Title

Authors

Affiliation

Plant Tissue Culture and Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.

Email

bm.khan@ncl.res.in; *Corresponding author

Article Type

Hypothesis

Date

Received February 04, 2013; Accepted February 11, 2013; Published March 02, 2013

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. 

Keywords

Cinnamoyl CoA reductase 1, Mutagenesis, Homology Modeling, Docking Simulations, Substrate Specificity.

Abbreviations

Ll-CCRH1, Leucaena leucocephala cinnamoyl CoA reductase 1, OPLS, Optimized Potentials for Liquid Simulations, RMSD, Root Mean Square Deviation.

Citation

Sonawane et al.   Bioinformation 9(5): 224-232 (2013)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.