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http://purl.uniprot.org/citations/6365916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6365916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6365916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/6365916http://www.w3.org/2000/01/rdf-schema#comment"Tetrahydrodipicolinate succinylase, an enzyme involved in the diaminopimelate-lysine pathway, was purified 1900-fold from crude extracts of Escherichia coli. The enzyme catalyzes the formation of CoA and N-succinyl-2-amino-6-keto-L-pimelate from succinyl-CoA and tetrahydrodipicolinate. The purified enzyme was shown to be homogeneous by polyacrylamide gel electrophoresis. The Stokes radius of the enzyme was determined from its elution volume on a Sephacryl S300 column and its sedimentation constant from sucrose density gradient centrifugation. These were 35 A and 4.7 (S20,w), respectively. The enzyme consists of two subunits each with a mass of 31,000 daltons, as determined using sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Tetrahydrodipicolinate succinylase was shown to be a sulfhydryl enzyme. It has a pH optimum of 8.2. The equilibrium lies predominantly in favor of product formation but the reverse reaction can be demonstrated in vitro."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)43207-8"xsd:string
http://purl.uniprot.org/citations/6365916http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)43207-8"xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/author"Gilvarg C."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/author"Gilvarg C."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/author"Simms S.A."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/author"Simms S.A."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/author"Voige W.H."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/author"Voige W.H."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/pages"2734-2741"xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/pages"2734-2741"xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/title"Purification and characterization of succinyl-CoA: tetrahydrodipicolinate N-succinyltransferase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/title"Purification and characterization of succinyl-CoA: tetrahydrodipicolinate N-succinyltransferase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/volume"259"xsd:string
http://purl.uniprot.org/citations/6365916http://purl.uniprot.org/core/volume"259"xsd:string
http://purl.uniprot.org/citations/6365916http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6365916
http://purl.uniprot.org/citations/6365916http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6365916
http://purl.uniprot.org/citations/6365916http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6365916