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http://purl.uniprot.org/citations/17030441http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17030441http://www.w3.org/2000/01/rdf-schema#comment"An alpha,beta-dicarbonyl reductase activity was purified from Saccharomyces cerevisiae and identified as the cytosolic enzyme D-Arabinose dehydrogenase (ARA1) by MALDI-TOF/TOF. Size exclusion chromatography analysis of recombinant Ara1p revealed that this protein formed a homodimer. Ara1p catalyzed the reduction of the reactive alpha,beta-dicarbonyl compounds methylglyoxal, diacetyl, and pentanedione in a NADPH dependant manner. Ara1p had apparent Km values of approximately 14 mM, 7 mM and 4 mM for methylglyoxal, diacetyl and pentanedione respectively, with corresponding turnover rates of 4.4, 6.9 and 5.9 s(-1) at pH 7.0. pH profiling showed that Ara1p had a pH optimum of 4.5 for the diacetyl reduction reaction. Ara1p also catalyzed the NADP+ dependant oxidation of acetoin; however this back reaction only occurred at alkaline pH values. That Ara1p was important for degradation of alpha,beta-dicarbonyl substrates was further supported by the observation that ara1-Delta knockout yeast mutants exhibited a decreased growth rate phenotype in media containing diacetyl."xsd:string
http://purl.uniprot.org/citations/17030441http://purl.org/dc/terms/identifier"doi:10.1016/j.bbagen.2006.08.025"xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/author"Jardim A."xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/author"Strasser R."xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/author"Cyr N."xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/author"Sheppard J.D."xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/author"van Bergen B."xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/name"Biochim Biophys Acta"xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/pages"1636-1645"xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/title"Alpha,beta-dicarbonyl reduction by Saccharomyces D-arabinose dehydrogenase."xsd:string
http://purl.uniprot.org/citations/17030441http://purl.uniprot.org/core/volume"1760"xsd:string
http://purl.uniprot.org/citations/17030441http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17030441
http://purl.uniprot.org/citations/17030441http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17030441
http://purl.uniprot.org/uniprot/#_A0A6A5Q1Y8-mappedCitation-17030441http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17030441
http://purl.uniprot.org/uniprot/#_P38115-mappedCitation-17030441http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17030441
http://purl.uniprot.org/uniprot/A0A6A5Q1Y8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17030441
http://purl.uniprot.org/uniprot/P38115http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17030441