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BIOspektrum

, Volume 25, Issue 5, pp 572–574 | Cite as

Pilzliche Peroxygenasen: der Schlüssel zu C-H-Hydroxylierungen und mehr?

  • Pascal Püllmann
  • Martin J. WeissenbornEmail author
Open Access
Biotechnologie Biokatalyse
  • 91 Downloads

Abstract

Fungal peroxygenases represent an exciting new enzyme class for stereo - selective hydroxylation reactions. They are capable of the oxyfunctionalisation of a large, diverse scope of substrates including alkanes and steroids as well as the heteroatoms sulfur and nitrogen. The outstanding activities and stabilities as well as their reliance on hydrogen peroxide as co-substrate renders it a highly interesting biocatalyst.

Literatur

  1. [1]
    Ullrich R, Nuske J, Scheibner K et al. (2004) Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes. Appl Environ Microbiol 70:4575–4581CrossRefPubMedPubMedCentralGoogle Scholar
  2. [2]
    Churakova E, Kluge M, Ullrich R et al. (2011) Specific photobiocatalytic oxyfunctionalization reactions. Angew Chem Int Ed 50:10716–10719CrossRefGoogle Scholar
  3. [3]
    Peter S, Kinne M, Wang X et al. (2011) Selective hydroxylation of alkanes by an extracellular fungal peroxygenase. FEBS J 278:3667–3675CrossRefPubMedPubMedCentralGoogle Scholar
  4. [4]
    Ni Y, Fernandez-Fueyo E, Gomez Baraibar A et al. (2016) Peroxygenase-catalyzed oxyfunctionalization reactions promoted by the complete oxidation of methanol. Angew Chem Int Ed 55:798–801CrossRefGoogle Scholar
  5. [5]
    Faiza M, Huang S, Lan D et al. (2019) New insights on unspecific peroxygenases: superfamily reclassification and evolution. BMC Evol Biol 19:76CrossRefPubMedPubMedCentralGoogle Scholar
  6. [6]
    Molina-Espeja P, Garcia-Ruiz E, Gonzalez-Perez D et al. (2014) Directed evolution of unspecific peroxygenase from Agrocybe aegerita. Appl Environ Microbiol 80:3496–3507CrossRefPubMedPubMedCentralGoogle Scholar
  7. [7]
    Püllmann P, Ulpinnis C, Marillonnet S et al. (2019) Golden Mutagenesis: an efficient multi-sitesaturation mutagenesis approach by Golden Gate cloning with automated primer design. bioRxiv:453621Google Scholar
  8. [8]
    Engler C, Kandzia R, Marillonnet S (2008) A one pot, one step, precision cloning method with high throughput capability. PLoS One 3:e3647CrossRefGoogle Scholar
  9. [9]
    Santos-Aberturas J, Dorr M, Waldo GS et al. (2015) Indepth high-throughput screening of protein engineering libraries by split-GFP direct crude cell extract data normalization. Chem Biol 22:1406–1414CrossRefPubMedGoogle Scholar
  10. [10]
    Kiebist J, Schmidtke KU, Zimmermann J et al. (2017) A peroxygenase from Chaetomium globosum catalyzes the selective oxygenation of testosterone. ChemBioChem 18:563–569CrossRefPubMedPubMedCentralGoogle Scholar
  11. [11]
    Babot ED, Del Rio JC, Canellas M et al. (2015) Steroid hydroxylation by basidiomycete peroxygenases: a combined experimental and computational study. Appl Environ Microbiol 81:4130–4142CrossRefPubMedPubMedCentralGoogle Scholar

Copyright information

© Die Autoren 2019

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits use, duplication, adaption, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

Open access funding provided by Leibniz Institute of Plant Biochemistry.

Authors and Affiliations

  1. 1.Junior Research Group Bioorganic Chemistry Leibniz-Institut für Pflanzenbiochemie (IPB)Institut für Chemie, Martin-Luther-Universität Halle-WittenbergHalle (Saale)Deutschland

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