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

8 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.
LanguageEnglish
Pages213-216
Number of pages3
JournalFEBS Letters
Volume503
Issue number2-3
DOIs
Publication statusPublished - 17 Aug 2001

Fingerprint

vanillyl-alcohol oxidase
Alkenes
Tuning
Alcohols
Water
Toluene
Organic solvents
Anions
Catalytic Domain
Enzymes

Keywords

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

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
van den Heuvel, R.H.H. ; Partridge, J. ; Laane, C. ; Halling, P.J. ; van Berkel, W.J.H. / Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering. In: FEBS Letters. 2001 ; Vol. 503, No. 2-3. pp. 213-216.
@article{30db0bbf9f13447292fa69f24362ac5d,
title = "Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering",
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.",
keywords = "vanillyl-alcohol oxidase, biocatalysis, flavoprotein, medium engineering, quinone methide, Penicillium-simplicissimum, substrate-specificity, organic- solvents, 4-alkylphenols, flavinylation, catalysis, mechanism, enzymes",
author = "{van den Heuvel}, R.H.H. and J. Partridge and C. Laane and P.J. Halling and {van Berkel}, W.J.H.",
year = "2001",
month = "8",
day = "17",
doi = "10.1016/S0014-5793(01)02658-8",
language = "English",
volume = "503",
pages = "213--216",
journal = "FEBS Letters",
issn = "0014-5793",
number = "2-3",

}

van den Heuvel, RHH, Partridge, J, Laane, C, Halling, PJ & van Berkel, WJH 2001, 'Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering' FEBS Letters, vol. 503, no. 2-3, pp. 213-216. https://doi.org/10.1016/S0014-5793(01)02658-8

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 journalArticle

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 -