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Please use this identifier to cite or link to this item: http://repository.iitr.ac.in/handle/123456789/1099
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dc.contributor.authorDhindwal S.-
dc.contributor.authorPatil D.N.-
dc.contributor.authorMohammadi M.-
dc.contributor.authorSylvestre M.-
dc.contributor.authorTomar, Shailly-
dc.contributor.authorKumar, Pravindra R.Manish-
dc.date.accessioned2020-09-30T11:32:42Z-
dc.date.available2020-09-30T11:32:42Z-
dc.date.issued2011-
dc.identifier.citationJournal of Biological Chemistry(2011), 286(42): 37011-37022-
dc.identifier.issn219258-
dc.identifier.other21880718-
dc.identifier.urihttps://doi.org/10.1074/jbc.M111.291013-
dc.identifier.urihttp://repository.iitr.ac.in/handle/123456789/1099-
dc.description.abstractBiphenyl dehydrogenase, a member of short-chain dehydrogenase/ reductase enzymes, catalyzes the second step of the biphenyl/polychlorinated biphenyls catabolic pathway in bacteria. To understand the molecular basis for the broad substrate specificity of Pandoraea pnomenusa strain B-356 biphenyl dehydrogenase (BphB B-356), the crystal structures of the apoenzyme, the binary complex with NAD +, and the ternary complexes with NAD +-2,3-dihydroxybiphenyl and NAD +-4,4?- dihydroxybiphenyl were determined at 2.2-, 2.5-, 2.4-, and 2.1- Åresolutions, respectively. A crystal structure representing an intermediate state of the enzyme was also obtained in which the substrate binding loop was ordered as compared with the apo and binary forms but it was displaced significantly with respect to the ternary structures. These five structures reveal that the substrate binding loop is highly mobile and that its conformation changes during ligand binding, starting from a disorganized loop in the apo state to a well organized loop structure in the ligand-bound form. Conformational changes are induced during ligand binding; forming a well defined cavity to accommodate a wide variety of substrates. This explains the biochemical data that shows BphB B-356 converts the dihydrodiol metabolites of 3,3?-dichlorobiphenyl, 2,4,4?-trichlorobiphenyl, and 2,6-dichlorobiphenyl to their respective dihydroxy metabolites. For the first time, a combination of structural, biochemical, and molecular docking studies of BphB B-356 elucidate the unique ability of the enzyme to transform the cis-dihydrodiols of double meta-, para-, and ortho-substituted chlorobiphenyls. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.-
dc.language.isoen_US-
dc.relation.ispartofJournal of Biological Chemistry-
dc.titleBiochemical studies and ligand-bound structures of biphenyl dehydrogenase from pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme-
dc.typeArticle-
dc.scopusid36082537700-
dc.scopusid26431600400-
dc.scopusid23390544500-
dc.scopusid7005984229-
dc.scopusid57203506001-
dc.scopusid55064809000-
dc.affiliationDhindwal, S., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India-
dc.affiliationPatil, D.N., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India-
dc.affiliationMohammadi, M., I-
dc.description.correspondingauthorKumar, P.; Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India; email: pravshai@gmail.com-
Appears in Collections:Journal Publications [BT]

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