Schneider G, Lindqvist Y
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden.
Biochim Biophys Acta. 1998 Jun 29;1385(2):387-98. doi: 10.1016/s0167-4838(98)00082-x.
The ThDP dependent enzyme transketolase is a convenient model system to study enzymatic thiamin catalysis. Crystallographic studies of the enzyme have identified the ThDP binding fold, the V-conformation of ThDP as the relevant conformation in enzymatic catalysis and details of enzyme-substrate interactions. Based on this structural information, the function of various active site residues in substrate binding and catalysis has been probed by site-directed mutagenesis.
硫胺素二磷酸（ThDP）依赖性酶转酮醇酶是研究酶促硫胺素催化作用的一个便捷模型系统。对该酶的晶体学研究已确定了ThDP结合结构域、ThDP的V构象为酶促催化中的相关构象以及酶与底物相互作用的细节。基于这些结构信息，已通过定点诱变探究了各个活性位点残基在底物结合和催化中的功能。
