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http://purl.uniprot.org/citations/527937http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/527937http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/527937http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/527937http://www.w3.org/2000/01/rdf-schema#comment"1) A new enzyme, 2,3-dimethylmalate lyase, was purified from Clostridium barkeri to about 80% homogeneity. Some of the properties of the enzyme are described. 2) It is shown that the 2,3-dimethylmalic acid (m.p. 143 degrees C) described in the literature represents only one racemic pair. This pair is not attacked by 2,3-dimethylmalate lyase. 3) The isolation of both racemic pairs of 2,3-dimethylmalic acid is described. Half of one pair, m.p. 104-106 degrees C, was converted to propionate and pyruvate by 2,3-dimethylmalate lyase. 4) In combination with earlier work performed by E.R. Stadtman and coworkers the results given under points 1--3 establish 2,3-dimethylmalate as an intermediate in the degradation of nicotinic acid by C. barkeri. 5) Experimental evidence indicates the 2,3-dimethylmalate lyase is no acyl-S-enzyme and that it is different in this respect as well as in quaternary structure from the apparently related enzymes citrate lyase and citramalate lyase."xsd:string
http://purl.uniprot.org/citations/527937http://purl.org/dc/terms/identifier"doi:10.1515/bchm2.1979.360.2.1693"xsd:string
http://purl.uniprot.org/citations/527937http://purl.org/dc/terms/identifier"doi:10.1515/bchm2.1979.360.2.1693"xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/author"Eggerer H."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/author"Eggerer H."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/author"Lill U."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/author"Lill U."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/author"Pirzer P."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/author"Pirzer P."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/date"1979"xsd:gYear
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/date"1979"xsd:gYear
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/name"Hoppe-Seyler's Z. Physiol. Chem."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/name"Hoppe-Seyler's Z. Physiol. Chem."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/pages"1693-1702"xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/pages"1693-1702"xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/title"Nicotinic acid metabolism. 2,3-Dimethylmalate lyase."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/title"Nicotinic acid metabolism. 2,3-Dimethylmalate lyase."xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/volume"360"xsd:string
http://purl.uniprot.org/citations/527937http://purl.uniprot.org/core/volume"360"xsd:string
http://purl.uniprot.org/citations/527937http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/527937
http://purl.uniprot.org/citations/527937http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/527937
http://purl.uniprot.org/citations/527937http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/527937