HOW DO ENZYMES WORK
HOW DO ENZYMES WORK
复制标题
DOI：
10.1126/science.3051385
复制
发表时间：
1988-10-28
期刊：
影响因子：
56.9
通讯作者：
KRAUT, J
中科院分区：
文献类型：
--
作者：
KRAUT, J
过渡态稳定化原理认为，酶催化的发生相当于说酶与过渡态的结合比与基态反应物的结合强得多。概述了这一想法的起源和逐步接受，并回顾了基本过渡态理论。指出了对催化与结合理论的误解导致了人们对催化与结合关系的理解过于简单化，并给出了一个修正的表达式。过渡态结合原理的一些影响，然后探讨。修正后的表达式表明，内部分子动力学也可能在酶催化中发挥作用。虽然这些影响可能不会造成重大影响，但其程度完全未知。最近的进展，由于过渡态结合原理的应用的两个例子进行了审查，一个有关锌蛋白酶的机制和其他催化抗体的产生。
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.