Easy as pi: Trp612 stabilizes the intermediary cation through a cation–π interaction. Leu734 and the π electrons of Tyr736 are perpendicular to the ligand. Tight CH–π complexation between Tyr736 and Leu734 and another between Val483 and Trp534 confer a robust local protein architecture and fix the ligand in a normal folding conformation, thus leading to a high degree of enzyme activity.

中文翻译：

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大戟大戟β-Amyrin环化酶中严格保守的残基：Trp612通过Tyr736与Leu734的阳离子-π相互作用和CH-π相互作用稳定了瞬态阳离子，从而提供了稳健的局部蛋白质结构

像pi一样容易：Trp612通过阳离子-π相互作用稳定中间阳离子。Leu734和Tyr736的π电子垂直于配体。Tyr736和Leu734之间的紧密CH-π络合物以及Val483和Trp534之间的紧密CH-π络合物赋予了稳健的局部蛋白质结构，并将配体固定在正常的折叠构象中，从而导致高度的酶活性。