6MYW
Gluconobacter Ene-Reductase (GluER) mutant - T36A
Summary for 6MYW
| Entry DOI | 10.2210/pdb6myw/pdb |
| Descriptor | N-ethylmaleimide reductase, FLAVIN MONONUCLEOTIDE, ACETATE ION, ... (7 entities in total) |
| Functional Keywords | g oxydans, old yellow enzyme, lactam cyclase, t36a gluer, oxidoreductase |
| Biological source | Gluconobacter oxydans |
| Total number of polymer chains | 4 |
| Total formula weight | 164588.31 |
| Authors | Garfinkle, S.E.,Jeffrey, P.,Hyster, T.K. (deposition date: 2018-11-02, release date: 2019-06-26, Last modification date: 2023-10-11) |
| Primary citation | Biegasiewicz, K.F.,Cooper, S.J.,Gao, X.,Oblinsky, D.G.,Kim, J.H.,Garfinkle, S.E.,Joyce, L.A.,Sandoval, B.A.,Scholes, G.D.,Hyster, T.K. Photoexcitation of flavoenzymes enables a stereoselective radical cyclization. Science, 364:1166-1169, 2019 Cited by PubMed Abstract: 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. PubMed: 31221855DOI: 10.1126/science.aaw1143 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.157 Å) |
Structure validation
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