8VCN
GluER mutant - W66F F269Y Q293T F68Y T36E P263L
Summary for 8VCN
| Entry DOI | 10.2210/pdb8vcn/pdb |
| Related | 6MYW |
| Descriptor | N-ethylmaleimide reductase, ACETATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | g oxydans, old yellow enzyme, lactam cyclase, gluer mutant, oxidoreductase |
| Biological source | Gluconobacter oxydans |
| Total number of polymer chains | 1 |
| Total formula weight | 40943.69 |
| Authors | Jeffrey, P.D.,Sorigue, D.R.,Liu, Y.,Hyster, T.K. (deposition date: 2023-12-14, release date: 2024-03-13, Last modification date: 2024-03-27) |
| Primary citation | Liu, Y.,Bender, S.G.,Sorigue, D.,Diaz, D.J.,Ellington, A.D.,Mann, G.,Allmendinger, S.,Hyster, T.K. Asymmetric Synthesis of alpha-Chloroamides via Photoenzymatic Hydroalkylation of Olefins. J.Am.Chem.Soc., 146:7191-7197, 2024 Cited by PubMed Abstract: Photoenzymatic intermolecular hydroalkylations of olefins are highly enantioselective for chiral centers formed during radical termination but poorly selective for centers set in the C-C bond-forming event. Here, we report the evolution of a flavin-dependent "ene"-reductase to catalyze the coupling of α,α-dichloroamides with alkenes to afford α-chloroamides in good yield with excellent chemo- and stereoselectivity. These products can serve as linchpins in the synthesis of pharmaceutically valuable motifs. Mechanistic studies indicate that radical formation occurs by exciting a charge-transfer complex templated by the protein. Precise control over the orientation of molecules within the charge-transfer complex potentially accounts for the observed stereoselectivity. The work expands the types of motifs that can be prepared using photoenzymatic catalysis. PubMed: 38442365DOI: 10.1021/jacs.4c00927 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
Download full validation report
