The importance of ligand binding for the regulation of the functioning of the enzyme and the presence of a diverse and multicomponent microenvironment of the biocatalyst is noted. The binding of chondroitin trimers (on centers cs2, cs4, cs7, cs8 or cs1, cs2, cs4, cs7, cs8) decreased the inhibition of the enzyme by tetramer heparin. As a result of this, the inactivation and stabilization of the enzyme globule are observed, and a change in its inhibition by heparin. The reported impact was due to electrostatic noncovalent interactions (without specific binding to the active site), causing noticeable conformational changes in the molecule biocatalyst/enzyme. Exploratory computational consideration of the interaction of a 3D model of bovine testicular hyaluronidase (BTH) with short chain glycosaminoglycan ligands demonstrated the diversity and significance of their effect on the structure of the enzyme. The computational study of a 3D model of the hyaluronidase interaction with shortchain glycosaminoglycan ligands demonstrated the diversity and significance of their reaction on enzyme structure.
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