ArticleJournal of molecular modeling2011
Structural and docking studies of Leucaena leucocephala Cinnamoyl CoA reductase.
Article in Journal of molecular modeling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 19 citations in OpenAlex.
- Identification and In Vitro Functional Characterization of thePlants (Basel, Switzerland) · 2026Article
- Genome-wide identification and expression pattern analysis of the cinnamoyl-CoA reductase gene family in flax (Linum usitatissimum L.).BMC genomics · 2025Article
- Identification and expression analysis of cinnamyl CoA reductase gene family and function ofFrontiers in plant science · 2025Article
- Characterization, Expression Profiling, and Biochemical Analyses of theInternational journal of molecular sciences · 2022Article
- Genome-wide identification and characterization ofFrontiers in plant science · 2022Article
- Article
- Molecular Characterization and In Silico Analysis of the Pheromone-Binding Protein of the European Grapevine Moth Lobesia botrana (Denis & Schiffermüller) (Lepidoptera, Tortricidae).Neotropical entomology · 2014Article
- Comparative proteomic analysis of somatic embryo maturation in Carica papaya L.Proteome science · 2014Article
- COX-2 structural analysis and docking studies with gallic acid structural analogues.SpringerPlus · 2012Article
- In silico analysis of Pycnoporus cinnabarinus laccase active site with toxic industrial dyes.Journal of molecular modeling · 2012Article
- Improving the prediction of protein binding sites by combining heterogeneous data and Voronoi diagrams.BMC bioinformatics · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lignin, a major constituent of plant call wall, is a phenolic heteropolymer. It plays a major role in the development of plants and their defense mechanism against pathogens. Therefore Lignin biosynthesis is one of the critical metabolic pathways. In lignin biosynthesis, the Cinnamoyl CoA reductase is a key enzyme which catalyzes the first step in the pathway. Cinnamoyl CoA reductase provides the substrates which represent the main transitional molecules of lignin biosynthesis pathway, exhibits a high in vitro kinetic preference for feruloyl CoA. In present study, the three-dimensional model of cinnamoyl CoA reductase was constructed based on the crystal structure of Grape Dihydroflavonol 4-Reductase. Furthermore, the docking studies were performed to understand the substrate interactions to the active site of CCR. It showed that residues ARG51, ASN52, ASP54 and ASN58 were involved in substrate binding. We also suggest that residue ARG51 in CCR is the determinant residue in competitive inhibition of other substrates. This structural and docking information have prospective implications to understand the mechanism of CCR enzymatic reaction with feruloyl CoA, however the approach will be applicable in prediction of substrates and engineering 3D structures of other enzymes as well.
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