The glucosinolate-myrosinase system.: New insights into enzyme-substrate interactions by use of simplied inhibitors

被引:27
作者
Bourderioux, A
Lefoix, M
Gueyrard, D
Tatibouët, A
Cottaz, S
Arzt, S
Burmeister, WP
Rollin, P
机构
[1] Univ Orleans, ICOA, UMR 6005, F-45067 Orleans, France
[2] Univ Grenoble 1, CERMAV, CNRS, F-38041 Grenoble, France
[3] European Synchrotron Radiat Facil, F-38043 Grenoble, France
[4] UJF, CNRS, Inst Univ France, Lab Virol Mol & Struct,FRE 2854, F-38042 Grenoble, France
[5] EMBL, Grenoble Outstn, F-38042 Grenoble, France
关键词
D O I
10.1039/b502990b
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
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.
引用
收藏
页码:1872 / 1879
页数:8
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