GLOSSARY

Allosteric Modulator alters enzyme behavior through regulatory binding.

Allosteric regulation changes activity through communication between regulatory binding and functional regions; it can activate or inhibit. Feedback carries downstream-product or state information upstream, whereas feedforward conveys input or upstream information onward. Both can operate in one network. Regulation coordinates supply and use rather than keeping every enzyme maximally active, so more activation is not automatically a better nutritional or training outcome.

The active site combines substrate recognition and reaction chemistry; catalytic site emphasizes reaction-performing components, while binding site emphasizes recognition. A regulatory site may be separate and alter activity through an effector. Binding away from the active site does not automatically produce pure noncompetitive inhibition. Binding location and kinetic behavior must be described separately rather than treating all distant binding as one inhibition pattern.

Cooperativity means that binding or state in one part affects another part's behavior. Positive and negative describe the direction of that effect rather than health benefit or harm. A Hill coefficient is an empirical response-slope measure, not necessarily an exact count of binding sites. Sigmoidal and hyperbolic responses differ, but curve shape alone cannot identify every molecular step or establish a complete regulatory mechanism.