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http://purl.uniprot.org/citations/16267294http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16267294http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16267294http://www.w3.org/2000/01/rdf-schema#comment"The xlnD gene from Pseudomonas alcaligenes NCIMB 9867 (strain P25X) was shown to encode 3-hydroxybenzoate 6-hydroxylase I, the enzyme that catalyzes the NADH-dependent conversion of 3-hydroxybenzoate to gentisate. Active recombinant XlnD was purified as a hexahistidine fusion protein from Escherichia coli, had an estimated molecular mass of 130 kDa, and is probably a trimeric protein with a subunit mass of 43 kDa. This is in contrast to the monomeric nature of the few 3-hydroxybenzoate 6-hydroxylases that have been characterized thus far. Like other 3-hydroxybenzoate 6-hydroxylases, XlnD could utilize either NADH or NADPH as the electron donor. P25X harbors a second 3-hydroxybenzoate 6-hydroxylase II that was strictly inducible by specific aromatic substrates. However, the degradation of 2,5-xylenol and 3,5-xylenol in strain P25X was found to be dependent on the xlnD-encoded 6-hydroxylase I and not the second, strictly inducible 6-hydroxylase II."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.org/dc/terms/identifier"doi:10.1128/jb.187.22.7696-7702.2005"xsd:string
http://purl.uniprot.org/citations/16267294http://purl.org/dc/terms/identifier"doi:10.1128/jb.187.22.7696-7702.2005"xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Gao X."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Gao X."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Poh C.L."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Poh C.L."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Tan C.L."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Tan C.L."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Yeo C.C."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/author"Yeo C.C."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/pages"7696-7702"xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/pages"7696-7702"xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/title"Molecular and biochemical characterization of the xlnD-encoded 3-hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/title"Molecular and biochemical characterization of the xlnD-encoded 3-hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867."xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/volume"187"xsd:string
http://purl.uniprot.org/citations/16267294http://purl.uniprot.org/core/volume"187"xsd:string
http://purl.uniprot.org/citations/16267294http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16267294
http://purl.uniprot.org/citations/16267294http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16267294