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General Comment |
Throughout most of the biological world, tetrahydrofolic acid (THF) serves as the principal carrier of single carbon units in
biosynthetic reactions. Single-carbon derivatives of THF are required in several metabolic pathways, including the biosynthesis
of purines, thymidylate, and certain amino acids and vitamins. During the analysis of liver protein expression in the offspring of
male mice irradiated with fission-spectrum neutrons, Champion et al. (1994) observed one that displayed a heritable 50%
decrease in the abundance of 2 proteins. Through breeding, they obtained homozygous mice lacking detectable quantities of
these proteins. Characterization of the protein deficiency identified the proteins as forms of the enzyme
10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6 ). Homozygous mice appeared completely normal, but breeding pairs of
homozygotes showed a dramatically decreased reproductive efficiency.
NCBI Summary:
Formyltetrahydrofolate dehydrogenase catalyzes the conversion of 10-formyltetrahydrofolate, NADP, and water to tetrahydrofolate, NADPH, and carbon dioxide. The protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies in formyltetrahydrofolate dehydrogenase result in an accumulation of formate and subsequent methanol poisoning. Two transcript variants encoding different isoforms have been found for this gene.
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