5fr9
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of transaminase ATA-117 arRmut11 from Arthrobacter sp. KNK168 inhibited with 1-(4-Bromophenyl)-2-fluoroethylamine== | |
| + | <StructureSection load='5fr9' size='340' side='right' caption='[[5fr9]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fr9]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FR9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FR9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9HC:[4-[3-(4-BROMOPHENYL)-3-OXIDANYLIDENE-PROPYL]-6-METHYL-5-OXIDANYL-PYRIDIN-3-YL]METHYL+PHOSPHATE'>9HC</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-alanine--pyruvate_transaminase Beta-alanine--pyruvate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.18 2.6.1.18] </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=5fr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fr9 OCA], [http://pdbe.org/5fr9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fr9 RCSB], [http://www.ebi.ac.uk/pdbsum/5fr9 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transaminases are valuable enzymes for industrial biocatalysis and enable the preparation of optically pure amines. For these transformations they require either an amine donor (amination of ketones) or an amine acceptor (deamination of racemic amines). Herein transaminases are shown to react with aromatic beta-fluoroamines, thus leading to simultaneous enantioselective dehalogenation and deamination to form the corresponding acetophenone derivatives in the absence of an amine acceptor. A series of racemic beta-fluoroamines was resolved in a kinetic resolution by tandem hydrodefluorination/deamination, thus giving the corresponding amines with up to greater than 99 % ee. This protocol is the first example of exploiting the catalytic promiscuity of transaminases as a tool for novel transformations. | ||
| - | + | Catalytic Promiscuity of Transaminases: Preparation of Enantioenriched beta-Fluoroamines by Formal Tandem Hydrodefluorination/Deamination.,Cuetos A, Garcia-Ramos M, Fischereder EM, Diaz-Rodriguez A, Grogan G, Gotor V, Kroutil W, Lavandera I Angew Chem Int Ed Engl. 2016 Feb;55(9):3144-7. doi: 10.1002/anie.201510554. Epub , 2016 Feb 2. PMID:26836037<ref>PMID:26836037</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5fr9" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-alanine--pyruvate transaminase]] | ||
[[Category: Cuetos, A]] | [[Category: Cuetos, A]] | ||
| - | [[Category: Lavandera, I]] | ||
[[Category: Grogan, G]] | [[Category: Grogan, G]] | ||
| + | [[Category: Kroutil, W]] | ||
| + | [[Category: Lavandera, I]] | ||
| + | [[Category: Aminotransferase]] | ||
| + | [[Category: Fluoroamine]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Plp]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Transminase]] | ||
Revision as of 15:03, 2 March 2016
Structure of transaminase ATA-117 arRmut11 from Arthrobacter sp. KNK168 inhibited with 1-(4-Bromophenyl)-2-fluoroethylamine
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