1W9D
S. alba myrosinase in complex with S-ethyl phenylacetothiohydroximate- O-sulfate
Summary for 1W9D
| Entry DOI | 10.2210/pdb1w9d/pdb |
| Related | 1MYR 1W9B |
| Descriptor | GLYCOSIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-xylopyranose-(1-2)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | thioglucosidase, thioglycosidase, myrosinase, hydrolase, thio-glucoside, thiohydroximate, glusosinolate, glucotropaeolin |
| Biological source | SINAPIS ALBA (WHITE MUSTARD) |
| Total number of polymer chains | 1 |
| Total formula weight | 62309.50 |
| Authors | Bourderioux, A.,Lefoix, M.,Gueyrard, D.,Tatibouet, A.,Cottaz, S.,Arzt, S.,Burmeister, W.P.,Rollin, P. (deposition date: 2004-10-08, release date: 2005-05-19, Last modification date: 2024-10-23) |
| Primary citation | Bourderioux, A.,Lefoix, M.,Gueyrard, D.,Tatibouet, A.,Cottaz, S.,Arzt, S.,Burmeister, W.P.,Rollin, P. The Glucosinolate-Myrosinase System. New Insights Into Enzyme-Substrate Interactions by Use of Simplified Inhibitors Org.Biomol.Chem., 3:1872-, 2005 Cited by PubMed 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. PubMed: 15889170DOI: 10.1039/B502990B PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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