Structural and docking studies of Leucaena leucocephala Cinnamoyl CoA reductase
| Autor: | Vikash Kumar, Manoj Kumar, Nirmal K. Prasad, Vaibhav Vindal, Navneet Phogat, Ashish Kabra |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Molecular Sequence Data Sequence alignment Lignin Catalysis Substrate Specificity Inorganic Chemistry chemistry.chemical_compound Non-competitive inhibition Catalytic Domain Amino Acid Sequence Physical and Theoretical Chemistry Plant Proteins chemistry.chemical_classification biology fungi Organic Chemistry Active site Fabaceae Aldehyde Oxidoreductases Computer Science Applications Metabolic pathway Enzyme Computational Theory and Mathematics Biochemistry chemistry Docking (molecular) biology.protein Cinnamoyl-CoA reductase Sequence Alignment |
| Zdroj: | Journal of Molecular Modeling. 17:533-541 |
| ISSN: | 0948-5023 1610-2940 |
| DOI: | 10.1007/s00894-010-0744-2 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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