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Homology Modelling of Lycopene Cleavage Oxygenase: The Key Enzyme of Bixin Production | OMICS International | Abstract
ISSN: 0974-7230

Journal of Computer Science & Systems Biology
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Research Article

Homology Modelling of Lycopene Cleavage Oxygenase: The Key Enzyme of Bixin Production

Raghunath Satpathy*, Rajesh Ku Guru, Rashmiranjan Behera and Aparajita Priyadarshini

Department of Biotechnology, MIRC LAB, MITS Engineering College, Rayagada, Odisha, India

*Corresponding Author:
Dr. Raghunath Satpathy
Department of Biotechnology
MIRC LAB, MITS Engineering College
Rayagada, Odisha, India
Email: [email protected]

Received Date: April 06, 2010; Accepted Date: June 21, 2010; Published June 21, 2010

Citation: Satpathy R, Guru RK, Behera R, Priyadarshini A (2010) Homology Modelling of Lycopene Cleavage Oxygenase: The Key Enzyme of Bixin Production. J Comput Sci Syst Biol 3:059-061. doi: 10.4172/jcsb.1000057

Copyright: © 2010 Satpathy R, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


Bixin is a natural dye and a high commercial important compound, produced from Bixin synthetic pathway in case of Bixa orellana plant. The particular enzyme Lycopene cleavage Oxygenase catalyzes the fi rst step of reaction pathways from Trans-lycopene to Bixin synthesis. The 3D structure of the enzyme was predicted by MODELLER program and the missing side chains were verifi ed by SCRWL4 tool. Model validation was done by using the output of PROCHECK and DOPE score. The Ramachandran plot for the model was observed as 87.3 percentages of residues is in favourable regions that indicate the model is reliable. Molecular dynamics simulation of the model protein was performed in water 5 lakh times for 1000 Pico second and at 300K by GROMACS software in a high performance computing environment. The energy value and RMSD (Root men square deviation) fl uctuation of Carbon alpha back bone of the model was computed that confi rms the stability of the model protein.


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