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http://purl.uniprot.org/citations/23110853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23110853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23110853http://www.w3.org/2000/01/rdf-schema#comment"Hydroxyacid dehydrogenases, responsible for the stereospecific conversion of 2-keto acids to 2-hydroxyacids in lactic acid producing bacteria, have a range of biotechnology applications including antibiotic synthesis, flavor development in dairy products and the production of valuable synthons. The genome of Lactobacillus delbrueckii ssp. bulgaricus, a member of the heterogeneous group of lactic acid bacteria, encodes multiple hydroxyacid dehydrogenases whose structural and functional properties remain poorly characterized. Here, we report the apo and coenzyme NAD⁺ complexed crystal structures of the L. bulgaricusD-isomer specific 2-hydroxyacid dehydrogenase, D2-HDH. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.org/dc/terms/identifier"doi:10.1016/j.jsb.2012.10.009"xsd:string
http://purl.uniprot.org/citations/23110853http://purl.org/dc/terms/identifier"doi:10.1016/j.jsb.2012.10.009"xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Wilmanns M."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Wilmanns M."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Anandhakrishnan M."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Anandhakrishnan M."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Holton S.J."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Holton S.J."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Geerlof A."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/author"Geerlof A."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/name"J. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/name"J Struct Biol"xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/pages"179-184"xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/pages"179-184"xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/title"Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/title"Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus."xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/volume"181"xsd:string
http://purl.uniprot.org/citations/23110853http://purl.uniprot.org/core/volume"181"xsd:string
http://purl.uniprot.org/citations/23110853http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23110853
http://purl.uniprot.org/citations/23110853http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23110853