4D03
Structure of the Cys65Asp mutant of phenylacetone monooxygenase: oxidised state
Summary for 4D03
| Entry DOI | 10.2210/pdb4d03/pdb |
| Related | 4CZZ 4D04 |
| Descriptor | PHENYLACETONE MONOOXYGENASE, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, biocatalysis |
| Biological source | THERMOBIFIDA FUSCA |
| Total number of polymer chains | 1 |
| Total formula weight | 63579.34 |
| Authors | Brondani, P.B.,Dudek, H.M.,Martinoli, C.,Mattevi, A.,Fraaije, M.W. (deposition date: 2014-04-24, release date: 2014-12-10, Last modification date: 2023-12-20) |
| Primary citation | Brondani, P.B.,Dudek, H.M.,Martinoli, C.,Mattevi, A.,Fraaije, M.W. Finding the Switch: Turning a Baeyer-Villiger Monooxygenase Into a Nadph Oxidase. J.Am.Chem.Soc., 136:16966-, 2014 Cited by PubMed Abstract: By a targeted enzyme engineering approach, we were able to create an efficient NADPH oxidase from a monooxygenase. Intriguingly, replacement of only one specific single amino acid was sufficient for such a monooxygenase-to-oxidase switch-a complete transition in enzyme activity. Pre-steady-state kinetic analysis and elucidation of the crystal structure of the C65D PAMO mutant revealed that the mutation introduces small changes near the flavin cofactor, resulting in a rapid decay of the peroxyflavin intermediate. The engineered biocatalyst was shown to be a thermostable, solvent tolerant, and effective cofactor-regenerating biocatalyst. Therefore, it represents a valuable new biocatalytic tool. PubMed: 25423359DOI: 10.1021/JA508265B PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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