Enzyme regulation encompasses the diverse molecular processes by which the catalytic activity, substrate specificity, and functional output of an enzyme are modulated within a living system, enabling metabolic pathways to respond dynamically to cellular demands ^[1]. A principal mode involves the reversible binding of effector molecules at sites spatially removed from the active site, known as allosteric regulation ^[2]. Another mode entails the reversible or irreversible covalent attachment of chemical groups, such as phosphate, to the enzyme polypeptide. Regulation also extends to processes that alter the effective concentration of active enzyme molecules, including controlled proteolytic activation of zymogen precursors and changes in the rate of enzyme synthesis and degradation ^[1]. Through these mechanisms, catalytic efficiency and ligand-binding affinity are adjusted in response to specific metabolic signals, coordinating flux through interconnected reaction networks and maintaining cellular homeostasis ^[3]. The regulatory apparatus of an enzyme is encoded within its three-dimensional structure, which determines the sensitivity of the protein to effector molecules and the kinetic consequences of regulatory modification ^[4].