7PN5
Evolved unspecific peroxygenase with A77L mutation in complex with hexane
Summary for 7PN5
| Entry DOI | 10.2210/pdb7pn5/pdb |
| Related | 5OXU 7PN4 7PN6 7PN7 7PN8 7PN9 7PNA |
| Descriptor | Aromatic peroxygenase, HEXANE, PROTOPORPHYRIN IX CONTAINING FE, ... (8 entities in total) |
| Functional Keywords | hexane complex, peroxygenase, peroxidase, oxidoreductase |
| Biological source | Agrocybe aegerita (Black poplar mushroom, Agaricus aegerita) |
| Total number of polymer chains | 1 |
| Total formula weight | 37818.41 |
| Authors | Fernandez-Garcia, A.,Sanz-Aparicio, J. (deposition date: 2021-09-06, release date: 2023-01-25, Last modification date: 2024-10-23) |
| Primary citation | Gomez de Santos, P.,Gonzalez-Benjumea, A.,Fernandez-Garcia, A.,Aranda, C.,Wu, Y.,But, A.,Molina-Espeja, P.,Mate, D.M.,Gonzalez-Perez, D.,Zhang, W.,Kiebist, J.,Scheibner, K.,Hofrichter, M.,Swiderek, K.,Moliner, V.,Sanz-Aparicio, J.,Hollmann, F.,Gutierrez, A.,Alcalde, M. Engineering a Highly Regioselective Fungal Peroxygenase for the Synthesis of Hydroxy Fatty Acids. Angew.Chem.Int.Ed.Engl., 62:e202217372-e202217372, 2023 Cited by PubMed Abstract: The hydroxylation of fatty acids is an appealing reaction in synthetic chemistry, although the lack of selective catalysts hampers its industrial implementation. In this study, we have engineered a highly regioselective fungal peroxygenase for the ω-1 hydroxylation of fatty acids with quenched stepwise over-oxidation. One single mutation near the Phe catalytic tripod narrowed the heme cavity, promoting a dramatic shift toward subterminal hydroxylation with a drop in the over-oxidation activity. While crystallographic soaking experiments and molecular dynamic simulations shed light on this unique oxidation pattern, the selective biocatalyst was produced by Pichia pastoris at 0.4 g L in a fed-batch bioreactor and used in the preparative synthesis of 1.4 g of (ω-1)-hydroxytetradecanoic acid with 95 % regioselectivity and 83 % ee for the S enantiomer. PubMed: 36583658DOI: 10.1002/anie.202217372 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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