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Vanillate hydroxylase from the white rot basidiomycete Phanerochaete chrysosporium

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Abstract

A soluble enzyme fraction from Phanerochaete chrysosporium catalyzed the oxidative decarboxylation of vanillic acid to methoxy-p-hydroquinone. The enzyme, partially purified by ammonium sulfate precipitation, required NADPH and molecular oxygen for activity. NADH was not effective. Optimal activity was displayed between pH 7.5–8.5. Neither EDTA, KCN, NaN3, nor o-phenanthroline (5 mM) were inhibitory. The enzyme was inducible with maximal activity displayed after incubation of previously grown cells with 0.1% vanillate for 30h.

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Abbreviations

MHQ:

Methoxy-p-hydroquinone

GLC:

gas liquid chromatography

TMSi:

trimethylsilane

TLC:

thin layer chromatography

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Authors and Affiliations

  1. Department of Chemistry and Biochemical Sciences, Oregon Graduate Center, 97005, Beaverton, Oregon, USA

    Yasuo Yajima, Akio Enoki, Mary B. Mayfield & Michael H. Gold

Authors
  1. Yasuo Yajima
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  2. Akio Enoki
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  3. Mary B. Mayfield
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  4. Michael H. Gold
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Yajima, Y., Enoki, A., Mayfield, M.B. et al. Vanillate hydroxylase from the white rot basidiomycete Phanerochaete chrysosporium . Arch. Microbiol. 123, 319–321 (1979). https://doi.org/10.1007/BF00406669

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  • DOI: https://doi.org/10.1007/BF00406669

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