Enzymes function in a highly crowded cellular interior, the latter being densely packed by a plethora of biomacromolecules and polysaccharides, with the concentration ranging from 0 – 400 g/L. Thus, for a better understanding of how such a congested interior affects the function of an enzyme, the cellular environment has often been mimicked using polymer based, water soluble, macromolecular crowding agents of different molecular weights (e.g., Ficoll 70, Dextran 70, Dextran 40, and PEG 8). Crowding effects on enzymes in solution have been described amongst others, by changes in effective concentration of the substrate and enzyme and slowed down diffusion of enzyme and/or substrate. Here, for the enzyme adenylate kinase (AK3L1), a phosphotransferase, where binding of a small substrate molecule induces large conformational changes, we have performed a combined study, based on enzyme activity, domain movement and solvation dynamics. Our data shows a strong correlation between enzyme dynamics and activity, with too much restriction on enzyme motion having an adverse effect on the manner in which the enzyme functions.

Understanding enzyme behavior in a crowded scenario: Correlating activity, conformation and dynamics

ACS Spring Meeting 2021

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