| http://purl.uniprot.org/citations/7592843 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7592843 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7592843 | http://www.w3.org/2000/01/rdf-schema#comment | "Escherichia coli galactoside acetyltransferase (GAT) is a member of a large family of acetyltransferases that O-acetylate dissimilar substrates but share limited sequence homology. Steady-state kinetic analysis of over-expressed GAT demonstrated that it accepted a range of substrates, including glucosides and lactosides which were acetylated at rates comparable to galactosides. GAT was shown to be a trimeric acetyltransferase by cross-linking with dimethyl suberimidate. Fluorometric analysis of coenzyme A binding showed that there is a fluorescence quench associated with acetyl-CoA binding whereas CoA has no effect. This difference was exploited to measure dissociation rates for both CoA and acetyl-CoA by stopped-flow fluorometry. The rate of dissociation of CoA (2500 s-1) is at least 170-fold faster than kcat for any substrate tested. The fluorescence response to acetyl-CoA binding is entirely due to Trp-139 since replacement by phenylalanine completely abolished the fluorescence quench. Treatment of GAT by [14C]iodoacetamide resulted in complete inactivation of the enzyme and the incorporation of label into histidyl and cysteinyl residues to approximately equal extents. Following replacement of His-115 by alanine, label was incorporated solely into cysteinyl residues. Furthermore, the substitution results in an 1800-fold decrease in kcat suggesting that His-115 has an important catalytic role in GAT."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.270.44.26326"xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.270.44.26326"xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/author | "Ellis J."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/author | "Ellis J."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/author | "Shaw W.V."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/author | "Shaw W.V."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/author | "Lewendon A."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/author | "Lewendon A."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/pages | "26326-26331"xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/pages | "26326-26331"xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/title | "Structural and mechanistic studies of galactoside acetyltransferase, the Escherichia coli LacA gene product."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/title | "Structural and mechanistic studies of galactoside acetyltransferase, the Escherichia coli LacA gene product."xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/volume | "270"xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://purl.uniprot.org/core/volume | "270"xsd:string |
| http://purl.uniprot.org/citations/7592843 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7592843 |
| http://purl.uniprot.org/citations/7592843 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7592843 |
| http://purl.uniprot.org/citations/7592843 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7592843 |
| http://purl.uniprot.org/citations/7592843 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7592843 |