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Comparative modeling of DszC, an enzyme in biodesulfurization, and performing in silico point mutation for increasing tendency to oil



Ibrahim Torktaz1, Zahra Etemadifar2* & Peyman Derikvand2



1Department of Biotechnology, Faculty of Advanced science and technologies, University of Isfahan, Hezarjarib St, 81746-73441, Isfahan, Iran, and National Institute of Genetic Engineering and Biotechnology, Tehran, Iran; 2Department of Biology, Faculty of Sciences, University of Isfahan, Hezarjarib St, 81746-73441, Isfahan, I.R. Iran.


Email; *Corresponding author


Article Type

Prediction model


Received December 06, 2011; Accepted January 01, 2012; Published March 17, 2012



Desulfurization protein named DszC from Rhodococcus erythropolis is the key enzyme for biodesulforization of dibenzothiophene (DBT) in 4S pathway, which is a pathway with four enzymes. DszC enzyme biodesulfurizes DBT and its derivatives in oil components and biphasic systems. It functions well at the oil- water interface. In this study point mutation performed in DszC enzyme regarding to increase protein hydrophobicity and stability for application in immobilized form. 3D model of DszC predicted using Phyre2, SAM-T08 and M4t servers. I-Mutant 2 server used to determine potential spots for point mutation, and Molegro Virtual Docker (MVD) used for performing point mutation on 3D model. Hydrophobicity plots generated by Bioedit version in Kyte-Doolittle scale indicated that protein hydrophobicity is increased after mutation. Also protein stability increased 26.11 units in scale of DDC2.



Torktaz et al. Bioinformation 8(5): 246-250 (2012)

Edited by

P Kangueane






Biomedical Informatics



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.