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http://purl.uniprot.org/citations/16511150http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16511150http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16511150http://www.w3.org/2000/01/rdf-schema#comment"Pyruvate kinase (PK) from a moderate thermophile, Bacillus stearothermophilus (BstPK), is an allosteric enzyme activated by AMP and ribose 5-phosphate but not by fructose 1,6-bisphosphate (FBP). However, almost all other PKs are activated by FBP. The wild-type and W416F/V435W mutant BstPKs were crystallized by the hanging-drop vapour-diffusion method. However, they were unsuitable for structural analysis because their data sets exhibited low completeness. A crystal suitable for structural analysis was obtained using C9S/C268S enzyme. The crystal belonged to space group P6(2)22, with unit-cell parameters a = b = 145.97, c = 118.03 A."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.org/dc/terms/identifier"doi:10.1107/s1744309105021093"xsd:string
http://purl.uniprot.org/citations/16511150http://purl.org/dc/terms/identifier"doi:10.1107/s1744309105021093"xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Ito S."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Ito S."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Sakai H."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Sakai H."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Suzuki K."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Suzuki K."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Shimizu-Ibuka A."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/author"Shimizu-Ibuka A."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/name"Acta Crystallogr. F"xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/name"Acta Crystallogr. F"xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/pages"759-761"xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/pages"759-761"xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/title"Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/title"Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus."xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/volume"61"xsd:string
http://purl.uniprot.org/citations/16511150http://purl.uniprot.org/core/volume"61"xsd:string
http://purl.uniprot.org/citations/16511150http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16511150
http://purl.uniprot.org/citations/16511150http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16511150