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| | <StructureSection load='5fr9' size='340' side='right'caption='[[5fr9]], [[Resolution|resolution]] 2.81Å' scene=''> | | <StructureSection load='5fr9' size='340' side='right'caption='[[5fr9]], [[Resolution|resolution]] 2.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fr9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Artsp Artsp]. 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://proteopedia.org/fgij/fg.htm?mol=5FR9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fr9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5FR9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9HC:[4-[3-(4-BROMOPHENYL)-3-OXIDANYLIDENE-PROPYL]-6-METHYL-5-OXIDANYL-PYRIDIN-3-YL]METHYL+PHOSPHATE'>9HC</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]] 2.81Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fr9 ProSAT]</span></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=5fr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fr9 OCA], [https://pdbe.org/5fr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fr9 RCSB], [https://www.ebi.ac.uk/pdbsum/5fr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fr9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F7J696_9MICC F7J696_9MICC] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Artsp]] | + | [[Category: Arthrobacter sp]] |
| - | [[Category: Beta-alanine--pyruvate transaminase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cuetos, A]] | + | [[Category: Cuetos A]] |
| - | [[Category: Grogan, G]] | + | [[Category: Grogan G]] |
| - | [[Category: Kroutil, W]] | + | [[Category: Kroutil W]] |
| - | [[Category: Lavandera, I]] | + | [[Category: Lavandera I]] |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Fluoroamine]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Plp]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transminase]]
| + | |
| Structural highlights
Function
F7J696_9MICC
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cuetos A, Garcia-Ramos M, Fischereder EM, Diaz-Rodriguez A, Grogan G, Gotor V, Kroutil W, Lavandera I. Catalytic Promiscuity of Transaminases: Preparation of Enantioenriched beta-Fluoroamines by Formal Tandem Hydrodefluorination/Deamination. Angew Chem Int Ed Engl. 2016 Feb;55(9):3144-7. doi: 10.1002/anie.201510554. Epub , 2016 Feb 2. PMID:26836037 doi:http://dx.doi.org/10.1002/anie.201510554
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