Inhibition of glycine N-methyltransferase activity by folate derivatives: implications for regulation of methyl group metabolism.

Wagner C, Briggs WT, Cook RJ
Biochem Biophys Res Commun. 1985 127 (3): 746-52

PMID: 3838667 · DOI:10.1016/s0006-291x(85)80006-1

Glycine N-methyltransferase, an enzyme that uses S-adenosylmethionine to methylate glycine with the production of sarcosine, was recently shown to be identical with a major folate binding protein of rat liver (Cook, R.J. and Wagner, C. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 3631-3634). We now present evidence that 5-methyltetrahydropteroylpentaglutamate (5-CH3-H4PteGlu5) is bound with high specificity, and is a powerful inhibitor of the enzyme. It is proposed that this information may be used to modify the "methyl trap" hypothesis which describes how the availability of one-carbon units is regulated by folate, vitamin B12 and methionine.

MeSH Terms (10)

Animals Binding, Competitive Folic Acid Glycine N-Methyltransferase Male Methyltransferases Pteroylpolyglutamic Acids Rats Rats, Inbred Strains Tetrahydrofolates

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