| http://purl.uniprot.org/citations/25308280 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25308280 | http://www.w3.org/2000/01/rdf-schema#comment | "Fatty acid ethyl esters are secondary metabolites that are produced during microbial fermentation, in fruiting plants and in higher organisms during ethanol stress. In particular, volatile medium-chain fatty acid ethyl esters are important flavour compounds that impart desirable fruit aromas to fermented beverages, including beer and wine. The biochemical synthesis of medium-chain fatty acid ethyl esters is poorly understood but likely involves acyl-CoA:ethanol O-acyltransferases. Here, we characterize the enzyme ethanol hexanoyl transferase 1 (Eht1) from the brewer's yeast Saccharomyces cerevisiae. Full-length Eht1 was successfully overexpressed from a recombinant yeast plasmid and purified at the milligram scale after detergent solubilization of sedimenting membranes. Recombinant Eht1 was functional as an acyltransferase and, unexpectedly, was optimally active toward octanoyl-CoA, with k(cat) = 0.28 ± 0.02/s and K(M) = 1.9 ± 0.6 μm. Eht1 was also revealed to be active as a thioesterase but was not able to hydrolyse p-nitrophenyl acyl esters, in contrast to the findings of a previous study. Low-resolution structural data and site-directed mutagenesis provide experimental support for a predicted α/β-hydrolase domain featuring a Ser-Asp-His catalytic triad. The S. cerevisiae gene YBR177C/EHT1 should thus be reannotated as coding for an octanoyl-CoA:ethanol acyltransferase that can also function as a thioesterase."xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.org/dc/terms/identifier | "doi:10.1002/yea.3046"xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/author | "Knight M.J."xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/author | "Bull I.D."xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/author | "Curnow P."xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/name | "Yeast"xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/pages | "463-474"xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/title | "The yeast enzyme Eht1 is an octanoyl-CoA:ethanol acyltransferase that also functions as a thioesterase."xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://purl.uniprot.org/core/volume | "31"xsd:string |
| http://purl.uniprot.org/citations/25308280 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25308280 |
| http://purl.uniprot.org/citations/25308280 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25308280 |
| http://purl.uniprot.org/uniprot/#_A0A8H4F7V3-mappedCitation-25308280 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25308280 |
| http://purl.uniprot.org/uniprot/#_P38295-mappedCitation-25308280 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25308280 |
| http://purl.uniprot.org/uniprot/A0A8H4F7V3 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/25308280 |
| http://purl.uniprot.org/uniprot/P38295 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/25308280 |