| Literature DB >> 31914816 |
Hu Liu1, Mingming Cao1, Ying Wang1, Bo Lv1, Chun Li1.
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
Year: 2020 PMID: 31914816 DOI: 10.1080/07388551.2019.1711014
Source DB: PubMed Journal: Crit Rev Biotechnol ISSN: 0738-8551 Impact factor: 8.429