Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties.
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.
Chang
Wen-Ni
WN
Institute of Basic Medical Science, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Lin
Hung-Chang
HC
Fu
Tzu-Fun
TF
D000447:Aldehydes; D000818:Animals; D002460:Cell Line; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D005260:Female; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002955:Leucovorin / Q000031:analogs & derivatives / Q000378:metabolism; D008297:Male; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010843:Pichia / Q000235:genetics; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015027:Zebrafish; D000099295:Formyltetrahydrofolate Dehydrogenase
D000447:Aldehydes; D007527:Isoenzymes; D002955:Leucovorin; D000587:Oxidoreductases Acting on CH-NH Group Donors; D011994:Recombinant Proteins; D000099295:Formyltetrahydrofolate Dehydrogenase; C010161:10-formyltetrahydropteroylglutamic acid; C005556:propionaldehyde