Enzyme adaptation is the adjustment of enzyme molecular properties and enzymatic capacity that permits catalytic function to be maintained within the physicochemical conditions experienced by an organism. At the molecular level, adaptation can involve heritable changes in amino-acid sequence that modify protein conformational dynamics, structural stability, substrate binding, catalytic rate, and the dependence of these properties on environmental variables such as temperature, pressure, pH, or ionic conditions ^[1][2]. Such adaptation reflects selection on the relationship between enzyme structure and catalytic function, so that functionally relevant conformational states and kinetic properties occur within the environmental range in which the enzyme operates ^[2][3]. At the cellular and physiological level, enzyme adaptation can also encompass regulated changes in enzyme abundance or the expression of enzyme variants that alter total catalytic capacity under prevailing conditions. Its defining scope therefore includes adaptive modification of intrinsic enzyme properties—such as catalytic efficiency, ligand affinity, stability, and conformational flexibility—and regulated variation in the amount or molecular form of enzymatic activity available in cells ^[3][4]. These mechanisms collectively establish an enzyme system whose catalytic behavior is compatible with the organism's biochemical and physicochemical environment ^[2][4].