Bash P A, Field M J, Davenport R C, Petsko G A, Ringe D, Karplus M
Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138.
Biochemistry. 1991 Jun 18;30(24):5826-32. doi: 10.1021/bi00238a003.
A theoretical approach designed for chemical reactions in the condensed phase is used to determine the energy along the reaction path of the enzyme triosephosphate isomerase. The calculations address the role of the enzyme in lowering the barrier to reaction and provide a decomposition into specific residue contributions. The results suggest that, although Lys-12 is most important, many other residues within 16 A of the substrate contribute and that histidine-95 as the imidazole/imidazolate pair could act as an acid/base catalyst.
一种为凝聚相化学反应设计的理论方法被用于确定磷酸丙糖异构酶沿着反应路径的能量。这些计算探讨了该酶在降低反应能垒中的作用，并对特定残基的贡献进行了分解。结果表明，虽然赖氨酸-12最为重要，但底物16埃范围内的许多其他残基也有贡献，并且组氨酸-95作为咪唑/咪唑鎓对可充当酸碱催化剂。
