Impaired functioning of thermolabile methylenetetrahydrofolate reductase is dependent on riboflavin status: implications for riboflavin requirements
Author(s) -
Helene McNulty,
Michelle C. McKinley,
Barbara J. Wilson,
Joseph McPartlin,
JJ Strain,
Donald G. Weir,
John M. Scott
Publication year - 2002
Publication title -
american journal of clinical nutrition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.608
H-Index - 336
eISSN - 1938-3207
pISSN - 0002-9165
DOI - 10.1093/ajcn/76.2.436
Subject(s) - methylenetetrahydrofolate reductase , thermolabile , riboflavin , homocysteine , reductase , medicine , b vitamins , genotype , flavin adenine dinucleotide , vitamin , chemistry , endocrinology , biochemistry , cofactor , biology , enzyme , gene
Methylenetetrahydrofolate reductase (MTHFR; EC 1.7.99.5) supplies the folate needed for the metabolism of homocysteine. A reduction in MTHFR activity, as occurs in the homozygous state for the 677C-->T (so-called thermolabile) enzyme variant (TT genotype), is associated with an increase in plasma total homocysteine (tHcy).
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