Kraut J
University of California, San Diego, La Jolla 92093.
Science. 1988 Oct 28;242(4878):533-40. doi: 10.1126/science.3051385.
The principle of transition-state stabilization asserts that the occurrence of enzymic catalysis is equivalent to saying that an enzyme binds the transition state much more strongly than it binds the ground-state reactants. An outline of the origin and gradual acceptance of this idea is presented, and elementary transition-state theory is reviewed. It is pointed out that a misconception about the theory has led to oversimplification of the accepted expression relating catalysis and binding, and an amended expression is given. Some implications of the transition-state binding principle are then explored. The amended expression suggests that internal molecular dynamics may also play a role in enzymic catalysis. Although such effects probably do not make a major contribution, their magnitude is completely unknown. Two examples of recent advances due to application of the transition-state binding principle are reviewed, one pertaining to the zinc protease mechanism and the other to the generation of catalytic antibodies.
过渡态稳定化原理认为，酶催化的发生等同于说酶与过渡态的结合比与基态反应物的结合要强得多。本文介绍了这一观点的起源及逐渐被接受的过程，并回顾了基本的过渡态理论。指出对该理论的一个误解导致了关于催化与结合的公认表达式被过度简化，进而给出了修正后的表达式。随后探讨了过渡态结合原理的一些影响。修正后的表达式表明，分子内动力学在酶催化中可能也发挥着作用。尽管这种效应可能并非主要贡献因素，但其大小完全未知。本文回顾了因应用过渡态结合原理而取得的两项最新进展，一个涉及锌蛋白酶机制，另一个涉及催化抗体的产生。
