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http://purl.uniprot.org/citations/19586914http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19586914http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19586914http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/19586914http://www.w3.org/2000/01/rdf-schema#comment"The Arabidopsis thaliana locus At5g06580 encodes an ortholog to Saccharomyces cerevisiae d-lactate dehydrogenase (AtD-LDH). The recombinant protein is a homodimer of 59-kDa subunits with one FAD per monomer. A substrate screen indicated that AtD-LDH catalyzes the oxidation of d- and l-lactate, d-2-hydroxybutyrate, glycerate, and glycolate using cytochrome c as an electron acceptor. AtD-LDH shows a clear preference for d-lactate, with a catalytic efficiency 200- and 2000-fold higher than that for l-lactate and glycolate, respectively, and a K(m) value for d-lactate of approximately 160 microm. Knock-out mutants showed impaired growth in the presence of d-lactate or methylglyoxal. Collectively, the data indicated that the protein is a d-LDH that participates in planta in the methylglyoxal pathway. Web-based bioinformatic tools revealed the existence of a paralogous protein encoded by locus At4g36400. The recombinant protein is a homodimer of 61-kDa subunits with one FAD per monomer. A substrate screening revealed highly specific d-2-hydroxyglutarate (d-2HG) conversion in the presence of an organic cofactor with a K(m) value of approximately 580 microm. Thus, the enzyme was characterized as a d-2HG dehydrogenase (AtD-2HGDH). Analysis of knock-out mutants demonstrated that AtD-2HGDH is responsible for the total d-2HGDH activity present in A. thaliana. Gene coexpression analysis indicated that AtD-2HGDH is in the same network as several genes involved in beta-oxidation and degradation of branched-chain amino acids and chlorophyll. It is proposed that AtD-2HGDH participates in the catabolism of d-2HG most probably during the mobilization of alternative substrates from proteolysis and/or lipid degradation."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.021253"xsd:string
http://purl.uniprot.org/citations/19586914http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.021253"xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Engqvist M."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Engqvist M."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Fluegge U.I."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Fluegge U.I."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Drincovich M.F."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Drincovich M.F."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Maurino V.G."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/author"Maurino V.G."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/pages"25026-25037"xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/pages"25026-25037"xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/title"Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and beta-oxidation pathways."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/title"Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and beta-oxidation pathways."xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/volume"284"xsd:string
http://purl.uniprot.org/citations/19586914http://purl.uniprot.org/core/volume"284"xsd:string
http://purl.uniprot.org/citations/19586914http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19586914
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