2fxl: Difference between revisions
New page: left|200px<br /><applet load="2fxl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fxl, resolution 1.76Å" /> '''Urate oxidase from a... |
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[[Image:2fxl.gif|left|200px]]<br /><applet load="2fxl" size=" | [[Image:2fxl.gif|left|200px]]<br /><applet load="2fxl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fxl, resolution 1.76Å" /> | caption="2fxl, resolution 1.76Å" /> | ||
'''Urate oxidase from aspergillus flavus complexed with allantoin'''<br /> | '''Urate oxidase from aspergillus flavus complexed with allantoin'''<br /> | ||
==Overview== | ==Overview== | ||
Urate oxidase from Aspergillus flavus catalyzes the degradation of uric | Urate oxidase from Aspergillus flavus catalyzes the degradation of uric acid to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate. The second degradation step is thought either catalyzed by another specific enzyme, or spontaneous. The structure of the enzyme was known at high resolution by X-ray diffraction of I222 crystals complexed with a purine-type inhibitor (8-azaxanthin). Analyzing the X-ray structure of urate oxidase treated with an excess of urate, the natural substrate, shows unexpectedly that the active site recaptures [S]-allantoin from the racemic end product of a second degradation step. | ||
==About this Structure== | ==About this Structure== | ||
2FXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with 2AL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http:// | 2FXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with <scene name='pdbligand=2AL:'>2AL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Chiadmi, M.]] | [[Category: Chiadmi, M.]] | ||
[[Category: Gabison, L.]] | [[Category: Gabison, L.]] | ||
[[Category: H, N | [[Category: H, N Colloc.]] | ||
[[Category: Prange, T.]] | [[Category: Prange, T.]] | ||
[[Category: 2AL]] | [[Category: 2AL]] | ||
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[[Category: uric acid degradation]] | [[Category: uric acid degradation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:06 2008'' |
Revision as of 18:26, 21 February 2008
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Urate oxidase from aspergillus flavus complexed with allantoin
OverviewOverview
Urate oxidase from Aspergillus flavus catalyzes the degradation of uric acid to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate. The second degradation step is thought either catalyzed by another specific enzyme, or spontaneous. The structure of the enzyme was known at high resolution by X-ray diffraction of I222 crystals complexed with a purine-type inhibitor (8-azaxanthin). Analyzing the X-ray structure of urate oxidase treated with an excess of urate, the natural substrate, shows unexpectedly that the active site recaptures [S]-allantoin from the racemic end product of a second degradation step.
About this StructureAbout this Structure
2FXL is a Single protein structure of sequence from Aspergillus flavus with as ligand. Active as Urate oxidase, with EC number 1.7.3.3 Full crystallographic information is available from OCA.
ReferenceReference
Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase., Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T, FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:16545381
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