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7PN9

Evolved unspecific peroxygenase with A77L mutation in complex with lauric acid

Summary for 7PN9
Entry DOI10.2210/pdb7pn9/pdb
Related5OXU 7PN4 7PN5 7PN6 7PN7 7PN8
DescriptorAromatic peroxygenase, PROTOPORPHYRIN IX CONTAINING FE, MAGNESIUM ION, ... (9 entities in total)
Functional Keywordslauric acid complex, peroxygenase, peroxidase, oxidoreductase
Biological sourceAgrocybe aegerita (Black poplar mushroom, Agaricus aegerita)
Total number of polymer chains1
Total formula weight37938.47
Authors
Fernandez-Garcia, A.,Sanz-Aparicio, J. (deposition date: 2021-09-06, release date: 2023-01-25, Last modification date: 2024-11-13)
Primary citationGomez 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: 36583658
DOI: 10.1002/anie.202217372
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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PDB entries from 2024-11-13

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