Functional expression of two forms of rat acyl-CoA oxidase and their substrate specificities.
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.
Setoyama
C
C
Department of Biochemistry, Kumamoto University School of Medicine, Japan.
Tamaoki
H
H
Nishina
Y
Y
Shiga
K
K
Miura
R
R
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
D017931:DNA Primers; D011994:Recombinant Proteins; D010088:Oxidoreductases; D042962:Acyl-CoA Oxidase