Methylenetetrahydrofolate Dehydrogenase (MTHFD) Recombinant Proteins are crucial in the study of one-carbon metabolism. MTHFD enzymes play a pivotal role in folate-mediated one-carbon metabolic pathways, which are essential for the synthesis of nucleotides, amino acids, and other biomolecules.
Technical Details
Structure:
- MTHFD enzymes are multi-domain proteins, often existing as monofunctional or trifunctional enzymes with dehydrogenase, cyclohydrolase, and synthetase activities.
- These domains facilitate the conversion of methylenetetrahydrofolate to different folate derivatives.
Production:
- MTHFD recombinant proteins are produced using recombinant DNA technology in systems such as E. coli, yeast, or mammalian cells.
- Recombinant production ensures high purity, activity, and structural integrity of the proteins, suitable for biochemical and functional studies.
Applications:
- Metabolic Pathway Studies:
- Used to study folate metabolism and its regulation.
- Helps elucidate the biochemical pathways involved in nucleotide synthesis and amino acid metabolism.
- Disease Research:
- MTHFD enzymes are linked to disorders like cancer, cardiovascular diseases, and neural tube defects.
- Recombinant proteins enable the study of mutations and polymorphisms affecting enzyme function and their role in disease pathogenesis.
- Drug Development:
- Target for antifolate drugs used in cancer therapy.
- Screening and development of inhibitors that can modulate MTHFD activity.
- Nutritional Studies:
- Understanding the role of folate metabolism in nutrition and the impact of dietary folate on health.
- Studying the effects of folate deficiency and supplementation.
Analytical Methods:
- Enzyme Assays: To measure the activity of dehydrogenase, cyclohydrolase, and synthetase domains.
- Crystallography: For structural determination and understanding enzyme mechanics.
- Mass Spectrometry: To analyze post-translational modifications and protein interactions.
- Western Blotting: For expression analysis in different tissues and conditions.
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