{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nancolas B"],"funding":["European Research Council","Natural Environment Research Council","Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["239-251"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5484351"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(6)"],"pubmed_abstract":["The alcohol-O-acyltransferases are bisubstrate enzymes that catalyse the transfer of acyl chains from an acyl-coenzyme A (CoA) donor to an acceptor alcohol. In the industrial yeast Saccharomyces cerevisiae this reaction produces acyl esters that are an important influence on the flavour of fermented beverages and foods. There is also a growing interest in using acyltransferases to produce bulk quantities of acyl esters in engineered microbial cell factories. However, the structure and function of the alcohol-O-acyltransferases remain only partly understood. Here, we recombinantly express, purify and characterize Atf1p, the major alcohol acetyltransferase from S. cerevisiae. We find that Atf1p is promiscuous with regard to the alcohol cosubstrate but that the acyltransfer activity is specif"],"journal":["Yeast (Chichester, England)"],"pubmed_title":["Saccharomyces cerevisiae Atf1p is an alcohol acetyltransferase and a thioesterase in vitro."],"pmcid":["PMC5484351"],"funding_grant_id":["EP/K03927X/1","R8/H10/63","BB/L01386X/1","EP/L016648/1","282101"],"pubmed_authors":["Stenner R","Curnow P","Dufour V","Nancolas B","Bull ID"],"additional_accession":[]},"is_claimable":false,"name":"Saccharomyces cerevisiae Atf1p is an alcohol acetyltransferase and a thioesterase in vitro.","description":"The alcohol-O-acyltransferases are bisubstrate enzymes that catalyse the transfer of acyl chains from an acyl-coenzyme A (CoA) donor to an acceptor alcohol. In the industrial yeast Saccharomyces cerevisiae this reaction produces acyl esters that are an important influence on the flavour of fermented beverages and foods. There is also a growing interest in using acyltransferases to produce bulk quantities of acyl esters in engineered microbial cell factories. However, the structure and function of the alcohol-O-acyltransferases remain only partly understood. Here, we recombinantly express, purify and characterize Atf1p, the major alcohol acetyltransferase from S. cerevisiae. We find that Atf1p is promiscuous with regard to the alcohol cosubstrate but that the acyltransfer activity is specif","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Jun","modification":"2025-04-22T16:34:23.143Z","creation":"2019-03-27T02:48:28Z"},"accession":"S-EPMC5484351","cross_references":{"pubmed":["28160314"],"doi":["10.1002/yea.3229"]}}