Michelot R, Legreverend M, Farrugia G, Lederer E
Biochimie. 1976;58(1-2):201-5. doi: 10.1016/s0300-9084(76)80370-7.
New structural analogs of S-adenosyl homocysteine (SAH) 1-9, 11-14, 19-21) and of S-adenosyl methionine (15-18) have been tested as inhibitors of a N-2 guanine methyltransferase extract from rabbit liver with E. coli B tRNA as substrate. The sulfonium compounds (mixture of +/- diastereoisomers) are more inhibitory than the sulfide derivatives but less inhibitory than SAH itself. The replacement of the aminoacid chain in SAH by various alphatic radicals leads to a correlation between their bulk and the size of the enzymatic site. The monosubstitution of N-6 amino group does not affect significantly the inhibitory effect, which is completely canceled by the disubstitution of N-6.
已对S-腺苷高半胱氨酸（SAH）（1-9、11-14、19-21）和S-腺苷甲硫氨酸（15-18）的新型结构类似物作为以大肠杆菌B tRNA为底物的兔肝N-2鸟嘌呤甲基转移酶提取物的抑制剂进行了测试。锍化合物（±非对映异构体混合物）的抑制作用比硫化物衍生物更强，但比SAH本身弱。用各种脂肪族基团取代SAH中的氨基酸链会导致其体积与酶位点大小之间存在相关性。N-6氨基的单取代对抑制作用没有显著影响，但N-6的双取代会完全消除这种抑制作用。
