5MQ6
Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila
Summary for 5MQ6
| Entry DOI | 10.2210/pdb5mq6/pdb |
| Descriptor | Pyridine nucleotide-disulfide oxidoreductase-like protein, FLAVIN-ADENINE DINUCLEOTIDE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | flavin, monooxygenase, baeyer-villiger, oxygen, biocatalysis, oxidoreductase |
| Biological source | Myceliophthora thermophila |
| Total number of polymer chains | 1 |
| Total formula weight | 73851.42 |
| Authors | Savino, S.,Furst, M.J.L.J.,Fraaije, M.W.,Mattevi, A. (deposition date: 2016-12-20, release date: 2017-01-11, Last modification date: 2024-10-23) |
| Primary citation | Furst, M.J.,Savino, S.,Dudek, H.M.,Gomez Castellanos, J.R.,Gutierrez de Souza, C.,Rovida, S.,Fraaije, M.W.,Mattevi, A. Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila: A Structurally Distinct Biocatalyst for Bulky Substrates. J. Am. Chem. Soc., 139:627-630, 2017 Cited by PubMed Abstract: Regio- and stereoselective Baeyer-Villiger oxidations are difficult to achieve by classical chemical means, particularly when large, functionalized molecules are to be converted. Biocatalysis using flavin-containing Baeyer-Villiger monooxygenases (BVMOs) is a well-established tool to address these challenges, but known BVMOs have shortcomings in either stability or substrate selectivity. We characterized a novel BVMO from the thermophilic fungus Thermothelomyces thermophila, determined its three-dimensional structure, and demonstrated its use as a promising biocatalyst. This fungal enzyme displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Most notably we observed that the enzyme can perform oxidations on both the A and D ring when converting steroids. These functional properties can be linked to unique structural features, which identify enzymes acting on bulky substrates as a distinct subgroup of the BVMO class. PubMed: 28010060DOI: 10.1021/jacs.6b12246 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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