Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver.
3-Hydroxyacyl-CoA dehydrogenase catalyzes the third reaction of fatty acid beta-oxidation spiral. There are three enzymes catalyzing the 3-hydroxyacyl-CoA dehydrogenase, mitochondrial enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein, and peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase 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.
Kobayashi
A
A
Department of Biochemistry, Shinshu University School of Medicine, Nagano.
Jiang
L L
LL
Hashimoto
T
T
D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000214:Acyl Coenzyme A / Q000378:metabolism; D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology; D009928:Organ Specificity; D011487:Protein Conformation; D051381:Rats; D013045:Species Specificity; D013379:Substrate Specificity
D000214:Acyl Coenzyme A; D007527:Isoenzymes; C010667:acetoacetyl CoA; C010701:crotonyl-coenzyme A; D015094:3-Hydroxyacyl CoA Dehydrogenases