PUBLICATION

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

Authors
Chang, W.N., Lin, H.C., and Fu, T.F.
ID
ZDB-PUB-100420-10
Date
2010
Source
Protein Expression and Purification   72(2): 217-222 (Journal)
Registered Authors
Chang, Wen-Ni, Fu, Tzu-Fun
Keywords
10-Formyltetrahydrofolate dehydrogenase, Folate, Folic acid, Folate-mediated one-carbon metabolism, Zebrafish, Enzyme
MeSH Terms
  • Aldehydes
  • Animals
  • Cell Line
  • Chromatography, Affinity
  • Chromatography, Gel
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli/genetics
  • Female
  • Humans
  • Isoenzymes/chemistry
  • Isoenzymes/genetics
  • Isoenzymes/metabolism
  • Leucovorin/analogs & derivatives
  • Leucovorin/metabolism
  • Male
  • Oxidoreductases Acting on CH-NH Group Donors/chemistry*
  • Oxidoreductases Acting on CH-NH Group Donors/genetics
  • Oxidoreductases Acting on CH-NH Group Donors/metabolism*
  • Pichia/genetics
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Recombinant Proteins/chemistry
  • Recombinant Proteins/genetics
  • Recombinant Proteins/metabolism
  • Zebrafish
PubMed
20381623 Full text @ Protein Expr. Purif.
Abstract
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.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping