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| ==Crystal structure of D-amino acid oxidase mutant== | | ==Crystal structure of D-amino acid oxidase mutant== |
| <StructureSection load='3wgt' size='340' side='right'caption='[[3wgt]], [[Resolution|resolution]] 1.88Å' scene=''> | | <StructureSection load='3wgt' size='340' side='right'caption='[[3wgt]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3wgt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WGT FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WGT FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=QSC:(1R)-1-PHENYLETHANAMINE'>QSC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | | </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=3wgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgt OCA], [https://pdbe.org/3wgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wgt RCSB], [https://www.ebi.ac.uk/pdbsum/3wgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgt ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgt OCA], [https://pdbe.org/3wgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wgt RCSB], [https://www.ebi.ac.uk/pdbsum/3wgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgt ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function ==
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| [[https://www.uniprot.org/uniprot/OXDA_PIG OXDA_PIG]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The deracemization of racemic amines to yield enantioenriched amines using S-stereoselective amine oxidases (AOx) has recently been attracting attention. However, R-stereoselective AOx that are suitable for deracemization have not yet been identified. An R-stereoselective AOx was now evolved from porcine kidney D-amino acid oxidase (pkDAO) and subsequently use for the deracemization of racemic amines. The engineered pkDAO, which was obtained by directed evolution, displayed a markedly changed substrate specificity towards R amines. The mutant enzyme exhibited a high preference towards the substrate alpha-methylbenzylamine and was used to synthesize the S amine through deracemization. The findings of this study indicate that further investigations on the structure-activity relationship of AOx are warranted and also provide a new method for biotransformations in organic synthesis.
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| Tailoring D-Amino Acid Oxidase from the Pig Kidney to R-Stereoselective Amine Oxidase and its Use in the Deracemization of alpha-Methylbenzylamine.,Yasukawa K, Nakano S, Asano Y Angew Chem Int Ed Engl. 2014 Mar 18. doi: 10.1002/anie.201308812. PMID:24644036<ref>PMID:24644036</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3wgt" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]] | | *[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: D-amino-acid oxidase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Asano, Y]] | | [[Category: Asano Y]] |
| [[Category: Nakano, S]] | | [[Category: Nakano S]] |
| [[Category: Yasukawa, K]] | | [[Category: Yasukawa K]] |
| [[Category: Fad-binding]]
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| [[Category: Oxidase]]
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| [[Category: Oxidoreductase]]
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