Methylenetetrahydrofolate Reductase and Methionine Synthase: Biochemistry and Molecular Biology

Eur. J. Pediatr, 157: Suppl. 2:S54‑S59, 1998

Posted: 12 Jul 2012

See all articles by Christal A. Sheppard

Christal A. Sheppard

University of Nebraska - College of Law

Date Written: 1998

Abstract

Methylenetetrahydrofolate reductase and cobalamin-dependent methionine synthase catalyze the penultimate and ultimate steps in the biosynthesis of methionine in prokaryotes, and are required for the regeneration of the methyl group of methionine in mammals. Defects in either of these enzymes can lead to hyperhomocysteinemia. The sequences of the human methylenetetrahydrofolate reductase and methionine synthase are now known, and show clear homology with their bacterial analogues. Mutations in both enzymes that are known to occur in humans and to be associated with hyperhomocysteinemia affect residues that are conserved in the bacterial enzymes. Structure/function studies on the bacterial proteins, summarized in this review, are therefore relevant to the function of the human enzymes; in particular studies on the effects of bacterial mutations analogous to those causing hyperhomocysteinemia in human may shed light on the defects associated with these mutations.

Suggested Citation

Sheppard, Christal A., Methylenetetrahydrofolate Reductase and Methionine Synthase: Biochemistry and Molecular Biology (1998). Eur. J. Pediatr, 157: Suppl. 2:S54‑S59, 1998. Available at SSRN: https://ssrn.com/abstract=2103762

Christal A. Sheppard (Contact Author)

University of Nebraska - College of Law ( email )

103 McCollum Hall
P.O. Box 830902
Lincoln, NE 68583-0902
United States
4024721250 (Phone)
4024725185 (Fax)

HOME PAGE: http://law.unl.edu/facstaff/faculty/resident/csheppard.shtml

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