ArticleNature communications2021
Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 35 citations in OpenAlex.
- Structural insights into pterocarpan reductases unveil a universal ring-opening mechanism in plant biosynthesis of 4-(furan-2-yl) phenol derivatives.Acta pharmaceutica Sinica. B · 2026Article
- Molecular basis and biological relevance of bacterial and plant pinoresinol/lariciresinol reductase specificities.Protein science : a publication of the Protein Society · 2026Article
- De novo biosynthesis of plant lignans by synthetic yeast consortia.Nature chemical biology · 2025Article
- Construction of lignan glycosides biosynthetic network in Escherichia coli using mutltienzyme modules.Microbial cell factories · 2024Article
- The ERF transcription factor LTF1 activates DIR1 to control stereoselective synthesis of antiviral lignans and stress defense inActa pharmaceutica Sinica. B · 2024Article
- Metabolome analysis of genus Forsythia related constituents in Forsythia suspensa leaves and fruits using UPLC-ESI-QQQ-MS/MS technique.PloS one · 2022Article
- Potential roles of gut microbes in biotransformation of natural products: An overview.Frontiers in microbiology · 2022Review
- The metabolic and proteomic repertoires of periderm tissue in skin of the reticulated Sikkim cucumber fruit.Horticulture research · 2022Article
- Isatis indigotica: from (ethno) botany, biochemistry to synthetic biology.Molecular horticulture · 2021Review
- Physiological and Proteomic Responses of Contrasting Alfalfa (Frontiers in plant science · 2021Article
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pinoresinol-lariciresinol reductases (PLRs) are enzymes involved in the lignan biosynthesis after the initial dimerization of two monolignols, and this represents the entry point for the synthesis of 8-8' lignans and contributes greatly to their structural diversity. Of particular interest has been the determination of how differing substrate specificities are achieved with these enzymes. Here, we present crystal structures of IiPLR1 from Isatis indigotica and pinoresinol reductases (PrRs) AtPrR1 and AtPrR2 from Arabidopsis thaliana, in the apo, substrate-bound and product-bound states. Each structure contains a head-to-tail homodimer, and the catalytic pocket comprises structural elements from both monomers. β4 loop covers the top of the pocket, and residue 98 from the loop governs catalytic specificity. The substrate specificities of IiPLR1 and AtPrR2 can be switched via structure-guided mutagenesis. Our study provides insight into the molecular mechanism underlying the substrate specificity of PLRs/PrRs and suggests an efficient strategy for the large-scale commercial production of the pharmaceutically valuable compound lariciresinol.
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