1w9d

From Proteopedia

Revision as of 11:53, 30 October 2007

S. ALBA MYROSINASE IN COMPLEX WITH S-ETHYL PHENYLACETOTHIOHYDROXIMATE-O-SULFATE

Overview

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.

About this Structure

1W9D is a [Single protein] structure of sequence from [Sinapis alba] with NAG, ZN, SO4, SEH and GOL as [ligands]. Active as [Transferred entry: 3.2.1.147], with EC number [3.2.3.1]. Structure known Active Site: AGB. Full crystallographic information is available from [OCA].

Reference

The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors., Bourderioux A, Lefoix M, Gueyrard D, Tatibouet A, Cottaz S, Arzt S, Burmeister WP, Rollin P, Org Biomol Chem. 2005 May 21;3(10):1872-9. Epub 2005 Apr 14. PMID:15889170

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