Wagner C, Briggs W T, Cook R J
Biochem Biophys Res Commun. 1985 Mar 29;127(3):746-52. 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.
甘氨酸N-甲基转移酶是一种利用S-腺苷甲硫氨酸使甘氨酸甲基化生成肌氨酸的酶，最近发现它与大鼠肝脏中的一种主要叶酸结合蛋白相同（库克，R.J.和瓦格纳，C.（1984年）《美国国家科学院院刊》81卷，3631 - 3634页）。我们现在提供证据表明，5-甲基四氢蝶酰戊谷氨酸（5-CH3-H4PteGlu5）以高特异性结合，并且是该酶的一种强效抑制剂。有人提出，这一信息可用于修正“甲基陷阱”假说，该假说描述了一碳单位的可用性是如何由叶酸、维生素B12和甲硫氨酸调节的。
