A mode of substrate-recognition mechanism by an enzayme, arylmalonate decarboxylase, is proposed. 19F- and 31P-NMR spectra of a complex consisting of the enzyme and an active site-directed inhibitor demonstrated that a hydrophobic interaction between the enzyme and its substrate via their aromatic rings was especially important for the enzyme function.
提出了一种酶、芳基
丙二酸脱羧酶的底物识别机制模式。由酶和活性位点定向
抑制剂组成的复合物的 19F-和 31P-NMR 谱表明,酶与其底物之间通过芳香环的疏
水相互作用对于酶功能尤其重要。