An unexpectedly efficient catalytic antibody operating by ping-pong and induced fit mechanisms.
An unexpectedly efficient catalytic antibody operating by ping-pong and induced fit mechanisms.
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一种出人意料的高效催化抗体，通过乒乓球和诱导契合机制发挥作用。
DOI：
10.1126/science.2024120
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Lerner,RA
中科院分区：
文献类型：
--
作者：
Wirsching,P;Ashley,JA;Benkovic,SJ;Janda,KD;Lerner,RA
一种过渡态类似物被用来生产一种在水中催化酯交换反应的小鼠抗体。该抗体是一种高效的催化剂，具有共价中间体和诱导配对的特性。虽然催化途径的一些特征是在设计半抗原时编程的，反映了良好的底物-抗体相互作用，但其他特征是抗体多样性的化学潜力的表现。抗体概括了以前被认为是高度进化的酶的一个特征的机制和途径，这一事实表明，一旦获得了适当的结合腔，就会出现与蛋白质的内在化学势相称的反应途径。
A transition state analogue was used to produce a mouse antibody that catalyzes transesterification in water. The antibody behaves as a highly efficient catalyst with a covalent intermediate and the characteristic of induced fit. While some features of the catalytic pathway were programmed when the hapten was designed and reflect favorable substrate-antibody interactions, other features are a manifestation of the chemical potential of antibody diversity. The fact that antibodies recapitulate mechanisms and pathways previously thought to be a characteristic of highly evolved enzymes suggests that once an appropriate binding cavity is achieved, reaction pathways commensurate with the intrinsic chemical potential of proteins ensue.