大鼠4-羟基苯丙酮酸双加氧酶的C末端对于酶活性是不可或缺的。
The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity.
作者信息
Lee M H, Zhang Z H, MacKinnon C H, Baldwin J E, Crouch N P
机构信息
Dyson Perrins Laboratory, University of Oxford, UK.
出版信息
FEBS Lett. 1996 Sep 16;393(2-3):269-72. doi: 10.1016/0014-5793(96)00902-7.
We have cloned and overexpressed rat 4-hydroxyphenylpyruvate dioxygenase (4HPPD) in Escherichia coli. The soluble, active recombinant enzyme was shown to contain both 4HPPD and alpha-ketoisocaproate dioxygenase (alpha KICD) activity. However, upon truncation of the 14 amino acids at the C-terminus by site-directed mutagenesis, the resulting mutant enzyme (rat F antigen) exhibited complete loss of 4HPPD and alpha KICD activities. This finding suggests that the C-terminal extension domain plays an essential role in the catalytic activity of the enzyme.
我们已在大肠杆菌中克隆并过量表达了大鼠4-羟基苯丙酮酸双加氧酶（4HPPD）。可溶性的活性重组酶显示同时具有4HPPD和α-酮异己酸双加氧酶（αKICD）活性。然而，通过定点诱变在C末端截短14个氨基酸后，所得突变酶（大鼠F抗原）表现出4HPPD和αKICD活性完全丧失。这一发现表明C末端延伸结构域在该酶的催化活性中起关键作用。
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