大肠杆菌硫解酶：纯化及链长特异性
Thiolases of Escherichia coli: purification and chain length specificities.
作者信息
Feigenbaum J, Schulz H
出版信息
J Bacteriol. 1975 May;122(2):407-11. doi: 10.1128/jb.122.2.407-411.1975.
Abstract
The presence of only one thiolase (EC 2.3.1.9) in wild-type Escherichia coli induced for enzymes of beta oxidation was demonstrated. A different thiolase was shown to be present in a mutant constitutive for the enzymes of butyrate degradation. The two thiolases were purified to near homogeneity by a simple two-step procedure and were found to be associated with different proteins as shown by gel electrophoresis. The thiolase isolated from induced wild-type Escherichia coli cell was active on beta-ketoacyl-coenzyme A derivatives containing 4 to 16 carbons, but exhibited optimal activity with medium-chain substrates. In contrast, the thiolase isolated from the constitutive mutant was shown to be specific for acetoacetyl-coenzyme A.
摘要
已证实在诱导产生β氧化酶的野生型大肠杆菌中仅存在一种硫解酶（EC 2.3.1.9）。在丁酸降解酶组成型突变体中发现存在一种不同的硫解酶。通过一个简单的两步程序将这两种硫解酶纯化至接近均一状态，并且如凝胶电泳所示，发现它们与不同的蛋白质相关联。从诱导的野生型大肠杆菌细胞中分离出的硫解酶对含4至16个碳的β-酮酰辅酶A衍生物有活性，但对中链底物表现出最佳活性。相比之下，从组成型突变体中分离出的硫解酶显示对乙酰乙酰辅酶A具有特异性。
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