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3wgt
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of D-amino acid oxidase mutant== | |
| - | === | + | <StructureSection load='3wgt' size='340' side='right' caption='[[3wgt]], [[Resolution|resolution]] 1.88Å' scene=''> |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3wgt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGT FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </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=3wgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wgt RCSB], [http://www.ebi.ac.uk/pdbsum/3wgt PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://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. | [[http://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: D-amino-acid oxidase]] | [[Category: D-amino-acid oxidase]] | ||
| - | [[Category: Asano, Y | + | [[Category: Pig]] |
| - | [[Category: Nakano, S | + | [[Category: Asano, Y]] |
| - | [[Category: Yasukawa, K | + | [[Category: Nakano, S]] |
| + | [[Category: Yasukawa, K]] | ||
[[Category: Fad-binding]] | [[Category: Fad-binding]] | ||
[[Category: Oxidase]] | [[Category: Oxidase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 20:36, 25 December 2014
Crystal structure of D-amino acid oxidase mutant
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