Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver

A Kobayashi, LL Jiang… - The journal of …, 1996 - academic.oup.com
A Kobayashi, LL Jiang, T Hashimoto
The journal of biochemistry, 1996academic.oup.com
Hydroxyacyl-CoA dehydrogenase catalyzes the third reaction of fatty acid β-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 …
Abstract
3-Hydroxyacyl-CoA dehydrogenase catalyzes the third reaction of fatty acid β-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.
Oxford University Press