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Homology modeling and docking studies of Comamonas testosteroni B-356 biphenyl-2, 3-dioxygenase involved in degradation of polychlorinated biphenyls
Poster

Homology modeling and docking studies of Comamonas testosteroni B-356 biphenyl-2, 3-dioxygenase involved in degradation of polychlorinated biphenyls

Homology modeling and docking studies of Comamonas testosteroni B-356 biphenyl-2, 3-dioxygenase involved in degradation of polychlorinated biphenyls
Poster

Homology modeling and docking studies of Comamonas testosteroni B-356 biphenyl-2, 3-dioxygenase involved in degradation of polychlorinated biphenyls

The three-dimensional model of a-subunit of Biphenyl dioxygenase (BphA) from Comamonas testosteroni B-356 has been constructed. The kinetic parameters of biphenyl compounds were well matched with the docking results. The binding properties of these biphenyl compounds along with identification of critical active site residues could be used for further site-directed mutagenesis experiments in order to identify their role in activity and substrate specificity.
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