Furuta S, Miyazawa S, Osumi T, Hashimoto T, Ui N
J Biochem. 1980 Oct;88(4):1059-70. doi: 10.1093/oxfordjournals.jbchem.a133057.
Mitochondrial and peroxisomal enoyl-CoA hydratases were purified from rat liver. The mitochondrial enzyme, with a molecular weight of 161,000, was composed of 6 identical subunits. The molecular structure of the rat liver enzyme was very similar to that of the bovine liver enzyme. Acetoacetyl-CoA was a competitive inhibitor of the mitochondrial enzymes. The results of titration of the rat liver enzyme with acetoacetyl-CoA suggest that 3 subunits of the enzyme exhibit catalytic activity. The catalytic properties of the enzyme were studied. The peroxisomal enzyme was composed of one polypeptide with a molecular weight of 70,000-81,000. Some of the enzyme molecules were shown to be cleaved to two polypeptides in the cell by the following methods: amino acid analysis, peptide mapping and immunoprecipitin reaction. The catalytic properties of the peroxisomal enzyme were different from those of the mitochondrial enzyme. The peroxisomal enzyme is a bifunctional enzyme exhibiting 3-hydroxyacyl-CoA dehydrogenase activity. Studies on the titration with acetoacetyl-CoA, the effects of salts, SH titration and proteolytic inactivation suggest that the active centers for these two reactions are located at different sites.
从大鼠肝脏中纯化出线粒体和过氧化物酶体烯酰辅酶A水合酶。线粒体酶分子量为161,000，由6个相同亚基组成。大鼠肝脏酶的分子结构与牛肝脏酶非常相似。乙酰乙酰辅酶A是线粒体酶的竞争性抑制剂。用乙酰乙酰辅酶A滴定大鼠肝脏酶的结果表明，该酶的3个亚基具有催化活性。对该酶的催化特性进行了研究。过氧化物酶体酶由一条分子量为70,000 - 81,000的多肽组成。通过氨基酸分析、肽图分析和免疫沉淀反应等方法表明，部分酶分子在细胞内被裂解为两条多肽。过氧化物酶体酶的催化特性与线粒体酶不同。过氧化物酶体酶是一种具有3-羟酰基辅酶A脱氢酶活性的双功能酶。用乙酰乙酰辅酶A滴定、盐的影响、巯基滴定和蛋白水解失活的研究表明，这两个反应的活性中心位于不同位点。
