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http://purl.uniprot.org/citations/8093000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8093000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8093000http://www.w3.org/2000/01/rdf-schema#comment"Acyl-CoA-binding protein (ACBP) is a 10 kDa protein characterized in vertebrates. We have isolated two ACBP homologues from the yeast Saccharomyces carlsbergensis, named yeast ACBP types 1 and 2. Both proteins contain 86 amino acid residues and are identical except for four conservative substitutions. In comparison with human ACBP, yeast ACBPs exhibit 48% (type 1) and 49% (type 2) conservation of amino acid residues. The amino acid sequence of S. carlsbergensis ACBP type 1 was found to be identical with the one ACBP present in Saccharomyces cerevisiae. A recombinant form of this protein was expressed in Escherichia coli and S. cerevisiae, purified, and its acyl-CoA-binding properties were characterized by isoelectric focusing and microcalorimetric analyses. The yeast ACBP was found to bind acyl-CoA esters with high affinity (Kd 0.55 x 10(-10) M). Overexpression of yeast ACBP in S. cerevisiae resulted in a significant expansion of the intracellular acyl-CoA pool. Finally, Southern-blotting analysis of the two genes encoding ACBP types 1 and 2 in S. carlsbergensis strongly indicated that this species is a hybrid between S. cerevisiae and Saccharomyces monacensis."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.org/dc/terms/identifier"doi:10.1042/bj3020479"xsd:string
http://purl.uniprot.org/citations/8093000http://purl.org/dc/terms/identifier"doi:10.1042/bj3020479"xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Andersen J.S."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Andersen J.S."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Roepstorff P."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Roepstorff P."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Hoejrup P."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Hoejrup P."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Knudsen J."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Knudsen J."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Boersting C."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Boersting C."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Faergeman N.J."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Faergeman N.J."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Hummel R."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Hummel R."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Kristiansen K."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Kristiansen K."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Rose T.M."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Rose T.M."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Skoett H."xsd:string
http://purl.uniprot.org/citations/8093000http://purl.uniprot.org/core/author"Skoett H."xsd:string