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Enzyme Kinetics

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Substrate

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

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Non-competitive Inhibition

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

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Allosteric Regulation

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

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Enzyme Specificity

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

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Competitive Inhibition

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

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Feedback Inhibition

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

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Enzyme-Substrate Complex

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

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Lineweaver-Burk Plot

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A double reciprocal graph of the Michaelis-Menten equation which plots 1/v1/v against 1/[S]1/[S].

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Active Site

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

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KmK_m (Michaelis constant)

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

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Michaelis-Menten Equation

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

v=Vmax[S]Km+[S]v = \frac{V_{max} [S]}{K_m + [S]}

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VmaxV_{max}

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

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Turnover Number (kcatk_{cat})

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

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Initial Rate of Reaction (v0v_0)

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

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Irreversible Inhibition

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A form of enzyme inhibition where the inhibitor permanently inactivates the enzyme, often by forming a covalent bond to it.

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Isoenzymes (Isozymes)

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

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Enzyme Cofactor

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

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Rate-limiting Step

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

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Hill's Coefficient

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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.

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Enzyme Induction

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

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Enzyme Inhibitor

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

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Uncompetitive Inhibition

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

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Transition State

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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.

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Saturation Kinetics

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

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Catalytic Efficiency

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

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