Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties

被引：13

作者：

Chang, Wen-Ni ^{[2
]}

Lin, Hung-Chang ^{[1
]}

Fu, Tzu-Fun ^{[1
,2
]}

机构：

[1] Natl Cheng Kung Univ, Coll Med, Dept Med Lab Sci & Biotechnol, Tainan 701, Taiwan

[2] Natl Cheng Kung Univ, Coll Med, Inst Basic Med Sci, Tainan 701, Taiwan

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2010年 / 72卷 / 02期

关键词：

10-Formyltetrahydrofolate dehydrogenase; Folate; Folic acid; Folate-mediated one-carbon metabolism; Zebrafish; Enzyme; SERINE HYDROXYMETHYLTRANSFERASE; HYDROLASE DOMAIN; PURIFICATION; EXPRESSION; FOLATE;

D O I：

10.1016/j.pep.2010.04.003

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：217 / 222

页数：6

共 18 条

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