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1: Chem Rec. 2002;2(1):4-12.Click here to read Links

Methylenetetrahydrofolate reductase: a common human polymorphism and its biochemical implications.

Matthews RG.

Biophysics Research Division, The University of Michigan, 930 N. University Avenue, Ann Arbor, Michigan 48109-1055, USA. rmatthew@umich.edu

Methlenetetrahydrofolate (CH2-H4folate) 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 CH2-H4folate into CH3-H4folate, 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. Copyright 2002 The Japan Chemical Journal Forum and John Wiley & Sons, Inc.

PMID: 11933257 [PubMed - indexed for MEDLINE]

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