van den Heuvel, R.H.H. and Partridge, J. and Laane, C. and Halling, P.J. and van Berkel, W.J.H. (2001) Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering. FEBS Letters, 503 (2-3). pp. 213-216. ISSN 0014-5793Full text not available in this repository. (Request a copy from the Strathclyde author)
The flavoenzyme vanillyl-alcohol oxidase (VAO) catalyzes the conversion of 4-alkylphenols through the initial formation of p-quinone methide intermediates. These electrophilic species are stereospecifically attacked by water to yield (R)-1-(4'- hydroxyphenyl) alcohols or rearranged in a competing reaction to 1-(4'-hydroxyphenyl)alkenes. Here, we show that the product spectrum of VAO can be controlled by medium engineering. When the enzymatic conversion of 4-propylphenol was performed in organic solvent, the concentration of the alcohol decreased and the concentration of the cis-alkene, but not the trans-alkene, increased. This change in selectivity occurred in both toluene and acetonitrile and was dependent on the water activity of the reaction medium. A similar shift in alcohol/cis-alkene product ratio was observed when the VAO-mediated conversion of 4- propylphenol was performed in the presence of monovalent anions that bind specifically near the enzyme active site. (C) 2001 Federation of European Biochemical Societies.
|Keywords:||vanillyl-alcohol oxidase, biocatalysis, flavoprotein, medium engineering, quinone methide, Penicillium-simplicissimum, substrate-specificity, organic- solvents, 4-alkylphenols, flavinylation, catalysis, mechanism, enzymes, Chemistry, Biochemistry, Structural Biology, Cell Biology, Genetics, Molecular Biology, Biophysics|
|Subjects:||Science > Chemistry|
|Department:||Faculty of Science > Pure and Applied Chemistry|
|Depositing user:||Users 16 not found.|
|Date Deposited:||13 Mar 2006|
|Last modified:||22 Mar 2017 09:07|