弱碳酸酐酶酯酶活性的机制解释。

Piazzetta Paolo, Marino Tiziana, Russo Nino

Dipartimento di Chimica e Tecnologie Chimiche (CTC), Università della Calabria, 87036 Arcavacata di Rende (CS), Italy.

Molecules. 2017 Jun 18;22(6):1009. doi: 10.3390/molecules22061009.

In order to elucidate the elementary mechanism of the promiscuous esterase activity of human carbonic anhydrase (h-CA), we present an accurate theoretical investigation on the hydrolysis of fully-acetylated d-glucose functionalized as sulfamate. This h-CA's inhibitor is of potential relevance in cancer therapy. The study has been performed within the framework of three-layer ONIOM (QM-high:QM'-medium:MM-low) hybrid approach. The computations revealed that the hydrolysis process is not energetically favored, in agreement with the observed weak carbonic anhydrase's esterase activity.

为了阐明人类碳酸酐酶（h-CA）混杂酯酶活性的基本机制，我们对作为氨基磺酸盐功能化的全乙酰化d-葡萄糖的水解进行了精确的理论研究。这种h-CA抑制剂在癌症治疗中具有潜在的相关性。该研究是在三层ONIOM（QM高：QM'中：MM低）混合方法的框架内进行的。计算结果表明，水解过程在能量上并不有利，这与观察到的碳酸酐酶的弱酯酶活性一致。