An "artificial enzyme" combining a metal catalytic group and a hydrophobic binding cavity.
An "artificial enzyme" combining a metal catalytic group and a hydrophobic binding cavity.
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DOI：
10.1021/ja00707a062
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发表时间：
1970-02
影响因子：
15
通讯作者：
R. Breslow;L. Overman
中科院分区：
文献类型：
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作者：
R. Breslow;L. Overman
对番茄碱样品进行部分降解，定位14C标记位点。分离的降解产物如图2所示。从番茄碱的活性样品中获得的这些产物的相对比活度见表1。用[3H， 14C]-球铁碱进行的实验中，番茄碱的3H: 14C比例与前体相匹配，这与番茄碱是球铁碱改性二聚体的假设相一致。[2-14C]球铁碱在番茄碱（苯甲酸）的C-5位点上没有活性。这个假说要求这个部位有50%的活性。很明显，番茄碱分子的C8单元，包括C-5（即Cl -8），不是以预测的方式从球铁碱中衍生出来的。由于源自[2-14C]球铁碱的所有活性都局限于7-甲基- 5,6,7,8 -四氢喹啉（C-7 -16）所代表的分子部分，因此，
The lycopodine samples were partially degraded to locate the sites of 14C labeling. The degradation prod-ucts which were isolated are shown in Scheme II. 6 The relative specific activities of these products, ob-tained from the active samples of lycopodine, are presented in Table I.The recovery, from the experiment with [3H, 14C]-pelletierine, of lycopodine whose 3H: 14C ratio matched that of the precursor was consistent with the hypothesis that lycopodine is a modified dimer of pelletierine. The absence of activity derived from [2-14C] pelletierine at C-5 of lycopodine (benzoic acid) was not, however. The hypothesis demands 50% of activity at this site. It is evident that the C8 unit of the lycopodine molecule which includes C-5 (ie, Cl to-8) is not derived from pelletierine in the predicted manner. Since all activity derived from [2-14C] pelletierine was confined to the portion of the molecule represented by 7-methyl-5, 6, 7, 8-tetrahydroquinoline (C-7 to-16), it seemed likely that,