Abstract
Under macromolecular crowding (MC) conditions such as cellular, extracellular, food and other environments of biotechnological interest, the thermodynamic activity of the different macromolecules present in the system is several orders of magnitude higher than in dilute solutions. In this state, the diffusion rates are affected by the volume exclusion induced by the crowders. Immiscible liquid phases, which may arise in MC by liquid–liquid phase separation, may induce a dynamic confinement of reactants, products and/or enzymes, tuning reaction rates. In cellular environments and other crowding conditions, membranes and macromolecules provide, on the whole, large surfaces that can perturb the solvent, causing its immobilisation by adsorption in the short range and also affecting the solvent viscosity in the long range. The latter phenomenon can affect the conformation of a protein and/or the degree of association of its protomers and, consequently, its activity. Changes in the water structure can also alter the enzyme–substrate interaction, and, in the case of hydrolytic enzymes, where water is one of the substrates, it also affects the reaction mechanism. Here, we review the evidence for how macromolecular crowding affects the catalysis induced by hydrolytic enzymes, focusing on the structure and dynamics of water.
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Acknowledgements
This work was partially financed by the SeCyT-Universidad Nacional de Córdoba, Foncyt and CONICET from Argentina. All authors are members of the later institution. JMS is supported with a María Zambrano postdoctoral researcher contract (677904) from the Ministerio de Universidades and European Union (“Financed by European Union-Next GenerationEU”).
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Perillo, M.A., Burgos, I., Clop, E.M. et al. The role of water in reactions catalysed by hydrolases under conditions of molecular crowding. Biophys Rev 15, 639–660 (2023). https://doi.org/10.1007/s12551-023-01104-2
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DOI: https://doi.org/10.1007/s12551-023-01104-2