J. Biochem, 1996, Vol. 119, No. 4 775-782
© 1996 Japanese Biochemical Society
research-article |
Two Mitochondrial 3-Hydroxyacyl-CoA Dehydrogenases in Bovine Liver1
Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390
2To whom correspondence should be addressed. Tel: + 81-263-35-4600 (Ext 5180), Fax: +81-263-33-6458
3-Hydroxyacyl-CoA dehydrogenase catalyzes the third reaction of fatty acid ß-oxidation spiral. There are three enzymes catalyzing the 3-hydroxyacyl-CoA dehydrogenase reaction: mitochondrial monofunctional 3-hydroxyacly-CoA dehydrogenase, mitochondrial enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase tri-functional protein, and peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein. The presence of isozymes of monofunctional 3-hydroxyacyl-CoA dehydrogenase was not known. In the present study, two monofunctional mitochondrial 3-hydroxyacyl-CoA dehydrogenases were purified from bovine liver. Type I enzyme was composed of two identical subunits with molecular mass of 35 kDa, and type II enzyme was a homotetramer of a 28 kDa polypeptide. In respect to the molecular structures, immunochemical properties, and carbon chain length specificities of acyl-CoA substrates, type I enzyme was the same as the well-known classical enzyme purified from various tissues, but type II enzyme was concluded to be a new enzyme. Type I enzyme was ubiquitous, but type II enzyme was rich in bovine and sheep, of several animal livers so far examined.
1This work was supported in part by Grant-in-Aid (06454175) for scientific research from the Ministry of Education, Science, Sports and Culture of Japan and a Research Grant for the Intractable Diseases from the Ministry of Health and Welfare of Japan.
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