Brief Communication

Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases

  • Nature Chemical Biologyvolume 14pages342344 (2018)
  • doi:10.1038/s41589-018-0005-8
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Abstract

Sugar O-methylation shields algal polysaccharides against microbial hydrolytic enzymes. Here, we describe cytochrome P450 monooxygenases from marine bacteria that, together with appropriate redox-partner proteins, catalyze the oxidative demethylation of 6-O-methyl-d-galactose, which is an abundant monosaccharide of the algal polysaccharides agarose and porphyran. This previously unknown biological function extends the group of carbohydrate-active enzymes to include the class of cytochrome P450 monooxygenases.

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Change history

  • Correction 08 March 2018

    In the version of this article originally published, the line of conditions shown for NADH in Figure 2b was shifted out of place. The error has been corrected in the HTML and PDF versions of the article.

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Acknowledgements

We thank the German Research Foundation (DFG) for funding through the Research Unit FOR2406. J.-H.H. acknowledges funding by the Emmy Noether Program of the DFG, grant number HE 7217/1-1. We are also grateful to V. Urlacher (Düsseldorf, Germany) for providing the genes encoding P450cam, PdX, PdR and CPR. We thank D. Nelson (Memphis, USA) for assigning the P450s to a subfamily in the P450 database.

Author information

Affiliations

  1. Department of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Greifswald, Germany

    • Lukas Reisky
    • , Hanna C. Büchsenschütz
    • , Jennifer Engel
    •  & Uwe T. Bornscheuer
  2. Max Planck Institute for Marine Microbiology, Bremen, Germany

    • Tao Song
    •  & Jan-Hendrik Hehemann
  3. Pharmaceutical Biotechnology, Institute of Pharmacy, University of Greifswald, Greifswald, Germany

    • Thomas Schweder
  4. University of Bremen, Center for Marine Environmental Sciences (MARUM), Bremen, Germany

    • Jan-Hendrik Hehemann

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Contributions

J.-H.H., T.S. and U.T.B. initiated the study and directed the project. J.E. together with L.R. cloned, expressed and purified the P450 enzymes and performed preliminary studies; H.C.B. and L.R. cloned, expressed and purified all other enzymes and performed all further experiments. S.T. and J.-H.H. performed the computational analysis. L.R., H.C.B., J.-H.H. and U.T.B. prepared the manuscript, which was revised and approved by all authors.

Competing interests

The authors declare no competing interests.

Corresponding authors

Correspondence to Jan-Hendrik Hehemann or Uwe T. Bornscheuer.

Supplementary information

  1. Supplementary Text and Figures

    Supplementary Tables 1 and 2 and Supplementary Figures 1–7

  2. Life Sciences Reporting Summary