Nagel Zachary D, Klinman Judith P
Department of Chemistry, University of California, Berkeley, California, USA.
Nat Chem Biol. 2009 Aug;5(8):543-50. doi: 10.1038/nchembio.204.
Despite the fact that the number of publications associated with the keyword 'enzyme' increases every year, the precise origin of enzyme catalysis has remained unresolved. Because of sustained intensive research efforts from an increasing number of laboratories, detailed information regarding the physics, chemistry and kinetics of enzymes is accumulating rapidly. The growing body of data contains many examples of kinetic behavior that are incompatible with a static view of enzyme catalysis. As a result, numerous laboratories are approaching the consensus that protein motion plays an essential role in enzyme catalysis. A model that incorporates nuclear quantum tunneling together with two classes of protein motion--termed conformational sampling (pre-organization) and reorganization--is recommended as a means of understanding the large body of data for enzyme-catalyzed hydrogen transfers. It should also serve as a vehicle for future efforts in the development of potent enzyme inhibitors and the de novo design of all classifications of enzymes.
尽管与“酶”这一关键词相关的出版物数量每年都在增加，但酶催化的确切起源仍未得到解决。由于越来越多的实验室持续进行深入研究，有关酶的物理、化学和动力学的详细信息正在迅速积累。不断增加的数据中包含许多与酶催化的静态观点不相容的动力学行为示例。因此，众多实验室逐渐达成共识，即蛋白质运动在酶催化中起着至关重要的作用。一种将核量子隧穿与两类蛋白质运动——称为构象采样（预组织）和重组——相结合的模型，被推荐作为理解大量酶催化氢转移数据的一种方式。它也应成为未来开发强效酶抑制剂以及从头设计各类酶的努力的载体。
