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Sci Rep. 2017 May 3;7:46738. doi: 10.1038/srep46738.

Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily.

Author information

1
Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria.
2
University of Graz, Institute of Molecular Biosciences, NAWI Graz, Humboldtstrasse 50, 8010 Graz, Austria.
3
Medical University of Graz, Institute of Pathology, Stiftingtalstrasse 24, 8010 Graz, Austria.
4
Omics Center Graz, BioTechMed Graz, Stiftingtalstraße 24, 8010 Graz, Austria.
5
Graz University of Technology, Institute of Molecular Biotechnology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria.
6
Bio-prodict BV, Nieuwe Marktstraat, 54E 6511 AA, Nijmengen, The Netherlands.

Abstract

Homology and similarity based approaches are most widely used for the identification of new enzymes for biocatalysis. However, they are not suitable to find truly novel scaffolds with a desired function and this averts options and diversity. Hydroxynitrile lyases (HNLs) are an example of non-homologous isofunctional enzymes for the synthesis of chiral cyanohydrins. Due to their convergent evolution, finding new representatives is challenging. Here we show the discovery of unique HNL enzymes from the fern Davallia tyermannii by coalescence of transcriptomics, proteomics and enzymatic screening. It is the first protein with a Bet v1-like protein fold exhibiting HNL activity, and has a new catalytic center, as shown by protein crystallography. Biochemical properties of D. tyermannii HNLs open perspectives for the development of a complementary class of biocatalysts for the stereoselective synthesis of cyanohydrins. This work shows that systematic integration of -omics data facilitates discovery of enzymes with unpredictable sequences and helps to extend our knowledge about enzyme diversity.

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