5FXE
Crystal structure of eugenol oxidase in complex with coniferyl alcohol
Summary for 5FXE
Entry DOI | 10.2210/pdb5fxe/pdb |
Related | 5FXD 5FXF 5FXP |
Descriptor | EUGENOL OXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enal, ... (5 entities in total) |
Functional Keywords | oxidoreductase, biocatalysis, selective oxidation, kinetic resolution, oxidases, eugenol |
Biological source | RHODOCOCCUS JOSTII RHA1 |
Total number of polymer chains | 2 |
Total formula weight | 119956.82 |
Authors | Nguyen, Q.-T.,de Gonzalo, G.,Binda, C.,Martinez, A.R.,Mattevi, A.,Fraaije, M.W. (deposition date: 2016-03-01, release date: 2016-07-27, Last modification date: 2024-10-09) |
Primary citation | Nguyen, Q.,De Gonzalo, G.,Binda, C.,Rioz-Martinez, A.,Mattevi, A.,Fraaije, M.W. Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus Jostii Rha1: A Versatile Oxidative Biocatalyst. Chembiochem, 17:1359-, 2016 Cited by PubMed Abstract: Eugenol oxidase (EUGO) from Rhodococcus jostii RHA1 had previously been shown to convert only a limited set of phenolic compounds. In this study, we have explored the biocatalytic potential of this flavoprotein oxidase, resulting in a broadened substrate scope and a deeper insight into its structural properties. In addition to the oxidation of vanillyl alcohol and the hydroxylation of eugenol, EUGO can efficiently catalyze the dehydrogenation of various phenolic ketones and the selective oxidation of a racemic secondary alcohol-4-(1-hydroxyethyl)-2-methoxyphenol. EUGO was also found to perform the kinetic resolution of a racemic secondary alcohol. Crystal structures of the enzyme in complexes with isoeugenol, coniferyl alcohol, vanillin, and benzoate have been determined. The catalytic center is a remarkable solvent-inaccessible cavity on the si side of the flavin cofactor. Structural comparison with vanillyl alcohol oxidase from Penicillium simplicissimum highlights a few localized changes that correlate with the selectivity of EUGO for phenolic substrates bearing relatively small p-substituents while tolerating o-methoxy substituents. PubMed: 27123962DOI: 10.1002/CBIC.201600148 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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