Cheat sheet 3: Biothermodynamics: Chemical Reactions and Enzyme Function

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18 Terms

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Anabolic Reaction

A process where small molecules combine to form a larger molecule.

<p>A process where small molecules combine to form a larger molecule.</p>
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Catabolic Reaction

A process where large molecules are broken down into smaller molecules.

<p>A process where large molecules are broken down into smaller molecules.</p>
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Exergonic Reaction

A reaction that releases free energy, making it spontaneous with a negative change in Gibbs free energy (−ΔG).

<p>A reaction that releases free energy, making it spontaneous with a negative change in Gibbs free energy (−ΔG).</p>
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Endergonic Reaction

A reaction that absorbs free energy, making it nonspontaneous with a positive change in Gibbs free energy (+ΔG).

<p>A reaction that absorbs free energy, making it nonspontaneous with a positive change in Gibbs free energy (+ΔG).</p>
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Kinetic Energy

The energy of an object in motion, such as a person jumping.

<p>The energy of an object in motion, such as a person jumping.</p>
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Potential Energy

Stored energy, such as that found in glycogen.

<p>Stored energy, such as that found in glycogen.</p>
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Enzyme

A biological catalyst that lowers the activation energy needed for a chemical reaction.

<p>A biological catalyst that lowers the activation energy needed for a chemical reaction.</p>
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Active Site

The specific region of an enzyme where the substrate binds.

<p>The specific region of an enzyme where the substrate binds.</p>
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Allosteric Site

A secondary site on an enzyme where an effector can bind, affecting enzyme activity.

<p>A secondary site on an enzyme where an effector can bind, affecting enzyme activity.</p>
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Induced Fit Model

A model describing how the binding of a substrate induces a change in the enzyme's shape to facilitate the reaction.

<p>A model describing how the binding of a substrate induces a change in the enzyme's shape to facilitate the reaction.</p>
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Vmax

The maximum rate of a reaction when the enzyme is saturated with substrate.

<p>The maximum rate of a reaction when the enzyme is saturated with substrate.</p>
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Michaelis Constant (Km)

The substrate concentration at which the reaction rate is half of Vmax, indicating the binding affinity of the enzyme.

<p>The substrate concentration at which the reaction rate is half of Vmax, indicating the binding affinity of the enzyme.</p>
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Competitive Inhibition

A type of inhibition where an inhibitor mimics the substrate and binds to the active site, preventing substrate binding.

<p>A type of inhibition where an inhibitor mimics the substrate and binds to the active site, preventing substrate binding.</p>
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How can competitive Inhibition be overcome?

increasing substrate concentration

Km Increases

V max stays the same

<p>increasing substrate concentration</p><p>Km Increases</p><p>V max stays the same</p>
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Noncompetitive Inhibition

A type of inhibition where an inhibitor binds to an allosteric site, reducing the enzyme's activity regardless of substrate concentration.

<p>A type of inhibition where an inhibitor binds to an allosteric site, reducing the enzyme's activity regardless of substrate concentration.</p>
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How is Km and V max affected in noncompetitive inhibition?

Km stays the same

V max Decreases

<p>Km stays the same</p><p>V max Decreases</p>
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ATP (Adenosine Triphosphate)

A molecule that serves as a primary energy carrier in cells, formed through phosphorylation.

<p>A molecule that serves as a primary energy carrier in cells, formed through phosphorylation.</p>
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ATP Hydrolysis

The process of breaking down ATP to release energy and phosphate, which is an exergonic reaction.

<p>The process of breaking down ATP to release energy and phosphate, which is an exergonic reaction.</p>