HOMOLOGY MODELING OF DSZA PROTEIN OF STREPTOMYCES SP. VUR PPR 101 AND ITS IN SILICO DOCKING STUDIES WITH DIBENZOTHIOPHENE SULFONEPRAVEEN REDDY, P. AND UMAMAHESHWARA RAO V.
Dibenzothiophene (DBT) biodesulfurization through the microbial enzymes has come forth in preference owed to its resistance to conventional hydrodesulfurization. Thus, much attention has gained to isolate new microorganisms and their key enzymes that effectively degrade DBT under viable conditions, consequently, improving technologies to get greater desulfurization rates by the increased protein expression levels. The present study was aimed to examine the DszA (DBT monooxygenase) activity, the second enzyme, in microbial DBT desulfurization which catalyzes the conversion of DBT sulfone to 2'- hydroxybiphenyl 2-sulfinic acid, in relation to the point mutations through insilico approaches in DszA protein of Streptomyces sp. VUR PPR 101 isolated from oil contaminated sites. Therefore, mutations were created in the homology modeled DszA protein and docking studies against DBTO2 with wild and mutant models (N151D, I150M, and A192T) were carried out. Based on the Libdock scores of the docked complexes, mutant model N151D had shown increased response towards DBTO2 inferring higher desulfurization activity.
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