New Insights into the Cooperativity and Dynamics of Dimeric Enzymes

Abstract

A survey of protein databases indicates that the majority of enzymes exist in oligomeric forms, with about half of those found in the UniProt database being homodimeric. Understanding why many enzymes are in their dimeric form is imperative. Recent developments in experimental and computational techniques have allowed for a deeper comprehension of the cooperative interactions between the subunits of dimeric enzymes. This review aims to succinctly summarize these recent advancements by providing an overview of experimental and theoretical methods, as well as an understanding of cooperativity in substrate binding and the molecular mechanisms of cooperative catalysis within homodimeric enzymes. Focus is set upon the beneficial effects of dimerization and cooperative catalysis. These advancements not only provide essential case studies and theoretical support for comprehending dimeric enzyme catalysis but also serve as a foundation for designing highly efficient catalysts, such as dimeric organic catalysts. Moreover, these developments have significant implications for drug design, as exemplified by Paxlovid, which was designed for the homodimeric main protease of SARS-CoV-2.

Development of a Novel Support Modification for Efficient Lipase Immobilization: Preparation, Characterization, and Application for Bio-flavor Production

“…Firstly, these metal ions play a crucial role in stabilizing the enzyme structure by interacting with specific amino acid residues in the enzyme's active site [51], thereby promoting optimal enzymesubstrate interactions. Secondly, they act as cofactors that bind to the enzyme-substrate complex, facilitating substrate binding and catalysis [52]. Additionally, these metal ions can modulate the enzyme's kinetic properties, such as substrate affinity and turnover rate, leading to increased enzyme activity [53].…”