Enzymes and Metabolism: Thermodynamics, ATP, and Regulation in Biology

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Last updated 1:31 PM on 4/15/26
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83 Terms

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Metabolism

All the chemical processes that occur within living organisms.

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Catabolic pathways

Breaking down of complex molecules that release energy.

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Anabolic pathways

Building of larger and complex molecules from smaller and simple molecules that consume energy.

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Thermodynamics

The study of energy transformations in a collection of matter.

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Isolated system

A system unable to exchange energy or matter with its surroundings.

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Open system

A system where energy and matter can be transferred between the system and its surroundings.

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Kinetic energy

Energy associated with motion.

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Thermal energy

The kinetic energy associated with random movement of atoms or molecules.

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Chemical energy

Potential energy available for release in a chemical reaction.

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Potential energy

Energy that matter possesses because of its location or structure.

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1st Law of Thermodynamics

Energy can be transferred or transformed but cannot be created or destroyed.

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2nd Law of Thermodynamics

Every energy transfer or transformation increases entropy.

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Entropy

A measure of molecular disorder or randomness.

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Spontaneous Process

Any process that leads to an increase in entropy that can proceed without requiring an input of energy.

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Non-spontaneous process

Any process that leads to a decrease in entropy.

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Non spontaneous process

Any process that leads to decrease in entropy is said non spontaneous process. This process will occur only if energy is supplied.

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Free-energy change

The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously.

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Energy and entropy changes

Biologists follow the energy and entropy changes during chemical reactions to determine whether they require an input of energy or occur spontaneously.

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Spontaneous reaction inquiry

Will this particular reaction happen or will we need to pay into it with energy?

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Gibbs free energy (G)

The portion of a system's energy that can do work when temperature and pressure are uniform throughout the system, as in a living cell.

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Change in free energy (ΔG)

Used to determine whether a process is spontaneous or not.

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Spontaneous processes

Processes that decrease the system's free energy and have a negative ΔG.

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Nonspontaneous processes

Processes that have a zero or positive ΔG.

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ΔG formula

ΔG = Gfinal state - Ginitial state.

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Negative ΔG

Indicates that the system loses free energy and becomes more stable.

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ΔG and temperature

Change in free energy during a reaction is related to temperature and changes in enthalpy and entropy.

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ΔG formula with variables

ΔG = ΔH - TΔS, where ΔH is change in enthalpy, ΔS is change in entropy, and T is temperature in Kelvin.

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Kelvin scale

Same as Celsius, but shifted down so that 0°K = -273°C.

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Exergonic reaction

A reaction that proceeds with a net release of free energy to the surroundings.

<p>A reaction that proceeds with a net release of free energy to the surroundings.</p>
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Endergonic reaction

A reaction that absorbs free energy from the surroundings.

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ATP (adenosine triphosphate)

Composed of ribose, adenine, and three phosphate groups.

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ATP hydrolysis

Energy is released from ATP when the terminal phosphate bond is broken by hydrolysis.

<p>Energy is released from ATP when the terminal phosphate bond is broken by hydrolysis.</p>
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Energy from ATP

Does not come directly from the phosphate bonds, but from the chemical change to a state of lower free energy in the products.

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Phosphorylation

Transfer of a phosphate group from ATP to another molecule, typically used to power endergonic reactions.

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Phosphorylated intermediate

The recipient molecule that is more reactive and has more free energy than the original molecule.

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Regeneration of ATP

ATP is regenerated by addition of a phosphate group to adenosine diphosphate (ADP).

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ATP cycle

The shuttling of inorganic phosphate and energy that couples energy-yielding processes to energy-consuming ones.

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Enzymes

Speed up metabolic reactions by lowering energy barriers.

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Spontaneous reactions

Do not need added energy, but can be very slow.

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Example of slow spontaneous reaction

The hydrolysis of sucrose to glucose and fructose can take years at room temperature without appreciable hydrolysis.

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Free-energy change (ΔG)

The change in free energy for a process can be used to determine whether it is spontaneous or not.

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Zero or positive ΔG

Indicates that a process is non-spontaneous.

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ΔG equation

ΔG = Gfinal state - Ginitial state.

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Stable system

A system with negative ΔG loses free energy and becomes more stable.

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Example of spontaneous reaction

The hydrolysis of sucrose to glucose and fructose is spontaneous but can take years at room temperature.

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Catalysts

Chemical agents that speed up a reaction without being consumed in the reaction.

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Enzyme

A macromolecule (typically protein) that acts as a catalyst to speed up a specific reaction.

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Sucrase

An enzyme that catalyzes the complete hydrolysis of sucrose within SECONDS when added to a sucrose solution at room temperature.

<p>An enzyme that catalyzes the complete hydrolysis of sucrose within SECONDS when added to a sucrose solution at room temperature.</p>
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Activation Energy (EA)

The initial energy needed to break the bonds of the reactants.

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Transition State

A highly unstable state that a molecule must reach for bonds to break and start a reaction.

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Catalysis

The process by which a catalyst selectively speeds up a reaction without itself being consumed.

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Substrate Specificity

The complementary fit between the shape of the active site of an enzyme and the shape of the substrate.

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Active Site

The region on the enzyme, often a pocket or groove, that binds to the substrate.

<p>The region on the enzyme, often a pocket or groove, that binds to the substrate.</p>
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ΔG

The change in free energy; enzymes cannot change ΔG.

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Denature

The process by which proteins lose their structure and function due to heat or other factors.

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Energy Profit

The excess energy released in an exergonic reaction after new bonds are formed.

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High Activation Energy

Most reactions that require additional energy (usually heat) to reach the transition state.

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Moderate Temperatures

The temperature range at which enzymes lower the activation energy barrier enough for reactions to occur.

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Chemical Reaction

A process involving the breaking and forming of bonds between molecules.

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Molecule Stability

Molecules become unstable when enough energy is absorbed to break bonds.

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Heat in Reactions

Adding heat is impractical in cells as it speeds up all reactions, not just those needed.

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Enzyme Function

Enzymes speed up reactions that would eventually occur anyway.

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Bonds Breaking

The process that must occur for a chemical reaction to start.

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Bonds Forming

The process that occurs after bonds break, leading to the release of energy.

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Substrates

Molecules that enzymes act upon, which may be oriented or stretched to facilitate reactions.

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Optimal Temperature

The temperature at which an enzyme catalyzes its reaction at the maximum possible rate.

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Denaturation

The process by which enzymes lose their functional shape due to extreme temperature or pH.

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Optimal Temperature for Human Enzymes

Approximately 37°C.

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Optimal Temperature for Thermophilic Bacteria

About 75°C.

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Optimal pH

The pH level at which an enzyme is most active.

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Optimal pH for Pepsin

2, which is suitable for the human stomach.

<p>2, which is suitable for the human stomach.</p>
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Optimal pH for Trypsin

8, which is suitable for the intestine.

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Cofactors

Non-protein helpers that assist enzymes, which can be either inorganic or organic.

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Inorganic Cofactors

Metal atoms such as zinc, iron, and copper in ionic form.

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Coenzymes

Organic cofactors that assist enzymes, often derived from vitamins.

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Enzyme Inhibitors

Chemicals that selectively inhibit the action of specific enzymes.

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Irreversible Inhibition

When an inhibitor forms covalent bonds with an enzyme, permanently disabling it.

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Reversible Inhibition

When inhibitors bind to enzymes through weak interactions, allowing for recovery of enzyme function.

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Competitive Inhibitors

Inhibitors that resemble substrates and bind to the enzyme's active site, blocking substrate access.

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Noncompetitive Inhibitors

Inhibitors that bind to an enzyme at a site other than the active site, altering enzyme shape and function.

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Metabolic Pathway

A series of chemical reactions in a cell, where a specific molecule is altered to produce a final product.

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Allosteric Regulation

Regulation of enzyme activity through the binding of a regulatory molecule at a site other than the active site.

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Feedback Inhibition

A regulatory mechanism where the end product of a metabolic pathway inhibits an earlier step in the pathway.

<p>A regulatory mechanism where the end product of a metabolic pathway inhibits an earlier step in the pathway.</p>