1w9b: Difference between revisions
No edit summary |
No edit summary |
||
| Line 6: | Line 6: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1myr|1myr]], [[1w9d|1w9d]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1myr|1myr]], [[1w9d|1w9d]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioglucosidase Thioglucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.147 3.2.1.147] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioglucosidase Thioglucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.147 3.2.1.147] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w9b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w9b RCSB], [http://www.ebi.ac.uk/pdbsum/1w9b PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w9b OCA], [http://pdbe.org/1w9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w9b RCSB], [http://www.ebi.ac.uk/pdbsum/1w9b PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 26: | Line 26: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1w9b" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:50, 10 September 2015
S. ALBA MYROSINASE IN COMPLEX WITH CARBA-GLUCOTROPAEOLINS. ALBA MYROSINASE IN COMPLEX WITH CARBA-GLUCOTROPAEOLIN
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMyrosinase, 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||