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http://purl.uniprot.org/citations/11889103http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11889103http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11889103http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11889103http://www.w3.org/2000/01/rdf-schema#comment"The Methanococcus jannaschii gene MJ0671 was cloned and overexpressed in Escherichia coli, and its gene product was tested for its ability to catalyze the pyridine nucleotide-dependent reduction of either 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (compound 3) to 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate (compound 4) or 5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate (compound 7) to 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate (compound 5). Only compound 3 was found to serve as a substrate for the enzyme. NADPH and NADH functioned equally well as the reductants. This specificity for the reduction of compound 3 was also confirmed by using cell extracts of M. jannaschii and Methanosarcina thermophila. Thus, this step in riboflavin biosynthesis in these archaea is the same as that found in yeasts. The absence of the other genes in the biosynthesis of riboflavin in Archaea is discussed."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.org/dc/terms/identifier"doi:10.1128/jb.184.7.1952-1957.2002"xsd:string
http://purl.uniprot.org/citations/11889103http://purl.org/dc/terms/identifier"doi:10.1128/jb.184.7.1952-1957.2002"xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/author"White R.H."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/author"White R.H."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/author"Xu H."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/author"Xu H."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/author"Graupner M."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/author"Graupner M."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/pages"1952-1957"xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/pages"1952-1957"xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/title"The pyrimidine nucleotide reductase step in riboflavin and F(420) biosynthesis in archaea proceeds by the eukaryotic route to riboflavin."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/title"The pyrimidine nucleotide reductase step in riboflavin and F(420) biosynthesis in archaea proceeds by the eukaryotic route to riboflavin."xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/volume"184"xsd:string
http://purl.uniprot.org/citations/11889103http://purl.uniprot.org/core/volume"184"xsd:string
http://purl.uniprot.org/citations/11889103http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11889103
http://purl.uniprot.org/citations/11889103http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11889103
http://purl.uniprot.org/citations/11889103http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11889103