4c9t
From Proteopedia
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| - | ''' | + | ==BACTERIAL CHALCONE ISOMERASE IN open CONFORMATION FROM EUBACTERIUM RAMULUS AT 2.0 A RESOLUTION, SelenoMet derivative== |
| + | <StructureSection load='4c9t' size='340' side='right' caption='[[4c9t]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4c9t]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C9T FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c9s|4c9s]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chalcone_isomerase Chalcone isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.6 5.5.1.6] </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=4c9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c9t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c9t RCSB], [http://www.ebi.ac.uk/pdbsum/4c9t PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The human fecal anaerobe Eubacterium ramulus is capable of degrading various flavonoids, including the flavone naringenin. The first step in the proposed degradation pathway is the isomerization of naringenin to the corresponding chalcone. Cell-free extracts of E. ramulus displayed chalcone isomerase activity. The enzyme from E. ramulus was purified to homogeneity. Its apparent molecular mass was estimated to be 136 and 129 kDa according to gel filtration and native polyacrylamide gel electrophoresis, respectively. Chalcone isomerase is composed of one type of subunit of 30 kDa. The purified enzyme catalyzed the isomerization of naringenin chalcone, isoliquiritigenin, and butein, three chalcones that differ in their hydroxylation pattern. N-bromosuccinimide, but also naringenin and phloretin, inhibited the purified enzyme considerably. This is the first report on a bacterial chalcone isomerase. The physiological function of the purified enzyme is unclear, but an involvement in the conversion of the flavanone naringenin to the chalcone is proposed. | ||
| - | + | First bacterial chalcone isomerase isolated from Eubacterium ramulus.,Herles C, Braune A, Blaut M Arch Microbiol. 2004 Jun;181(6):428-34. Epub 2004 May 1. PMID:15127184<ref>PMID:15127184</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chalcone isomerase]] | ||
| + | [[Category: Hinrichs, W.]] | ||
| + | [[Category: Palm, G J.]] | ||
| + | [[Category: Thomsen, M.]] | ||
| + | [[Category: Flavonoid]] | ||
| + | [[Category: Isomerase]] | ||
Revision as of 11:35, 22 October 2014
BACTERIAL CHALCONE ISOMERASE IN open CONFORMATION FROM EUBACTERIUM RAMULUS AT 2.0 A RESOLUTION, SelenoMet derivative
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