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728 of folates in humans.1 Homocysteine is formed in the metabolism of methionine (an amino acid necessary for the proper functioning of the body, supplied in animal proteins), and then is con‐ verted back to methionine in a reaction cat‐ alyzed by methionine synthase, whose coen‐ zyme is 5 ‐methyltetrahydrofolate (the product of the MTHFR ‐catalyzed reaction). S ‐adenosyl‐ methionine is formed from methionine, consti‐ tuting the main source of methyl groups used in the synthesis of nucleic acids, many proteins, and lipid neurotransmitters.2 Homocysteine is finally transformed in a transsulfuration reac‐ tion involving cystathionine β ‐synthase to cys‐ teine and excreted in the urine (FIGURE 1). The de‐ crease in MTHFR activity promotes an increase in total homocysteine (tHcy) in the blood, espe‐ cially in folate deficiency. The MTHFR enzyme is encoded by the gene MTHFR located on chromosome 1 (1p36.22, OMIM 607093, NM_005957). The 2 most common con‐ genital MTHFR polymorphisms in the white pop‐ ulation are MTHFR 677C>T and MTHFR 1298A>C.

Determination and interpretation of MTHFR gene mutations in gynecology and internal medicine