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http://purl.uniprot.org/citations/18558723http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18558723http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18558723http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/18558723http://www.w3.org/2000/01/rdf-schema#comment"The exclusive presence of glycerol-1-phosphate dehydrogenases (G1PDH) has been postulated to be a key feature that distinguishes archaea from bacteria. However, homologues of G1PDH genes can be found in several bacterial species, among them the hitherto uncharacterized open reading frame araM from Bacillus subtilis. We produced recombinant AraM in Escherichia coli and demonstrate that the purified protein forms a homodimer that reversibly reduces dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. AraM, which constitutes the first identified G1PDH from bacteria, has a similar catalytic efficiency as its archaeal homologues, but its activity is dependent on the presence of Ni (2+) instead of Zn (2+). On the basis of these findings and the analysis of an araM knockout mutant, we propose that AraM generates G1P for the synthesis of phosphoglycerolipids in Gram-positive bacterial species."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.org/dc/terms/identifier"doi:10.1021/bi8005779"xsd:string
http://purl.uniprot.org/citations/18558723http://purl.org/dc/terms/identifier"doi:10.1021/bi8005779"xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/author"Sterner R."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/author"Sterner R."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/author"Babinger P."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/author"Babinger P."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/author"Guldan H."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/author"Guldan H."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/pages"7376-7384"xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/pages"7376-7384"xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/title"Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/title"Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis."xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/volume"47"xsd:string
http://purl.uniprot.org/citations/18558723http://purl.uniprot.org/core/volume"47"xsd:string
http://purl.uniprot.org/citations/18558723http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18558723
http://purl.uniprot.org/citations/18558723http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18558723
http://purl.uniprot.org/citations/18558723http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18558723