Methylenetetrahydrofolate reductase

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Function

Methylenetetrahydrofolate reductase (MTHFR) is a regulatory agent of one carbon folate metabolism. The enzyme catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate to be recycled back into the folate cycle, and for aiding folate uptake in the body. This reduction reaction requires the cofactor molecule flavin adenine dinucleotide (FAD) and the second substrate nicotinamide adenine dinucleotide phosphate (NADPH) as the electron donor in the reaction. MTHFR has a unique folding structure. Its N-terminal is abundant in serine and acts as a phosphorylation site, its situated in close proximity to it's C-terminal S-adenosyl methionine (SAM) binding site. A linker joins the catalytic domain (N-terminal) to the regulatory domain (C-terminal) for interaction and increases the sensitivity to SAM binding and feedback properties.

Disease

Association with disease is prevalent with the enzyme. If the human body is deficient of MTHFR, it can result in hyperhomocysteinemia with homocystinuria, or mild hyperhomocysteinemia.

Relevance

Structural highlights

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