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Methylenetetrahydrofolate reductase: A common human polymorphism and its biochemical implications
Author(s) -
Matthews Rowena G.
Publication year - 2002
Publication title -
the chemical record
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.61
H-Index - 78
eISSN - 1528-0691
pISSN - 1527-8999
DOI - 10.1002/tcr.10006
Subject(s) - methylenetetrahydrofolate reductase , methionine , homocysteine , valine , alanine , biochemistry , genetics , purine , reductase , biology , gene , enzyme , chemistry , amino acid , allele
Methlenetetrahydrofolate (CH 2 ‐H 4 folate) is required for the conversion of homocysteine to methionine and of dUMP to dTMP in support of DNA synthesis, and also serves as a major source of one carbon unit for purine biosynthesis. This review presents biochemical studies of a human polymorphism in methylenetetrahydrofolate reductase, which catalyzes the reaction shown below. The mutation decreases the flux of CH 2 ‐H 4 folate into CH 3 ‐H 4 folate, and is associated with both beneficial and deleterious effects that can be traced to the molecular effect of the substitution of alanine 222 by valine. © 2002 The Japan Chemical Journal Forum and John Wiley & Sons, Inc. Chem Rec 2: 4–12, 2002
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