6myw | pdb_00006myw

Gluconobacter Ene-Reductase (GluER) mutant - T36A

spinqualitylabelsall models 6myw, resolution 1.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6myw is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, FMN, GOL, NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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