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http://purl.uniprot.org/citations/23770562http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23770562http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23770562http://www.w3.org/2000/01/rdf-schema#comment"Reductases convert some achiral ketone compounds into chiral alcohols, which are important materials for the synthesis of chiral drugs. The Saccharomyces cerevisiae reductase YOR120W converts ethyl-4-chloro-3-oxobutanoate (ECOB) enantioselectively into (R)-ethyl-4-chloro-3-hydroxybutanoate ((R)-ECHB), an intermediate of a pharmaceutical. As YOR120W requires NADPH as a cofactor for the reduction reaction, a cofactor recycling system using Bacillus subtilis glucose dehydrogenase was employed. Using this coupling reaction system, 100 mM ECOB was converted to (R)-ECHB. A homology modeling and site-directed mutagenesis experiment were performed to determine the NADPH-binding site of YOR120W. Four residues (Q29, K264, N267, and R270) were suggested by homology and docking modeling to interact directly with 2'-phosphate of NADPH. Among them, two positively charged residues (K264 and R270) were experimentally demonstrated to be necessary for NADPH 2'-phosphate binding. A mutant enzyme (Q29E) showed an enhanced enantiomeric excess value compared with that of the wild-type enzyme."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.org/dc/terms/identifier"doi:10.4014/jmb.1305.05030"xsd:string
http://purl.uniprot.org/citations/23770562http://purl.org/dc/terms/identifier"doi:10.4014/jmb.1305.05030"xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/author"Kim H.K."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/author"Kim H.K."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/author"Yoon S.A."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/author"Yoon S.A."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/name"J. Microbiol. Biotechnol."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/name"J. Microbiol. Biotechnol."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/pages"1395-1402"xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/pages"1395-1402"xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/title"Development of a bioconversion system using Saccharomyces cerevisiae reductase YOR120W and Bacillus subtilis glucose dehydrogenase for chiral alcohol synthesis."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/title"Development of a bioconversion system using Saccharomyces cerevisiae reductase YOR120W and Bacillus subtilis glucose dehydrogenase for chiral alcohol synthesis."xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/23770562http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/23770562http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23770562
http://purl.uniprot.org/citations/23770562http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23770562
http://purl.uniprot.org/citations/23770562http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23770562
http://purl.uniprot.org/citations/23770562http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23770562
http://purl.uniprot.org/uniprot/P14065http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23770562
http://purl.uniprot.org/uniprot/P14065#attribution-E3EFB55F16E5B84800E709EDBFBDE659http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23770562