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http://purl.uniprot.org/citations/9109378http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9109378http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9109378http://www.w3.org/2000/01/rdf-schema#comment"The padA gene encoding the phenylacetaldehyde dehydrogenase involved in the catabolism of 2-phenylethylamine in Escherichia coli has been cloned, sequenced, and located at 31.0 min on the chromosome. The deduced PadA polypeptide contains 499 amino acid residues with a predicted molecular mass of 53.7 kDa, and its primary structure reveals significant similarity with that of members of the aldehyde dehydrogenase superfamily. By engineering optimal transcription and translation elements, a high expression of the padA gene has been achieved. The active PadA enzyme is a homodimer that prefers NAD+ over NADP+ as coenzyme. The enzyme efficiently oxidizes only phenylacetaldehyde-like aromatic aldehydes, and has a weak esterase activity with p-nitrophenol. The padA gene constitutes a new catabolic tool for designing DNA cassettes to expand the abilities of microorganisms to degrade toxic aromatic compounds."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(97)00228-7"xsd:string
http://purl.uniprot.org/citations/9109378http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(97)00228-7"xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Diaz E."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Diaz E."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Garcia J.L."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Garcia J.L."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Ferrandez A."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Ferrandez A."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Prieto M.A."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/author"Prieto M.A."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/pages"23-27"xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/pages"23-27"xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/title"Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/title"Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/volume"406"xsd:string
http://purl.uniprot.org/citations/9109378http://purl.uniprot.org/core/volume"406"xsd:string
http://purl.uniprot.org/citations/9109378http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9109378
http://purl.uniprot.org/citations/9109378http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9109378