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http://purl.uniprot.org/citations/8020470http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8020470http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8020470http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/8020470http://www.w3.org/2000/01/rdf-schema#comment"The (R)- and (S)-isomers of alpha-methyl-branched fatty acids were shown to be rapidly interconverted as coenzyme A thioesters, by an alpha-methylacyl-CoA racemase. The enzyme was purified some 5600-fold from rat liver, to apparent homogeneity. It is a monomer of 45 kDa with an isolectric point of pH 6.1 and is optimally active between pH 6 and pH 7. It acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA and trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), but neither 3-methyl-branched nor linear-chain acyl-CoAs. The racemase catalyzes a rapid exchange of the H atom in the alpha-position of the fatty acid against a proton from water, indicating that the mechanism involves abstraction of a proton. Based on this observation, a very sensitive and convenient radiometric assay, with 2-methyl[2-(3)H]acyl-CoAs as substrates, was developed. The enzyme was inactivated by micromolar concentrations of Hg2+ and to a lesser extent by Cu2+ but not by iodoacetamide and only slightly by N-ethylmaleimide and thimerosal."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1994.tb18870.x"xsd:string
http://purl.uniprot.org/citations/8020470http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1994.tb18870.x"xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/author"Conzelmann E."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/author"Conzelmann E."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/author"Schmitz W."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/author"Schmitz W."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/author"Fingerhut R."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/author"Fingerhut R."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/pages"313-323"xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/pages"313-323"xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/title"Purification and properties of an alpha-methylacyl-CoA racemase from rat liver."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/title"Purification and properties of an alpha-methylacyl-CoA racemase from rat liver."xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/volume"222"xsd:string
http://purl.uniprot.org/citations/8020470http://purl.uniprot.org/core/volume"222"xsd:string
http://purl.uniprot.org/citations/8020470http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8020470
http://purl.uniprot.org/citations/8020470http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8020470
http://purl.uniprot.org/citations/8020470http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8020470