Ferro A J, Spence K D
J Bacteriol. 1973 Nov;116(2):812-7. doi: 10.1128/jb.116.2.812-817.1973.
Two methionine biosynthetic enzymes and the methionine adenosyltransferase are repressed in Saccharomyces cerevisiae when grown under conditions where the intracellular levels of S-adenosylmethionine are high. The nature of the co-repressor molecule of this repression was investigated by following the intracellular levels of methionine, S-adenosylmethionine, and S-adenosylhomocysteine, as well as enzyme activities, after growth under various conditions. Under all of the conditions found to repress these enzymes, there is an accompanying induction of the S-adenosylmethionine-homocysteine methyltransferase which suggests that this enzyme may play a key role in the regulation of S-adenosylmethionine and methionine balance and synthesis. S-methylmethionine also induces the methyltransferase, but unlike S-adenosylmethionine, it does not repress the methionine adenosyltransferase or other methionine biosynthetic enzymes tested.
当酿酒酵母在细胞内S-腺苷甲硫氨酸水平较高的条件下生长时,两种甲硫氨酸生物合成酶和甲硫氨酸腺苷转移酶会受到抑制。通过在各种条件下培养后跟踪甲硫氨酸、S-腺苷甲硫氨酸和S-腺苷高半胱氨酸的细胞内水平以及酶活性,研究了这种抑制作用的共抑制分子的性质。在所有被发现能抑制这些酶的条件下,都会伴随诱导S-腺苷甲硫氨酸-高半胱氨酸甲基转移酶,这表明该酶可能在S-腺苷甲硫氨酸和甲硫氨酸平衡及合成的调节中起关键作用。S-甲基甲硫氨酸也能诱导甲基转移酶,但与S-腺苷甲硫氨酸不同的是,它不会抑制甲硫氨酸腺苷转移酶或所测试的其他甲硫氨酸生物合成酶。