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http://purl.uniprot.org/citations/11934293http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11934293http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11934293http://www.w3.org/2000/01/rdf-schema#comment"An NADPH-dependent enzyme that reduces ethyl 2-methylacetoacetate stereoselectively to ethyl (2R)-methyl-(3S)-hydroxybutanoate was purified 730-fold from Escherichia coli. The N-terminal amino acid sequence data obtained from the purified reductase were used to search the E. coli genome, and a single match was found at the start of the yqhE open reading frame. The YqhE protein had been identified previously by Yum et al. as a 2,5-diketo-D-gluconate reductase on the basis of sequence similarity to other bacterial homologues [Yum, D.-Y.; Lee, B.-Y.; Pan, J.-G. Appl.Environ. Microbiol. 1999, 65, 3341-3346]; however, it had not been examined for beta-keto ester reductions. Our results thus link a key enzyme in the microbial production of ascorbate with stereoselective beta-keto ester reductions, two important fields in biocatalysis. The purified YqhE reductase accepts ethyl acetoacetate and a variety of 2-substituted derivatives, and its sequence is similar to other aldose reductase superfamily members that also reduce alpha-substituted beta-keto esters to syn-(2R,3S) alcohols."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.org/dc/terms/identifier"doi:10.1021/bp0101841"xsd:string
http://purl.uniprot.org/citations/11934293http://purl.org/dc/terms/identifier"doi:10.1021/bp0101841"xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/author"Rodriguez S."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/author"Rodriguez S."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/author"Habrych M."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/author"Habrych M."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/author"Stewart J.D."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/author"Stewart J.D."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/name"Biotechnol. Prog."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/name"Biotechnol. Prog."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/pages"257-261"xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/pages"257-261"xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/title"Purification and identification of an Escherichia coli beta-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/title"Purification and identification of an Escherichia coli beta-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE."xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/11934293http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/11934293http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11934293
http://purl.uniprot.org/citations/11934293http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11934293
http://purl.uniprot.org/citations/11934293http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11934293
http://purl.uniprot.org/citations/11934293http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11934293