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 language | English |
|---|---|
| Pages (from-to) | 213-216 |
| Number of pages | 3 |
| Journal | FEBS Letters |
| Volume | 503 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 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