Viger, Jean-Francois; Mohammadi, Mahmood; Barriault, Diane et Sylvestre, Michel (2012). Metabolism of chlorobiphenyls by a variant biphenyl dioxygenase exhibiting enhanced activity toward dibenzofuran Biochemical and Biophysical Research Communications , vol. 419 , nº 2. pp. 362-367. DOI: 10.1016/j.bbrc.2012.02.029.
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The biphenyl dioxygenase of Burkholderia xenovorans LB400 (BphAELB400) catalyzes the dihydroxylation of biphenyl and of several polychlorinated biphenyls (PCBs) but it poorly oxidizes dibenzofuran. In this work we showed that BphAERR41, a variant which was previously found to metabolize dibenzofuran more efficiently than its parent BphAELB400, metabolized a broader range of PCBs than BphAELB400. Hence, BphAERR41 was able to metabolize 2,6,2',6'-, 3,4,3',5'- and 2,4,3',4'-tetrachlorobiphenyl that BphAELB400 is unable to metabolize. BphAERR41 was obtained by changing Thr335Phe336Asn338Ile341Leu409 of BphAELB400 to Ala335Met336Gln338Val341Phe409. Site-directed mutagenesis was used to create combinations of each substitution, in order to assess their individual contributions. Data show that the same Asn338Glu/Leu409Phe substitution that enhanced the ability to metabolize dibenzofuran resulted in a broadening of the PCB substrates range of the enzyme. The role of these substitutions on regiospecificities toward selected PCBs is also discussed.
| Type de document: | Article |
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| Mots-clés libres: | - |
| Centre: | Centre INRS-Institut Armand Frappier |
| Date de dépôt: | 09 mars 2024 21:43 |
| Dernière modification: | 09 mars 2024 21:43 |
| URI: | https://espace.inrs.ca/id/eprint/14102 |
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