A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone

Research output: Contribution to journal › Article › Research › peer review

Authors

  • Marco A. Fraatz
  • Stephanie J.L. Riemer
  • Regina Stöber
  • Rüdiger Kaspera
  • Manfred Nimtz
  • Ralf G. Berger
  • Holger Zorn

Research Organisations

External Research Organisations

  • Justus Liebig University Giessen
  • TU Dortmund University
  • University of Washington
  • Helmholtz Centre for Infection Research (HZI)
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Details

Original languageEnglish
Pages (from-to)202-207
Number of pages6
JournalJournal of Molecular Catalysis B: Enzymatic
Volume61
Issue number3-4
Publication statusPublished - 9 Jul 2009

Abstract

A selective and highly efficient allylic oxidation of the sesquiterpene (+)-valencene to (+)-nootkatone was achieved with lyophilisate of the basidiomycete Pleurotus sapidus. The responsible enzymatic activity was biochemically characterised and purified by chromatographic and electrophoretic methods. Peptide sequences obtained by mass spectrometry showed homologies to oxygenases from various ascomycetes. Based on the peptide sequences, the encoding cDNA was amplified from a cDNA library of P. sapidus by PCR. The cloned sequence consisted of 1309 bp with an open reading frame of 1191 bp. Based on database research, the translated amino acid sequence of 396 amino acids showed on the protein level homologies of ∼50% to putative lipoxygenases from Aspergillus fumigatus and Laccaria bicolor as well as 26% homology to the sequence of lipoxygenase-1 from soy bean (Glycine max). A lipoxygenase from a basidiomycetous fungus has not yet been characterised on a molecular level.

Keywords

    Basidiomycete, Biotransformation, Nootkatone, Oxygenase, Valencene

ASJC Scopus subject areas

Cite this

A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone. / Fraatz, Marco A.; Riemer, Stephanie J.L.; Stöber, Regina et al.
In: Journal of Molecular Catalysis B: Enzymatic, Vol. 61, No. 3-4, 09.07.2009, p. 202-207.

Research output: Contribution to journal › Article › Research › peer review

Fraatz, MA, Riemer, SJL, Stöber, R, Kaspera, R, Nimtz, M, Berger, RG & Zorn, H 2009, 'A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone', Journal of Molecular Catalysis B: Enzymatic, vol. 61, no. 3-4, pp. 202-207. https://doi.org/10.1016/j.molcatb.2009.07.001
Fraatz, M. A., Riemer, S. J. L., Stöber, R., Kaspera, R., Nimtz, M., Berger, R. G., & Zorn, H. (2009). A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone. Journal of Molecular Catalysis B: Enzymatic, 61(3-4), 202-207. https://doi.org/10.1016/j.molcatb.2009.07.001
Fraatz MA, Riemer SJL, Stöber R, Kaspera R, Nimtz M, Berger RG et al. A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone. Journal of Molecular Catalysis B: Enzymatic. 2009 Jul 9;61(3-4):202-207. doi: 10.1016/j.molcatb.2009.07.001
Fraatz, Marco A. ; Riemer, Stephanie J.L. ; Stöber, Regina et al. / A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone. In: Journal of Molecular Catalysis B: Enzymatic. 2009 ; Vol. 61, No. 3-4. pp. 202-207.
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title = "A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone",
abstract = "A selective and highly efficient allylic oxidation of the sesquiterpene (+)-valencene to (+)-nootkatone was achieved with lyophilisate of the basidiomycete Pleurotus sapidus. The responsible enzymatic activity was biochemically characterised and purified by chromatographic and electrophoretic methods. Peptide sequences obtained by mass spectrometry showed homologies to oxygenases from various ascomycetes. Based on the peptide sequences, the encoding cDNA was amplified from a cDNA library of P. sapidus by PCR. The cloned sequence consisted of 1309 bp with an open reading frame of 1191 bp. Based on database research, the translated amino acid sequence of 396 amino acids showed on the protein level homologies of ∼50% to putative lipoxygenases from Aspergillus fumigatus and Laccaria bicolor as well as 26% homology to the sequence of lipoxygenase-1 from soy bean (Glycine max). A lipoxygenase from a basidiomycetous fungus has not yet been characterised on a molecular level.",
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AU - Fraatz, Marco A.

AU - Riemer, Stephanie J.L.

AU - Stöber, Regina

AU - Kaspera, Rüdiger

AU - Nimtz, Manfred

AU - Berger, Ralf G.

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