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http://purl.uniprot.org/citations/2199330http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2199330http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2199330http://www.w3.org/2000/01/rdf-schema#comment"Genes argD and ARG8, encoding the acetylornithine aminotransferase (ACOAT) subunit in Escherichia coli and Saccharomyces cerevisiae, respectively, have been cloned and sequenced. The deduced amino acid sequences show substantial similarity. Moreover, they resemble ornithine aminotransferase (OAT) sequences (i.e., those from yeast, rat and man); the observed similarities are statistically significant, indicating that the enzymes are homologous. However, in contrast to OATs, which appear to be substrate (i.e., ornithine)-specific, S. cerevisiae ACOAT transaminates ornithine about as efficiently as E. coli does. The evolutionary relationship between ACOATs and OATs is discussed in terms of substrate ambiguity."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.org/dc/terms/identifier"doi:10.1016/0378-1119(90)90440-3"xsd:string
http://purl.uniprot.org/citations/2199330http://purl.org/dc/terms/identifier"doi:10.1016/0378-1119(90)90440-3"xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Glansdorff N."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Glansdorff N."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Boyen A."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Boyen A."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Crabeel M."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Crabeel M."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Heimberg H."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/author"Heimberg H."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/name"Gene"xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/name"Gene"xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/pages"69-78"xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/pages"69-78"xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/title"Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/title"Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase."xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/volume"90"xsd:string
http://purl.uniprot.org/citations/2199330http://purl.uniprot.org/core/volume"90"xsd:string
http://purl.uniprot.org/citations/2199330http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2199330
http://purl.uniprot.org/citations/2199330http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2199330