title: Functional expression of two forms of rat acyl-CoA oxidase and their substrate specificities.
abstract: Using the reverse transcription of RNA followed by the polymerase chain reaction, we cloned the cDNAs for the rat acyl-CoA oxidases I and II, which are produced by alternative splicing from a single gene, and developed a system for their expression in Escherichia coli. The homogeneous preparations of these enzymes, without proteolytic procession, showed oxidase activity with acyl-CoAs having various acyl-chain lengths. The two types of the enzyme exhibited different substrate specificities with respect to the acyl-chain length, acyl-CoA oxidase I showing the optimum activity at shorter chain-length relative to acyl-CoA oxidase II.
authors.affiliation: Department of Biochemistry, Kumamoto University School of Medicine, Japan.
authors.forename: C
authors.initials: C
authors.lastname: Setoyama
authors.forename: H
authors.initials: H
authors.lastname: Tamaoki
authors.forename: Y
authors.initials: Y
authors.lastname: Nishina
authors.forename: K
authors.initials: K
authors.lastname: Shiga
authors.forename: R
authors.initials: R
authors.lastname: Miura
mesh_terms: D042962:Acyl-CoA Oxidase; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers / Q000737:chemistry; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D017931:DNA Primers; D011994:Recombinant Proteins; D010088:Oxidoreductases; D042962:Acyl-CoA Oxidase