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http://purl.uniprot.org/citations/31058311http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31058311http://www.w3.org/2000/01/rdf-schema#comment"In Azospirillum brasilense, a gram-negative nitrogen-fixing bacterium, l-arabinose is converted to α-ketoglutarate through a nonphosphorylative metabolic pathway. In the first step in the pathway, l-arabinose is oxidized to l-arabino-γ-lactone by NAD(P)-dependent l-arabinose 1-dehydrogenase (AraDH) belonging to the glucose-fructose oxidoreductase/inositol dehydrogenase/rhizopine catabolism protein (Gfo/Idh/MocA) family. Here, we determined the crystal structures of apo- and NADP-bound AraDH at 1.5 and 2.2 Å resolutions, respectively. A docking model of l-arabinose and NADP-bound AraDH and structure-based mutational analyses suggest that Lys91 or Asp169 serves as a catalytic base and that Glu147, His153, and Asn173 are responsible for substrate recognition. In particular, Asn173 may play a role in the discrimination between l-arabinose and d-xylose, the C4 epimer of l-arabinose."xsd:string
http://purl.uniprot.org/citations/31058311http://purl.org/dc/terms/identifier"doi:10.1002/1873-3468.13424"xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/author"Watanabe Y."xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/author"Watanabe S."xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/author"Watanabe Y.'"xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/author"Iga C."xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/pages"1257-1266"xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/title"Structural insights into the catalytic and substrate recognition mechanisms of bacterial l-arabinose 1-dehydrogenase."xsd:string
http://purl.uniprot.org/citations/31058311http://purl.uniprot.org/core/volume"593"xsd:string
http://purl.uniprot.org/citations/31058311http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31058311
http://purl.uniprot.org/citations/31058311http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31058311
http://purl.uniprot.org/uniprot/#_Q53TZ2-mappedCitation-31058311http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31058311
http://purl.uniprot.org/uniprot/Q53TZ2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31058311