The Plant journal : for cell and molecular biology · 2025Article
- The palmitoyl-CoA ligase Fum16 is part of amBio · 2025Article
- Dual feedback inhibition of ATP-dependent caffeate activation economizes ATP in caffeate-dependent electron bifurcation.Applied and environmental microbiology · 2024Article
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- Fusion gene 4CL-CCR promotes lignification in tobacco suspension cells.Plant cell reports · 2023Article
- KIPEs3: Automatic annotation of biosynthesis pathways.PloS one · 2023Article
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- Biocontrol activity and action mechanism ofFrontiers in microbiology · 2022Article
- Characterization of a Cytosolic Acyl-Activating Enzyme Catalyzing the Formation of 4-Methylvaleryl-CoA for Pogostone Biosynthesis in Pogostemon Cablin.Plant & cell physiology · 2021Article
- Underwater CAM photosynthesis elucidated by Isoetes genome.Nature communications · 2021Article
- Key Enzymes Involved in the Synthesis of Hops Phytochemical Compounds: From Structure, Functions to Applications.International journal of molecular sciences · 2021Review
- Plant Secondary Metabolites with an Overview ofInternational journal of molecular sciences · 2021Review
- Structural insight of two 4-Coumarate CoA ligase (3 Biotech · 2020Article
- Chemoenzymatic Synthesis and Biological Evaluation for Bioactive Molecules Derived from Bacterial Benzoyl Coenzyme A Ligase and Plant Type III Polyketide Synthase.Biomolecules · 2020Article
- A novel hydroxycinnamoyl transferase for synthesis of hydroxycinnamoyl spermine conjugates in plants.BMC plant biology · 2019Article
- Molecular cloning and functional analysis of 4-Coumarate:CoA ligase 4(4CL-like 1)from Fraxinus mandshurica and its role in abiotic stress tolerance and cell wall synthesis.BMC plant biology · 2019Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
4-Coumaric acid:CoA ligase (4CL) is the central enzyme of the plant-specific phenylpropanoid pathway. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters, the precursors of lignin and other important phenylpropanoids, in two-step reactions involving the formation of hydroxycinnamate-AMP anhydride and then the nucleophilic substitution of AMP by CoA. In this study, we determined the crystal structures of Populus tomentosa 4CL1 in the unmodified (apo) form and in forms complexed with AMP and adenosine 5'-(3-(4-hydroxyphenyl)propyl)phosphate (APP), an intermediate analog, at 2.4, 2.5, and 1.9 Å resolution, respectively. 4CL1 consists of two globular domains connected by a flexible linker region. The larger N-domain contains a substrate binding pocket, while the C-domain contains catalytic residues. Upon binding of APP, the C-domain rotates 81° relative to the N-domain. The crystal structure of 4CL1-APP reveals its substrate binding pocket. We identified residues essential for catalytic activities (Lys-438, Gln-443, and Lys-523) and substrate binding (Tyr-236, Gly-306, Gly-331, Pro-337, and Val-338) based on their crystal structures and by means of mutagenesis and enzymatic activity studies. We also demonstrated that the size of the binding pocket is the most important factor in determining the substrate specificities of 4CL1. These findings shed light on the enzymatic mechanisms of 4CLs and provide a solid foundation for the bioengineering of these enzymes.
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