A strategy using pressure was devised to structurally identify conformational transitions in protein ensembles, allowing the rational prediction of mutations that induce pressure-driven enzyme activation. These results highlight the power of flexibility–function analyses in protein engineering design and applications.
References
Campbell, E. et al. Nat. Chem. Biol. 12, 944–50 (2016).
Narayanan, C. et al. Structure 26, 426–36 (2018).
Stiller, J. B. et al. Nat. Catal. https://doi.org/10.1038/s41929-019-0307-6 (2019).
Lisi, G. P. & Loria, J. P. Prog. Nucl. Magn. Reson. Spectrosc. 92–93, 1–17 (2016).
Akasaka, K. Chem. Rev. 106, 1814–35 (2006).
Wilding, M., Hong, N., Spence, M., Buckle, A. M. & Jackson, C. J. Biochem. Soc. Trans. 47, 701–11 (2019).
Davey, J. A., Damry, A. M., Goto, N. K. & Chica, R. A. Nat. Chem. Biol. 13, 1280–85 (2017).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Doucet, N. Enzyme catalysis under pressure. Nat Catal 2, 646–647 (2019). https://doi.org/10.1038/s41929-019-0326-3
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41929-019-0326-3
- Springer Nature Limited