Kochetov G A
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia.
Biochemistry (Mosc). 2001 Oct;66(10):1077-85. doi: 10.1023/a:1012424711871.
Transketolase is the simplest representative of the thiamine diphosphate-dependent enzymes. It was the first of these enzymes for which X-ray analysis was performed. Based on the data of X-ray studies and using the mutagenesis technique, the nature of functional groups of the enzyme involved in the interaction with substrates and cofactors and in the coenzyme activation was defined. Thus, considerable achievements have been made in studying the structure of transketolase. However, there is relatively little information on the conformational flexibility of the enzyme molecule while it is functioning, i.e., during its interaction with cofactors and substrates and in the course of intermediate product formation. This review summarizes mainly the results obtained in the author's group, as well as those rare data on this subject that could be found in literature.
转酮醇酶是硫胺素二磷酸依赖性酶中最简单的代表。它是第一种进行X射线分析的此类酶。基于X射线研究数据并利用诱变技术，确定了该酶中与底物、辅因子相互作用以及辅酶激活所涉及的官能团的性质。因此，在转酮醇酶结构研究方面取得了相当大的成就。然而，关于该酶分子在发挥功能时，即在与辅因子和底物相互作用以及中间产物形成过程中的构象灵活性，相关信息相对较少。本综述主要总结了作者所在团队获得的结果，以及文献中能找到的关于该主题的那些稀少数据。
