Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering

R.H.H. van den Heuvel, J. Partridge, C. Laane, P.J. Halling, W.J.H. van Berkel

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)213-216
Number of pages3
JournalFEBS Letters
Volume503
Issue number2-3
DOIs
Publication statusPublished - 17 Aug 2001

Keywords

  • vanillyl-alcohol oxidase
  • biocatalysis
  • flavoprotein
  • medium engineering
  • quinone methide
  • Penicillium-simplicissimum
  • substrate-specificity
  • organic- solvents
  • 4-alkylphenols
  • flavinylation
  • catalysis
  • mechanism
  • enzymes

Fingerprint Dive into the research topics of 'Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering'. Together they form a unique fingerprint.

  • Cite this

    van den Heuvel, R. H. H., Partridge, J., Laane, C., Halling, P. J., & van Berkel, W. J. H. (2001). Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering. FEBS Letters, 503(2-3), 213-216. https://doi.org/10.1016/S0014-5793(01)02658-8