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YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

Nature Chemical Biology volume 12, pages 215–217 (2016)Cite this article

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Abstract

Sulfoquinovose is produced by photosynthetic organisms at a rate of 1010 tons per annum and is degraded by bacteria as a source of carbon and sulfur. We have identified Escherichia coli YihQ as the first dedicated sulfoquinovosidase and the gateway enzyme to sulfoglycolytic pathways. Structural and mutagenesis studies unveiled the sequence signatures for binding the distinguishing sulfonate residue and revealed that sulfoquinovoside degradation is widespread across the tree of life.

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Figure 1: E. coli YihQ is a sulfoquinovosidase that hydrolyzes SQDG to SQ.
Figure 2: Structural identification of SQ-binding residues.

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Acknowledgements

We thank S.G. Withers for the gift of 5-fluoro-β-L-idopyranosyl fluoride and N.A. Williamson for technical assistance. This work was supported by grants from the UK Biotechnology and Biological Sciences Research Council and the European Research Council (AdG-322942 to G.J.D.), the Australian Research Council (to S.J.W.), the Ramaciotti Foundation and the Victorian Endowment for Science Knowledge and Innovation, with additional support from the Australian Cancer Research Foundation and Victorian State Government Operational Infrastructure Support, NHMRC IRIISS grant 9000220 (to E.D.G.-B.). We thank the Diamond Light Source (Didcot, UK) for access to beamlines IO4, IO4-1 and IO2 (proposal number mx-9948).

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Author notes

  1. Gaetano Speciale and Yi Jin: These authors contributed equally to this work.

Authors and Affiliations

  1. School of Chemistry, University of Melbourne, Parkville, Victoria, Australia

    Gaetano Speciale & Spencer J Williams

  2. Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia

    Gaetano Speciale & Spencer J Williams

  3. Department of Chemistry, University of York, Heslington, York, UK

    Yi Jin & Gideon J Davies

  4. ACRF Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia

    Ethan D Goddard-Borger

  5. Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia

    Ethan D Goddard-Borger

Authors
  1. Gaetano Speciale
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  2. Yi Jin
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  3. Gideon J Davies
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  4. Spencer J Williams
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  5. Ethan D Goddard-Borger
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Contributions

G.S. synthesized substrate and performed LC/MS analysis. G.S. and E.D.G.-B. cloned, expressed, mutagenized and purified enzymes and performed kinetic analyses. Y.J. performed crystallographic studies and prepared the accompanying figures. Experiments were designed by G.J.D., S.J.W. and E.D.G.-B., who collectively wrote the paper.

Corresponding author

Correspondence to Ethan D Goddard-Borger.

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The authors declare no competing financial interests.

Supplementary information

Supplementary Text and Figures

Supplementary Results, Supplementary Tables 1–3 and Supplementary Figures 1–7. (PDF 2820 kb)

Supplementary Note

Synthetic Procedures (PDF 529 kb)

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Speciale, G., Jin, Y., Davies, G. et al. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids. Nat Chem Biol 12, 215–217 (2016). https://doi.org/10.1038/nchembio.2023

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  • DOI: https://doi.org/10.1038/nchembio.2023

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