Abstract
| Language | English |
|---|---|
| Pages | 213-216 |
| Number of pages | 3 |
| Journal | FEBS Letters |
| Volume | 503 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 17 Aug 2001 |
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Keywords
- vanillyl-alcohol oxidase
- biocatalysis
- flavoprotein
- medium engineering
- quinone methide
- Penicillium-simplicissimum
- substrate-specificity
- organic- solvents
- 4-alkylphenols
- flavinylation
- catalysis
- mechanism
- enzymes
Cite this
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Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering. / van den Heuvel, R.H.H.; Partridge, J.; Laane, C.; Halling, P.J.; van Berkel, W.J.H.
In: FEBS Letters, Vol. 503, No. 2-3, 17.08.2001, p. 213-216.Research output: Contribution to journal › Article
TY - JOUR
T1 - Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering
AU - van den Heuvel, R.H.H.
AU - Partridge, J.
AU - Laane, C.
AU - Halling, P.J.
AU - van Berkel, W.J.H.
PY - 2001/8/17
Y1 - 2001/8/17
N2 - 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.
AB - 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.
KW - vanillyl-alcohol oxidase
KW - biocatalysis
KW - flavoprotein
KW - medium engineering
KW - quinone methide
KW - Penicillium-simplicissimum
KW - substrate-specificity
KW - organic- solvents
KW - 4-alkylphenols
KW - flavinylation
KW - catalysis
KW - mechanism
KW - enzymes
UR - http://dx.doi.org/10.1016/S0014-5793(01)02658-8
U2 - 10.1016/S0014-5793(01)02658-8
DO - 10.1016/S0014-5793(01)02658-8
M3 - Article
VL - 503
SP - 213
EP - 216
JO - FEBS Letters
T2 - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2-3
ER -