1344912-75-9Relevant academic research and scientific papers
Multienzyme One-Pot Cascade for the Stereoselective Hydroxyethyl Functionalization of Substituted Phenols
Payer, Stefan E.,Pollak, Hannah,Schmidbauer, Benjamin,Hamm, Florian,Juri?i?, Filip,Faber, Kurt,Glueck, Silvia M.
, p. 5139 - 5143 (2018/09/13)
The operability and substrate scope of a redesigned vinylphenol hydratase as a single biocatalyst or as part of multienzyme cascades using either substituted coumaric acids or phenols as stable, cheap, and readily available substrates are reported.
Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus jostii RHA1: A Versatile Oxidative Biocatalyst
Nguyen, Quoc-Thai,de Gonzalo, Gonzalo,Binda, Claudia,Rioz-Martínez, Ana,Mattevi, Andrea,Fraaije, Marco W.
, p. 1359 - 1366 (2016/08/31)
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.
Asymmetric enzymatic hydration of hydroxystyrene derivatives
Wuensch, Christiane,Gross, Johannes,Steinkellner, Georg,Gruber, Karl,Glueck, Silvia M.,Faber, Kurt
supporting information, p. 2293 - 2297 (2013/04/10)
More than one activity: Owing to their hydratase activity, phenolic acid decarboxylases catalyze the regio- and stereoselective addition of H 2O across the C=C double bond of hydroxystyrene derivatives yielding (S)-4-(1-hydroxyethyl)phenols with up to 82 % conversion and 71 % ee. Based on structure analysis and molecular docking simulations, a catalytic mechanism for this novel enzymatic reaction is proposed. Copyright
