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Molecules 2017, 22(6), 1009; doi:10.3390/molecules22061009

Mechanistic Explanation of the Weak Carbonic Anhydrase’s Esterase Activity

Dipartimento di Chimica e Tecnologie Chimiche (CTC), Università della Calabria, 87036 Arcavacata di Rende (CS), Italy
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Received: 10 May 2017 / Revised: 8 June 2017 / Accepted: 13 June 2017 / Published: 18 June 2017
(This article belongs to the Special Issue Metallopeptides)
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Abstract

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. View Full-Text
Keywords: carbonic anhydrase; DFT; enzyme promiscuity; enzyme inhibitors carbonic anhydrase; DFT; enzyme promiscuity; enzyme inhibitors
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Piazzetta, P.; Marino, T.; Russo, N. Mechanistic Explanation of the Weak Carbonic Anhydrase’s Esterase Activity. Molecules 2017, 22, 1009.

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