dc.creator | Andújar, Eloísa | es |
dc.creator | Hernáez, María José | es |
dc.creator | Kaschabek, Stefan R. | es |
dc.creator | Reineke, Walter | es |
dc.creator | Santero Santurino, Eduardo | es |
dc.date.accessioned | 2017-07-24T10:58:46Z | |
dc.date.available | 2017-07-24T10:58:46Z | |
dc.date.issued | 2000-02 | |
dc.identifier.citation | Andújar, E., Hernáez, M.J., Kaschabek, S.R., Reineke, W. y Santero, E. (200-). Identification of an extradiol dioxygenase involved in tetralin biodegradation: Gene sequence analysis and purification and characterization of the gene product. Journal of Bacteriology, 182 (3), 789-795. | |
dc.identifier.issn | 0021-9193 (impreso) | es |
dc.identifier.issn | 1098-5530 (electronico) | es |
dc.identifier.uri | http://hdl.handle.net/11441/63005 | |
dc.description.abstract | A genomic region involved in tetralin biodegradation was recently identified in Sphingomonas strain TFA. We have cloned and sequenced from this region a gene designated thnC, which codes for an extradiol dioxygenase required for tetralin utilization. Comparison to similar sequences allowed us to define a subfamily of 1,2-dihydroxynaphthalene extradiol dioxygenases, which comprises two clearly different groups, and to show that ThnC clusters within group 2 of this subfamily. 1,2-Dihydroxy-5,6,7,8-tetrahydronaphthalene was found to be the metabolite accumulated by a thnC insertion mutant. The ring cleavage product of this metabolite exhibited behavior typical of a hydroxymuconic semialdehyde toward pH-dependent changes and derivatization with ammonium to give a quinoline derivative. The gene product has been purified, and its biochemical properties have been studied. The enzyme is a decamer which requires Fe(II) for activity and shows high activity toward its substrate (V(max), 40.5 U mg-1 K(m) 18.6 μM). The enzyme shows even higher activity with 1,2-dihydroxynaphthalene and also significant activity toward 1,2-dihydroxybiphenyl or methylated catechols. The broad substrate specificity of ThnC is consistent with that exhibited by other extradiol dioxygenases of the same group within the subfamily of 1,2- dihydroxynaphthalene dioxygenases. | es |
dc.description.sponsorship | Comisión Interministerial de Ciencia y Tecnología BIO96-0908 | es |
dc.description.sponsorship | Unión Europea EV5V-CT92-0192 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | American Society for Microbiology | es |
dc.relation.ispartof | Journal of Bacteriology, 182 (3), 789-795. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Identification of an extradiol dioxygenase involved in tetralin biodegradation: Gene sequence analysis and purification and characterization of the gene product | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Genética | es |
dc.relation.projectID | BIO96-0908 | es |
dc.relation.projectID | EV5V-CT92-0192 | es |
dc.relation.publisherversion | http://dx.doi.org/10.1128/JB.182.3.789-795.2000 | es |
dc.identifier.doi | 10.1128/JB.182.3.789-795.2000 | es |
idus.format.extent | 7 p. | es |
dc.journaltitle | Journal of Bacteriology | es |
dc.publication.volumen | 182 | es |
dc.publication.issue | 3 | es |
dc.publication.initialPage | 789 | es |
dc.publication.endPage | 795 | es |
dc.contributor.funder | Comisión Interministerial de Ciencia y Tecnología (CICYT). España | |
dc.contributor.funder | European Union (UE) | |