The focus of our attention is directed towards the small molecule of oxaloacetate.This work is dedicated to the investigation of the role played by natural intermediates as metabolism switches in intermolecular interactions.The full range of biological activity for oxaloacetate has been unveiled through the utilization of computer modeling methods.Furthermore, the interaction partner proteins have been characterized.It has been demonstrated that small molecules act as metabolic intermediates, serving as points of intersection for numerous metabolic pathways encompassing protein, carbohydrate, and lipid metabolism.Concurrently, a coordinating role is assumed by these molecules in the execution and modulation of mediator, hormonal, receptor responses, immunological, inflammatory, antibacterial, and antiviral reactions, thus manifesting anticarcinogenic properties.Through the application of differential scanning fluorimetry and microcapillary thermophoresis, the interaction between lactate dehydrogenase and ligands of endogenous origin has been established.The calculated Kd value obtained for the interaction between oxaloacetate and lactate dehydrogenase was determined to be 0.5±0.01μM.The thermalstability of LDH is enhanced by final concentrations of oxaloacetate ranging from 0.5 to 1 µM, whereas a concentration of 16 µM of the metabolite diminishes its thermostable characteristics.In intermolecular processes in in vitro cell culture, the stimulating effect of oxaloacetate 33,8 % (p=0.028) on the primary culture of human dermal fibroblasts was shown.
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