Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties
Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties
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DOI：
10.1016/j.pep.2010.04.003
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发表时间：
2010-08-01
影响因子：
1.6
通讯作者：
Fu, Tzu-Fun
中科院分区：
文献类型：
--
作者：
Chang, Wen-Ni;Lin, Hung-Chang;Fu, Tzu-Fun
10-斑马鱼的甲酰四氢叶酸脱氢酶已被克隆并在大肠杆菌和酵母中表达。此外，N-末端和C-末端结构域也已被克隆和表达。将每种表达的蛋白质纯化至均一性，并测定结构和动力学性质。这些研究表明，斑马鱼的酶是结构和催化非常相似的酶从哺乳动物来源，这表明，斑马鱼可用于研究体内功能的10-甲酰四氢叶酸脱氢酶。(C)2010年爱思唯尔公司All rights reserved.
10-Formyltetrahydrofolate dehydrogenase from zebrafish has been cloned and expressed in both Escherichia coli and yeast. In addition, the N-terminal and C-terminal domains have also been cloned and expressed. Each expressed protein was purified to homogeneity and structural and kinetic properties determined. These studies show that the zebrafish enzyme is structurally and catalytically very similar to the enzymes from mammalian sources, suggesting that zebrafish can be used to study the in vivo function of 10-formyltetrahydrofolate dehydrogenase. (C) 2010 Elsevier Inc. All rights reserved.