IR @ Goa University

Structural and docking studies of Leucaena leucocephala Cinnamoyl CoA reductase

Show simple item record Prasad, N.K. Vindal, V. VikashKumar Kabra, A. Phogat, N. ManojKumar 2015-06-04T03:02:03Z 2015-06-04T03:02:03Z 2011
dc.identifier.citation Journal of Molecular Modeling. 17(3); 2011; 533-541. en_US
dc.description.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. en_US
dc.publisher Springer Verlag (Germany) en_US
dc.subject Biotechnology en_US
dc.title Structural and docking studies of Leucaena leucocephala Cinnamoyl CoA reductase en_US
dc.type Journal article en_US
dc.identifier.impf y

Files in this item

This item appears in the following Collection(s)

Show simple item record

Search IR

Advanced Search


My Account