The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors |
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Authors: | Bourderioux Aurélie Lefoix Myriam Gueyrard David Tatibouét Arnaud Cottaz Sylvain Arzt Steffi Burmeister Wim P Rollin Patrick |
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Affiliation: | Institut de Chimie Organique et Analytique (ICOA), UMR 6005, Université d'Orléans, BP 6759, F-45067, Orléans Cedex 2, France. |
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Abstract: | Myrosinase, a thioglucoside glucohydrolase, is the only enzyme able to hydrolyse glucosinolates, a unique family of molecules bearing an anomeric O-sulfated thiohydroximate function. Non-hydrolysable myrosinase inhibitors have been devised and studied for their biological interaction. Diverse modifications of the O-sulfate moiety did not result in a significant inhibitory effect, whereas replacing the D-glucopyrano residue by its carba-analogue allowed inhibition to take place. X-Ray experiments carried out after soaking allowed for the first time inclusion of a non-hydrolysable inhibitor inside the enzymatic pocket. Structural tuning of the aglycon part in its pocket is being used as a guide for the development of simplified and more potent inhibitors. |
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