4OVI
Phenylacetone monooxygenase: oxidised enzyme in complex with APADP
Summary for 4OVI
| Entry DOI | 10.2210/pdb4ovi/pdb |
| Descriptor | Phenylacetone monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, 3-ACETYLPYRIDINE ADENINE DINUCLEOTIDE, ... (8 entities in total) |
| Functional Keywords | flavin, cofactor, baeyer-villiger, oxidoreductase |
| Biological source | Thermobifida fusca |
| Total number of polymer chains | 1 |
| Total formula weight | 63053.16 |
| Authors | Martinoli, C.,Fraaije, M.W.,Mattevi, A. (deposition date: 2013-09-19, release date: 2014-05-28, Last modification date: 2023-09-27) |
| Primary citation | Martinoli, C.,Dudek, H.M.,Orru, R.,Edmondson, D.E.,Fraaije, M.W.,Mattevi, A. Beyond the Protein Matrix: Probing Cofactor Variants in a Baeyer-Villiger Oxygenation Reaction. Acs Catalysis, 3:3058-3062, 2013 Cited by PubMed Abstract: A general question in biochemistry is the interplay between the chemical properties of cofactors and the surrounding protein matrix. Here, the functions of NADP and FAD are explored by investigation of a representative monooxygenase reconstituted with chemically-modified cofactor analogues. Like pieces of a jigsaw puzzle, the enzyme active site juxtaposes the flavin and nicotinamide rings, harnessing their H-bonding and steric properties to finely construct an oxygen-reacting center that restrains the flavin-peroxide intermediate in a catalytically-competent orientation. Strikingly, the regio- and stereoselectivities of the reaction are essentially unaffected by cofactor modifications. These observations indicate a remarkable robustness of this complex multi-cofactor active site, which has implications for enzyme design based on cofactor engineering approaches. PubMed: 24443704DOI: 10.1021/cs400837z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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