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The region on an enzyme where substrate molecules bind and undergo a chemical reaction.

The reactant that an enzyme acts on during a biochemical reaction.

A temporary molecule formed when an enzyme comes into perfect contact with its substrate.

Describes the rate of enzymatic reactions by relating reaction rate $v$ to $[S]$, concentration of a substrate S.

The maximum rate of an enzyme-catalyzed reaction when the enzyme is saturated with substrate.

The substrate concentration at which the reaction rate is half of $V_{max}$.

The number of substrate molecules converted to product by an enzyme molecule per unit time when the enzyme is fully saturated with substrate.

The ability of an enzyme to choose exact substrate from a group of similar chemical molecules.

A double reciprocal graph of the Michaelis-Menten equation which plots $1/v$ against $1/[S]$.

A form of enzyme inhibition where the inhibitor competes with the substrate for binding at the active site.

A type of enzyme inhibition where the inhibitor binds to an enzyme at a site other than the active site.

The regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site.

A process where the end product of a metabolic pathway acts as an inhibitor of an enzyme within that pathway.

Different enzymes that catalyze the same reaction but have different properties, such as different kinetics.

A phenomenon where, at high substrate concentrations, the reaction rate levels off and becomes independent of substrate concentration as all enzyme molecules are occupied.

The rate of an enzyme-catalyzed reaction when the reaction is just starting and the substrate concentration is much higher than the enzyme concentration.

The slowest step in a pathway or reaction mechanism that determines the overall rate of the other steps.

A molecule that binds to an enzyme and decreases its activity.

A non-protein chemical compound or metallic ion that is required for an enzyme's activity as a catalyst.

A type of inhibition where the inhibitor can only bind to the enzyme-substrate complex, not to the free enzyme.

A measure of cooperativity in binding multiple ligands by an enzyme or a receptor; values >1 indicate positive cooperativity, <1 indicate negative cooperativity, and =1 indicate non-cooperativity.

A measure of the efficiency of an enzyme in catalyzing a reaction, defined as $k_{cat}/K_m$.

The process by which a molecule (e.g., a drug) enhances the expression of an enzyme.

An unstable molecular state that is formed during the conversion from substrate to product and has higher energy than both the reactants and the products.