Designing better enzymes: Insights from directed evolution
Designing better enzymes: Insights from directed evolution
Authors (3): H. A. Bunzel, J. L. R. Anderson, A. J. Mulholland
Themes: Core
DOI: 10.1016/j.sbi.2020.12.015
Citations: 81
Pub type: journal-article
Pub year: 2021

Publisher: Elsevier BV

Issue:

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Publication date(s): 2021/04 (print)

Pages: 212-218

Volume: 67 Issue:

Journal: Current Opinion in Structural Biology

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De novo enzymes can be created by computational design and directed evolution. Here, we review recent insights into the origins of catalytic power in evolved designer enzymes to pinpoint opportunities for next-generation designs: Evolution precisely organizes active sites, introduces catalytic H-bonding networks, invokes electrostatic catalysis, and creates dynamical networks embedding the active site in a reactive protein scaffold. Such insights foster our fundamental knowledge of enzyme catalysis and fuel the future design of tailor-made enzymes.

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