Implication of a peroxisomal enzyme in the catabolism of glutaryl-CoA.
Implication of a peroxisomal enzyme in the catabolism of glutaryl-CoA.
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过氧化物酶体酶在戊二酰辅酶A分解代谢中的意义。
DOI：
10.1042/bj2210203
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
VanHoof,F
中科院分区：
文献类型：
--
作者：
Vamecq,J;VanHoof,F
当戊二酰辅酶A与肝匀浆孵育时，发现H2 O2产生的线性速率。我们称这种酶活性为戊二酰辅酶A氧化酶。描述了该酶的主要特性，并与戊二酰辅酶A脱氢酶（EC 1.3.99.7）和棕榈酰辅酶A氧化酶（EC 1.1.3.-）的特性进行了比较。后一种酶催化过氧化物酶体β-氧化的第一步。戊二酰辅酶A氧化酶与棕榈酰辅酶A氧化酶具有几种相同的性质。小鼠肝脏中两种酶的活性通过用含氯贝酯的饮食喂养动物而增加。在线性蔗糖梯度上的肝匀浆的亚细胞分级表明戊二酰辅酶A氧化酶是过氧化物酶体酶。
A linear rate of H2O2 production is found when glutaryl-CoA is incubated with liver homogenates. We term this enzyme activity glutaryl-CoA oxidase. Its main characteristics are described and compared with those of glutaryl-CoA dehydrogenase (EC 1.3.99.7) and palmitoyl-CoA oxidase (EC 1.1.3.-). The latter enzyme catalyses the first step of peroxisomal beta-oxidation. Glutaryl-CoA oxidase shares several properties with palmitoyl-CoA oxidase. The activities of both enzymes in mouse liver are increased by feeding the animals with a clofibrate-containing diet. Subcellular fractionation of the liver homogenates on a linear sucrose gradient indicates that glutaryl-CoA oxidase is a peroxisomal enzyme.