Substrate inhibition is a phenomenon observed in enzyme kinetics in which increased substrate concentrations result in reduced, often dramatically, enzyme-catalyzed reaction rates. Presently observed in an estimated 25% of studied enzymes, substrate inhibition has serious implications in the understanding of many crucial biological processes, the function of these proteins inside the cell, as well as the utilization of enzymatic reactions for industrial applications. Studies show substrate inhibition to be a real limitation in vitro and logical conclusions have been drawn to explain the relevance of substrate inhibition in the self-regulation of biological pathways. However, there is currently no consensus on how important a role, if any, substrate inhibition plays in vivo as it is not clear whether cellular substrate concentrations reach the levels required to initiate substrate inhibition or what effects the cellular environment and organization may have. Conditions within the cell are high in macromolecular concentration and are segregated and confined, properties that are not easily duplicated by in vitro assays and may have an influence on substrate inhibition effects. Here, HK97 virus-like particles (VLPs) were employed to encapsulate various enzymes known to undergo substrate inhibition in-order-to mimic cellular conditions and examine what effects close confinement and localization may have on enzyme kinetics.

Investigating substrate inhibition of enzymes encapsulated within HK97 virus-like particles

ACS Spring 2022

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