Expression in Escherichia coli, purification and characterization of two mammalian thioesterases involved in fatty acid synthesis.
Expression in Escherichia coli, purification and characterization of two mammalian thioesterases involved in fatty acid synthesis.
复制标题
两种参与脂肪酸合成的哺乳动物硫酯酶在大肠杆菌中的表达、纯化和表征。
DOI：
10.1042/bj2730787
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Smith,S
中科院分区：
文献类型：
--
作者：
Naggert,J;Witkowski,A;Wessa,B;Smith,S
硫酯酶I是多功能脂肪酸合成酶的组成域，硫酯酶II是一种独立的单功能蛋白，分别在长链和中链上催化脂肪酸从头合成的链终止反应。这些酶已被克隆并在温度敏感的λ抑制因子控制下在大肠杆菌中表达。重组蛋白是全长催化活性的硫酯酶，具有与天然酶无异的特异性。
Thioesterase I, a constituent domain of the multifunctional fatty acid synthase, and thioesterase II, an independent monofunctional protein, catalyse the chain-terminating reaction in fatty acid synthesis de novo at long and medium chain lengths respectively. The enzymes have been cloned and expressed in Escherichia coli under the control of the temperature-sensitive lambda repressor. The recombinant proteins are full-length catalytically competent thioesterases with specificities indistinguishable from those of the natural enzymes.