8AUH
Xenobiotic reductase A Y27F variant in complex with ethyl (Z)-2-(hydroxyimino)-3-oxobutanoate
Summary for 8AUH
| Entry DOI | 10.2210/pdb8auh/pdb |
| Descriptor | NADH:flavin oxidoreductase, FLAVIN MONONUCLEOTIDE, ethyl (2Z)-2-hydroxyimino-3-oxidanylidene-butanoate, ... (6 entities in total) |
| Functional Keywords | ene-reductase, complex, oxime, fmn, oxidoreductase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 2 |
| Total formula weight | 83695.88 |
| Authors | Polidori, N.,Gruber, K. (deposition date: 2022-08-25, release date: 2023-03-01, Last modification date: 2024-02-07) |
| Primary citation | Breukelaar, W.B.,Polidori, N.,Singh, A.,Daniel, B.,Glueck, S.M.,Gruber, K.,Kroutil, W. Mechanistic Insights into the Ene-Reductase-Catalyzed Promiscuous Reduction of Oximes to Amines. Acs Catalysis, 13:2610-2618, 2023 Cited by PubMed Abstract: The biocatalytic reduction of the oxime moiety to the corresponding amine group has only recently been found to be a promiscuous activity of ene-reductases transforming α-oximo β-keto esters. However, the reaction pathway of this two-step reduction remained elusive. By studying the crystal structures of enzyme oxime complexes, analyzing molecular dynamics simulations, and investigating biocatalytic cascades and possible intermediates, we obtained evidence that the reaction proceeds an imine intermediate and not the hydroxylamine intermediate. The imine is reduced further by the ene-reductase to the amine product. Remarkably, a non-canonical tyrosine residue was found to contribute to the catalytic activity of the ene-reductase OPR3, protonating the hydroxyl group of the oxime in the first reduction step. PubMed: 36846821DOI: 10.1021/acscatal.2c06137 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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