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. 2020 Mar;40(2):231-246.
doi: 10.1080/07388551.2019.1711014. Epub 2020 Jan 8.

Bioengineering oligomerization and monomerization of enzymes: learning from natural evolution to matching the demands for industrial applications

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Bioengineering oligomerization and monomerization of enzymes: learning from natural evolution to matching the demands for industrial applications

Hu Liu et al. Crit Rev Biotechnol. 2020 Mar.

Abstract

It is generally accepted that oligomeric enzymes evolve from their monomeric ancestors, and the evolution process generates superior structural benefits for functional advantages. Furthermore, adjusting the transition between different oligomeric states is an important mechanism for natural enzymes to regulate their catalytic functions for adapting environmental fluctuations in nature, which inspires researchers to mimic such a strategy to develop artificially oligomerized enzymes through protein engineering for improved performance under specific conditions. On the other hand, transforming oligomeric enzymes into their monomers is needed in fundamental research for deciphering catalytic mechanisms as well as exploring their catalytic capacities for better industrial applications. In this article, strategies for developing artificially oligomerized and monomerized enzymes are reviewed and highlighted by their applications. Furthermore, advances in the computational prediction of oligomeric structures are introduced, which would accelerate the systematic design of oligomeric and monomeric enzymes. Finally, the current challenges and future directions in this field are discussed.

Keywords: Oligomeric structures; catalytic capacity; computational prediction; monomeric enzymes; protein engineering; stability.

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