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http://purl.uniprot.org/citations/9880484http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9880484http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9880484http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9880484http://www.w3.org/2000/01/rdf-schema#comment"Two enzymes, designated, E-2 and E-2', catalyze different oxidation reactions of an aci-reductone intermediate in the methionine salvage pathway. E-2 and E-2', overproduced in Escherichia coli from the same gene, have the same protein component. E-2 and E-2' are separable on an anion exchange column or a hydrophobic column. Their distinct catalytic and chromatographic properties result from binding different metals. The apo-enzyme, obtained after metal is removed from either enzyme, is catalytically inactive. Addition of Ni2+ or Co2+ to the apo-protein yields E-2 activity. E-2' activity is obtained when Fe2+ is added. Production in intact E. coli of E-2 and E-2' depends on the availability of the corresponding metals. These observations suggest that the metal component dictates reaction specificity."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.3.1193"xsd:string
http://purl.uniprot.org/citations/9880484http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.3.1193"xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/author"Dai Y."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/author"Dai Y."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/author"Abeles R.H."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/author"Abeles R.H."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/author"Wensink P.C."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/author"Wensink P.C."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/pages"1193-1195"xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/pages"1193-1195"xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/title"One protein, two enzymes."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/title"One protein, two enzymes."xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/9880484http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/9880484http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9880484
http://purl.uniprot.org/citations/9880484http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9880484
http://purl.uniprot.org/citations/9880484http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9880484