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| | ==Anaerobic complex of urate oxidase with uric acid== | | ==Anaerobic complex of urate oxidase with uric acid== |
| - | <StructureSection load='3obp' size='340' side='right' caption='[[3obp]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='3obp' size='340' side='right'caption='[[3obp]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3obp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OBP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OBP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3obp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OBP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=URC:URIC+ACID'>URC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=URC:URIC+ACID'>URC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bjp|3bjp]], [[1r4s|1r4s]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3obp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3obp OCA], [https://pdbe.org/3obp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3obp RCSB], [https://www.ebi.ac.uk/pdbsum/3obp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3obp ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uaZ, uox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 ASPFL])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Factor_independent_urate_hydroxylase Factor independent urate hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] </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=3obp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3obp OCA], [http://pdbe.org/3obp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3obp RCSB], [http://www.ebi.ac.uk/pdbsum/3obp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3obp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL]] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. | + | [https://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3obp" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3obp" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspfl]] | + | [[Category: Aspergillus flavus]] |
| - | [[Category: Factor independent urate hydroxylase]] | + | [[Category: Large Structures]] |
| - | [[Category: Castro, B]] | + | [[Category: Castro B]] |
| - | [[Category: Chiadmi, M]] | + | [[Category: Chiadmi M]] |
| - | [[Category: Chopard, C]] | + | [[Category: Chopard C]] |
| - | [[Category: Gabison, L]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Hajji, M El]] | + | [[Category: El Hajji M]] |
| - | [[Category: Prange, T]] | + | [[Category: Gabison L]] |
| - | [[Category: H, N Colloc]] | + | [[Category: Prange T]] |
| - | [[Category: Degradation mechanism]]
| + | |
| - | [[Category: Inhibition]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxisome]]
| + | |
| - | [[Category: Purine metabolism]]
| + | |
| - | [[Category: Uric acid]]
| + | |
| Structural highlights
Function
URIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Publication Abstract from PubMed
Urate oxidase (EC 1.7.3.3 or UOX) catalyzes the conversion of uric acid using gaseous molecular oxygen to 5-hydroxyisourate and hydrogen peroxide in absence of any cofactor or transition metal. The catalytic mechanism was investigated using X-ray diffraction, electron spin resonance spectroscopy (ESR), and quantum mechanics calculations. The X-ray structure of the anaerobic enzyme-substrate complex gives credit to substrate activation before the dioxygen fixation in the peroxo hole, where incoming and outgoing reagents (dioxygen, water, and hydrogen peroxide molecules) are handled. ESR spectroscopy establishes the initial monoelectron activation of the substrate without the participation of dioxygen. In addition, both X-ray structure and quantum mechanic calculations promote a conserved base oxidative system as the main structural features in UOX that protonates/deprotonates and activate the substrate into the doublet state now able to satisfy the Wigner's spin selection rule for reaction with molecular oxygen in its triplet ground state. Proteins 2011; (c) 2011 Wiley-Liss, Inc.
X-ray, ESR, and quantum mechanics studies unravel a spin well in the cofactor-less urate oxidase.,Gabison L, Chopard C, Colloc'h N, Peyrot F, Castro B, Hajji ME, Altarsha M, Monard G, Chiadmi M, Prange T Proteins. 2011 Jun;79(6):1964-76. doi: 10.1002/prot.23022. Epub 2011 Apr, 12. PMID:21491497[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gabison L, Chopard C, Colloc'h N, Peyrot F, Castro B, Hajji ME, Altarsha M, Monard G, Chiadmi M, Prange T. X-ray, ESR, and quantum mechanics studies unravel a spin well in the cofactor-less urate oxidase. Proteins. 2011 Jun;79(6):1964-76. doi: 10.1002/prot.23022. Epub 2011 Apr, 12. PMID:21491497 doi:10.1002/prot.23022
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