Hersh L B
J Neurochem. 1981 Apr;36(4):1594-6. doi: 10.1111/j.1471-4159.1981.tb00605.x.
Puromycin analogs in which the o-methyl-L-tyrosine moiety was substituted by a number of amino acids were examined as inhibitors of the puromycin-sensitive rat brain aminopeptidase and bovine erythrocyte acetylcholinesterase. In the case of the aminopeptidase, the structure and stereochemistry of the amino acid substituent were important factors in determining inhibitor effectiveness. In the case of the acetylcholinesterase reaction, the aminonucleoside of puromycin was nearly as effective an inhibitor as puromycin itself, with little effect dependent of the nature or stereochemistry of the amino acid.
研究了一系列将邻甲基-L-酪氨酸部分替换为多种氨基酸的嘌呤霉素类似物，作为嘌呤霉素敏感的大鼠脑氨肽酶和牛红细胞乙酰胆碱酯酶的抑制剂。对于氨肽酶而言，氨基酸取代基的结构和立体化学是决定抑制剂有效性的重要因素。对于乙酰胆碱酯酶反应，嘌呤霉素的氨基核苷作为抑制剂的效果几乎与嘌呤霉素本身一样，氨基酸的性质或立体化学对其影响很小。
