4cog: Difference between revisions
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==Crystal structure of kynurenine formamidase from Burkholderia cenocepacia== | ==Crystal structure of kynurenine formamidase from Burkholderia cenocepacia== | ||
<StructureSection load='4cog' size='340' side='right' caption='[[4cog]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4cog' size='340' side='right' caption='[[4cog]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4co9|4co9]], [[4cob|4cob]], [[4cz1|4cz1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4co9|4co9]], [[4cob|4cob]], [[4cz1|4cz1]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arylformamidase Arylformamidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.9 3.5.1.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arylformamidase Arylformamidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.9 3.5.1.9] </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=4cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cog RCSB], [http://www.ebi.ac.uk/pdbsum/4cog 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=4cog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cog OCA], [http://pdbe.org/4cog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cog RCSB], [http://www.ebi.ac.uk/pdbsum/4cog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cog ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 4cog" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:06, 5 August 2016
Crystal structure of kynurenine formamidase from Burkholderia cenocepaciaCrystal structure of kynurenine formamidase from Burkholderia cenocepacia
Structural highlights
Function[KYNB_BURCJ] Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation (By similarity). Publication Abstract from PubMedTryptophan is an important precursor for chemical entities that ultimately support the biosynthesis of key metabolites. The second stage of tryptophan catabolism is catalyzed by kynurenine formamidase, an enzyme that is different between eukaryotes and prokaryotes. Here, we characterize the catalytic properties and present the crystal structures of three bacterial kynurenine formamidases. The structures reveal a new amidase protein fold, a highly organized and distinctive binuclear Zn2+ catalytic centre in a confined, hydrophobic and relatively rigid active site. The structure of a complex with 2-aminoacetophenone delineates aspects of molecular recognition extending to the observation that the substrate itself may be conformationally restricted to assist binding in the confined space of the active site and for subsequent processing. The cations occupy a crowded environment and unlike most Zn2+-dependent enzymes there is little scope to increase coordination number during catalysis. We propose that the presence of a bridging water/hydroxide ligand in conjunction with the placement of an active site histidine supports a distinctive amidation mechanism. Structures of bacterial kynurenine formamidase reveal a crowded binuclear-zinc catalytic site primed to generate a potent nucleophile.,Diaz Saez L, Srikannathasan V, Zoltner M, Hunter WN Biochem J. 2014 Jun 19. PMID:24942958[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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