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6o08
From Proteopedia
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<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=6o08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o08 OCA], [http://pdbe.org/6o08 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o08 RCSB], [http://www.ebi.ac.uk/pdbsum/6o08 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o08 ProSAT]</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=6o08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o08 OCA], [http://pdbe.org/6o08 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o08 RCSB], [http://www.ebi.ac.uk/pdbsum/6o08 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o08 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Photoexcitation is a common strategy for initiating radical reactions in chemical synthesis. We found that photoexcitation of flavin-dependent "ene"-reductases changes their catalytic function, enabling these enzymes to promote an asymmetric radical cyclization. This reactivity enables the construction of five-, six-, seven-, and eight-membered lactams with stereochemical preference conferred by the enzyme active site. After formation of a prochiral radical, the enzyme guides the delivery of a hydrogen atom from flavin-a challenging feat for small-molecule chemical reagents. The initial electron transfer occurs through direct excitation of an electron donor-acceptor complex that forms between the substrate and the reduced flavin cofactor within the enzyme active site. Photoexcitation of promiscuous flavoenzymes has thus furnished a previously unknown biocatalytic reaction. | ||
| + | |||
| + | Photoexcitation of flavoenzymes enables a stereoselective radical cyclization.,Biegasiewicz KF, Cooper SJ, Gao X, Oblinsky DG, Kim JH, Garfinkle SE, Joyce LA, Sandoval BA, Scholes GD, Hyster TK Science. 2019 Jun 21;364(6446):1166-1169. doi: 10.1126/science.aaw1143. PMID:31221855<ref>PMID:31221855</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6o08" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:55, 3 July 2019
Gluconobacter Ene-Reductase (GluER)
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