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http://purl.uniprot.org/citations/10527934http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10527934http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10527934http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/10527934http://www.w3.org/2000/01/rdf-schema#comment"Sulfolobus solfataricus is a hyperthermophilic archaeon growing optimally at 80-85 degrees C. It metabolizes glucose via a novel non-phosphorylated Entner-Doudoroff pathway, in which the reversible C(6) to C(3) aldol cleavage is catalysed by 2-keto-3-deoxygluconate aldolase (KDG-aldolase), generating pyruvate and glyceraldehyde. Given the ability of such a hyperstable enzyme to catalyse carbon-carbon-bond synthesis with non-phosphorylated metabolites, we report here the cloning and sequencing of the S. solfataricus gene encoding KDG-aldolase, and its expression in Escherichia coli to give fully active enzyme. The recombinant enzyme was purified in a simple two-step procedure, and shown to possess kinetic properties indistinguishable from the enzyme purified from S. solfataricus cells. The KDG-aldolase is a thermostable tetrameric protein with a half-life at 100 degrees C of 2.5 h, and is equally active with both d- and l-glyceraldehyde. It exhibits sequence similarity to the N-acetylneuraminate lyase superfamily of Schiff-base-dependent aldolases, dehydratases and decarboxylases, and evidence is presented for a similar catalytic mechanism for the archaeal enzyme by substrate-dependent inactivation by reduction with NaBH(4)."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.org/dc/terms/identifier"doi:10.1042/bj3430563"xsd:string
http://purl.uniprot.org/citations/10527934http://purl.org/dc/terms/identifier"doi:10.1042/bj3430563"xsd:string
http://purl.uniprot.org/citations/10527934http://purl.org/dc/terms/identifier"doi:10.1042/bj3430563"xsd:string
http://purl.uniprot.org/citations/10527934http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10527934
http://purl.uniprot.org/citations/10527934http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10527934
http://purl.uniprot.org/citations/10527934http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10527934
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Danson M.J."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Danson M.J."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Hough D.W."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Hough D.W."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Connaris H."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Connaris H."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Buchanan C.L."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Buchanan C.L."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Reeve C.D."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/author"Reeve C.D."xsd:string
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10527934http://purl.uniprot.org/core/pages"563-570"xsd:string