Gleisner J M, Peterson D L, Blakley R L
Proc Natl Acad Sci U S A. 1974 Aug;71(8):3001-5. doi: 10.1073/pnas.71.8.3001.
The amino-acid sequence of dihydrofolate reductase (7,8-dihydrofolate:NADP(+) oxidoreductase, EC 1.5.1.4) from S. faecium var Durans strain A is reported, and methionine residues 28 and 50 are shown to be protected by the inhibitor aminopterin from carboxymethylation by iodoacetate which occurs in absence of the inhibitor. Comparison of the sequence with that of the Escherichia coli reductase reveals two domains of considerable homology, one (the N-terminal region) presumably concerned with dihydrofolate and inhibitor binding and the other with dinucleotide binding. No significant sequence homology was found between larger dehydrogenases and the dihydrofolate reductases, which must, therefore, have evolved from a different ancestral protein.
报道了来自屎肠球菌变种杜兰斯菌株A的二氢叶酸还原酶(7,8 - 二氢叶酸:NADP(+)氧化还原酶,EC 1.5.1.4)的氨基酸序列,并且显示甲硫氨酸残基28和50受到抑制剂氨甲蝶呤的保护,可免受在没有抑制剂时碘乙酸的羧甲基化作用。将该序列与大肠杆菌还原酶的序列进行比较,发现有两个具有相当同源性的结构域,一个(N端区域)可能与二氢叶酸和抑制剂结合有关,另一个与二核苷酸结合有关。在较大的脱氢酶和二氢叶酸还原酶之间未发现明显的序列同源性,因此,二氢叶酸还原酶必定是从不同的祖先蛋白质进化而来的。