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http://purl.uniprot.org/citations/3611054http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3611054http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3611054http://www.w3.org/2000/01/rdf-schema#comment"cDNA encoding the precursor of rat liver medium chain acyl-CoA dehydrogenase (EC 1.3.99.3) was cloned and sequenced. The longest cDNA insert isolated was 1866 bases in length. This cDNA encodes the entire protein of 421-amino acids including a 25-amino acid leader peptide and a 396-amino acid mature polypeptide. The identity of the medium chain acyl-CoA dehydrogenase clone was confirmed by matching the amino acid sequence predicted from the cDNA to the NH2-terminal and nine internal tryptic peptide sequences derived from pure rat liver medium chain acyl-CoA dehydrogenase. The calculated molecular masses of the precursor medium chain acyl-CoA dehydrogenase, the mature medium chain acyl-CoA dehydrogenase, and the leader peptide are 46,600, 43,700, and 2,900 daltons, respectively. The leader peptide contains five basic amino acids and only one acidic amino acid; thus, it is positively charged, overall. Cysteine residues are unevenly distributed in the mature portion of the protein; five of six are found within the NH2-terminal half of the polypeptide. Comparison of medium chain acyl-CoA dehydrogenase sequence to other flavoproteins and enzymes which act on coenzyme A ester substrates did not lead to unambiguous identification of a possible FAD-binding site nor a coenzyme A-binding domain. The sequencing of other homologous acyl-CoA dehydrogenases will be informative in this regard."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)61083-x"xsd:string
http://purl.uniprot.org/citations/3611054http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)61083-x"xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Matsubara Y."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Matsubara Y."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Ikeda Y."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Ikeda Y."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Finocchiaro G."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Finocchiaro G."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Glassberg R."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Glassberg R."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Kraus J.P."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Kraus J.P."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Mole J."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Mole J."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Ozasa H."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Ozasa H."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Rosenberg L.E."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/author"Rosenberg L.E."xsd:string
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3611054http://purl.uniprot.org/core/date"1987"xsd:gYear