Homology modeling and in silico docking studies of DszB enzyme protein,hydroxyphenyl benzene sulfinate desulfinase of streptomyces sp. VUR PPR 101

Biodesulfurization of organosulfur compounds in fossil fuels by employing microbes is advantageous over traditional hydrodesulfurization. dibenzothiophene (dbt) is the most common model organosulfur compound used in biodesulfurization studies by means of microbes. the microbial desulfurization of dbt via the 4s pathway involves four enzymatic steps. the present study investigated the activity of wild type dszb (hydroxyphenyl benzene sulfinate desulfinase),the last enzyme in the 4s pathway,and several mutant forms. the 3-d protein model of dszb was developed and mutant proteins of dszb viz.,q65h,y63f and y63a were constructed. docking studies were done between wild dszb and the substrate,hydroxy phenyl benzene sulfinate (hpbs) as well as between mutant dszb proteins and hpbs. based on the libdock scores obtained from docked complexes,mutant protein y63a was found to have highest affinity towards the substrate,hpbs likely suggesting highest activity. © 2017 jordan journal of biological sciences.