title: in Silico mutagenesis and docking studies of active site residues suggest altered substrate specificity and possible physiological role of Cinnamoyl CoA Reductase 1 (Ll-CCRH1).
abstract: : Cinnamoyl CoA reductase (CCR) carries out the first committed step in monolignol biosynthesis and acts as a first regulatory point in lignin formation. CCR shows multiple substrate specificity towards various cinnamoyl CoA esters. Here, in Silico mutagenesis studies of active site residues of Ll-CCRH1 were carried out. Homology modeling based modeled 3D structure of Ll-CCRH1 was used as template for in Silico mutant preparations. Docking simulations of Ll-CCRH1 mutants with CoA esters by AutoDock Vina tools showed altered substrate specificity as compared to wild type. The study evidences that conformational changes, and change in geometry or architecture of active site pocket occurred following mutations. The altered substrate specificity for active site mutants suggests the possible physiological role of CCR either in lignin formation or in defense system in plants.
  
  
  BACKGROUND
  Ll-CCRH1 - Leucaena leucocephala cinnamoyl CoA reductase 1, OPLS - Optimized Potentials for Liquid Simulations, RMSD - Root Mean Square Deviation.
authors.affiliation: Plant Tissue Culture and Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.
authors.forename: Prashant
authors.initials: P
authors.lastname: Sonawane
authors.forename: Krunal
authors.initials: K
authors.lastname: Patel
authors.forename: Rishi Kishore
authors.initials: RK
authors.lastname: Vishwakarma
authors.forename: Somesh
authors.initials: S
authors.lastname: Singh
authors.forename: Bashir Mohammad
authors.initials: BM
authors.lastname: Khan
keywords: Cinnamoyl CoA reductase 1; Docking Simulations; Homology Modeling; Mutagenesis; Substrate Specificity