Enzyme Activity and Regulation Quiz

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Questions and Answers

What is the effect of allosteric activators on enzyme activity?

  • Activators decrease the affinity of the enzyme for the substrate.
  • Activators increase the rate of enzyme synthesis.
  • Activators directly bind to the active site of the enzyme.
  • Activators increase the affinity of the enzyme for the substrate. (correct)

What is a key difference between non-competitive inhibition and transcriptional control of enzyme activity?

  • Non-competitive inhibition is reversible, while transcriptional control is irreversible.
  • Non-competitive inhibition affects protein synthesis, while transcriptional control affects protein breakdown.
  • Non-competitive inhibition directly affects the enzyme's active site, while transcriptional control indirectly affects enzyme levels. (correct)
  • Non-competitive inhibition is long-term, while transcriptional control is short-term.

Which of the following is NOT a post-translational modification that can control enzyme activity?

  • Acetylation
  • Phosphorylation
  • Glycosylation (correct)
  • Methylation

Which state of an enzyme has a higher affinity for its substrate?

<p>R state (D)</p> Signup and view all the answers

What is the significance of enzyme turnover in regulating enzyme activity?

<p>Enzyme turnover allows for a continuous supply of new enzymes to replace degraded ones. (D)</p> Signup and view all the answers

What is the relationship between bond strength and potential energy?

<p>Stronger bonds have lower potential energy. (B)</p> Signup and view all the answers

When a reaction is exothermic, what is the relationship between the enthalpy of the reactants and the enthalpy of the products?

<p>The enthalpy of the reactants is higher than the enthalpy of the products. (D)</p> Signup and view all the answers

What is the relationship between the change in free energy (deltaG) and the spontaneity of a reaction?

<p>A negative deltaG indicates a spontaneous reaction. (D)</p> Signup and view all the answers

Which of the following is an example of an endergonic reaction?

<p>The synthesis of proteins from amino acids. (A)</p> Signup and view all the answers

What is the role of high-energy intermediates in metabolic reactions?

<p>They provide energy to drive endergonic reactions. (D)</p> Signup and view all the answers

What is the change in free energy for a reaction that has an enthalpy change of -50 kJ/mol and an entropy change of +100 J/mol*K at a temperature of 298 K?

<p>-80 kJ/mol (B)</p> Signup and view all the answers

Which of the following is not a characteristic of an exergonic reaction?

<p>It requires an input of energy. (A)</p> Signup and view all the answers

Which statement correctly describes the relationship between the change in entropy (deltaS) and the randomness of a reaction?

<p>A positive deltaS indicates increased randomness. (A)</p> Signup and view all the answers

What is the net effect of the conversion of succinyl-CoA into succinate?

<p>Production of one GTP (B)</p> Signup and view all the answers

Which enzyme catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA?

<p>Alpha-ketoglutarate dehydrogenase (B)</p> Signup and view all the answers

Which of the following statements accurately describes the role of FAD in the TCA cycle?

<p>FAD is reduced to FADH2 during the conversion of succinate to fumarate (B)</p> Signup and view all the answers

Which of the following processes is directly involved in replenishing TCA cycle intermediates?

<p>Anaplerotic reactions (D)</p> Signup and view all the answers

Which of the following molecules acts as an allosteric activator of the TCA cycle?

<p>Calcium (D)</p> Signup and view all the answers

How does citrate accumulation affect the TCA cycle?

<p>It inhibits the activity of pyruvate dehydrogenase (D)</p> Signup and view all the answers

Which step of the TCA cycle involves a direct phosphorylation of GDP?

<p>Conversion of succinyl-CoA to succinate (C)</p> Signup and view all the answers

Which of the following statements accurately describes the regulation of the TCA cycle?

<p>The TCA cycle is regulated by the concentrations of key intermediates, such as oxaloacetate and acetyl-CoA, as well as allosteric effectors like calcium (A)</p> Signup and view all the answers

What is the primary function of thermogenin in brown adipose tissue?

<p>Enables proton movement for heat generation (B)</p> Signup and view all the answers

Which compound is known to generate heat similar to thermogenin?

<p>DNP (2,4-dinitrophenol) (D)</p> Signup and view all the answers

What is a major consequence of using DNP as a weight loss supplement?

<p>Development of hyperthermia (A)</p> Signup and view all the answers

What occurs when complex IV inhibitors, such as carbon monoxide, are present in the cell?

<p>The entire electron transport chain backs up (C)</p> Signup and view all the answers

What is the effect of a Complex I inhibitor like rotenone?

<p>Blocks electron transfer from NADH in the ETC (B)</p> Signup and view all the answers

What is the primary function of the gamma subunit in ATP synthase?

<p>To rotate and induce conformational changes in alpha-beta dimers (D)</p> Signup and view all the answers

Which statement accurately describes the malate-aspartate shuttle?

<p>It enables the transport of electrons into the mitochondrial matrix (A)</p> Signup and view all the answers

What is the purpose of the glycerol-3-phosphate shuttle?

<p>To transport electrons into the inner mitochondrial membrane (D)</p> Signup and view all the answers

What occurs during the tight conformation of ATP synthase?

<p>ATP is formed and tightly bound to the enzyme (C)</p> Signup and view all the answers

Which of the following correctly describes the mechanism of oxidative phosphorylation?

<p>It uses a chemiosmotic coupling mechanism (C)</p> Signup and view all the answers

How do chemical uncouplers affect ATP synthesis?

<p>They prevent protons from returning through ATP synthase (C)</p> Signup and view all the answers

Which process is used to transport electrons across the inner mitochondrial membrane when NADH cannot directly cross?

<p>Shuttle systems such as malate-aspartate and glycerol-3-phosphate (A)</p> Signup and view all the answers

What confirms that the inner mitochondrial membrane is impermeable to NADH?

<p>NADH must be oxidized to transport electrons (D)</p> Signup and view all the answers

Which molecule is a direct inhibitor of the PDH complex?

<p>Acetyl-CoA (A)</p> Signup and view all the answers

Which of the following is NOT a direct activator of PDH phosphatase?

<p>ATP (B)</p> Signup and view all the answers

In the reaction catalyzed by isocitrate dehydrogenase, which molecule is reduced?

<p>NAD+ (A)</p> Signup and view all the answers

Which of the following statements about the TCA cycle is CORRECT?

<p>The TCA cycle generates reducing equivalents that are used in oxidative phosphorylation to produce ATP. (B)</p> Signup and view all the answers

What is the role of the lipoic domain in the PDH complex?

<p>To carry acetyl groups from pyruvate to coenzyme A. (A)</p> Signup and view all the answers

Which of the following statements about the regulation of the PDH complex is CORRECT?

<p>PDH phosphatase is activated by high levels of calcium and magnesium. (B)</p> Signup and view all the answers

What is the net yield of ATP from the complete oxidation of one molecule of acetyl-CoA in the TCA cycle?

<p>10 ATP (A)</p> Signup and view all the answers

Which step in the TCA cycle is irreversible and involves the hydrolysis of a thioester bond?

<p>Citrate synthase (D)</p> Signup and view all the answers

Flashcards

Non-competitive inhibition

Inhibition where a ligand binds to a site other than the active site, altering enzyme structure and function.

T state (tense state)

The form of an enzyme with low or no affinity for its substrate.

R state (relaxed state)

The form of an enzyme with high affinity for its substrate, allowing efficient binding.

Post-translational modifications

Changes made to enzymes after synthesis that affect their activity, such as phosphorylation.

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Enzyme turnover

The rate at which enzymes are degraded and replaced, affecting their half-life and activity duration.

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Thermodynamics

The study of energy transfer and transformations in systems.

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Delta G (ΔG)

The change in total Free Gibbs energy, indicates the potential for work in a reaction.

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Exothermic reaction

A reaction that releases energy, indicated by a negative delta H.

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Endothermic reaction

A reaction that absorbs energy, indicated by a positive delta H.

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Anabolic reactions

Reactions that build complex molecules, often requiring energy (endergonic).

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Catabolic reactions

Reactions that break down complex molecules, releasing energy (exergonic).

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Free energy and spontaneity

A negative delta G indicates a spontaneous reaction, while a positive one is not.

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Coupled reactions

Linking an exergonic reaction to an endergonic one to drive the latter forward.

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ATP synthase

An enzyme that synthesizes ATP from ADP and Pi using proton motive force.

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F0 component

The part of ATP synthase that allows protons to flow through, causing rotation.

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Alpha-beta dimers

Stationary parts of ATP synthase that undergo conformational changes during ATP synthesis.

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Malate-aspartate shuttle

A mechanism to transport electrons into the mitochondria using malate and aspartate.

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Glycerol-3-phosphate shuttle

A pathway for transporting electrons into mitochondria in muscle and brain tissues.

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Uncoupling proteins

Proteins that allow protons to re-enter the mitochondrial matrix without generating ATP.

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Oxidative phosphorylation

The process of ATP production through electron transport and chemiosmosis.

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Proton motive force

The force generated by the movement of protons across the mitochondrial membrane, driving ATP synthase.

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Thermogenin (UCP1)

A protein in brown adipose tissue that generates heat through proton movement.

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DNP (2,4-dinitrophenol)

A chemical that uncouples oxidative phosphorylation and generates heat.

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Complex I inhibitor

Rotenone blocks electrons from NADH in the electron transport chain.

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Complex IV inhibitors

Carbon monoxide and cyanide block electron transfer, halting ATP production.

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Chemical uncoupling

Process that allows protons to transport across membranes, generating heat.

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Oxidative decarboxylation

Conversion of alpha-ketoglutarate into succinyl-CoA by alpha-ketoglutarate dehydrogenase, producing CO2 and NADH.

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Succinyl-CoA synthetase

Enzyme that transforms succinyl-CoA into succinate, producing GTP, in a reversible reaction.

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Succinate dehydrogenase

Enzyme that oxidizes succinate to fumarate, using FAD and yielding FADH2.

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Fumarase

Enzyme that hydrates fumarate to L-malate by adding water, a reversible reaction.

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Malate dehydrogenase

Enzyme converting L-malate into oxaloacetate, producing NADH, also reversible.

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TCA cycle regulation

Regulated by the speed of PDH, and the 3 irreversible reactions influenced by oxaloacetate and acetyl-CoA concentrations.

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Citrate inhibition

High citrate accumulation inhibits citrate synthase, affecting acetyl-CoA production and PFK in glycolysis.

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Amphibolic pathway

Pathway involving both catabolic and anabolic processes, with reactions that replenish or utilize TCA cycle intermediates.

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Transesterification

A reaction that converts esters and alcohols via the exchange of alkoxy groups.

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Lipoic Domain

A component in the enzyme that undergoes oxidation and reduction during reactions.

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PDH Inhibition

The inhibition of pyruvate dehydrogenase by acetyl-CoA and NADH, reducing its activity.

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PDH Kinase Activation

Enzyme that inhibits E1 by phosphorylation in response to high ATP, NADH, and acetyl-CoA.

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Calcium's Role

Signaling molecule that activates PDH phosphatase for energy production during muscle contraction.

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TCA Cycle Products

The cycle generates GTP, NADH, FADH2, and CO2 from one acetyl-CoA.

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Citrate Synthase

Enzyme that catalyzes the reaction of acetyl-CoA with oxaloacetate to form citrate.

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Irreversible Reactions in TCA

Three specific reactions in the TCA cycle that cannot proceed backward.

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Study Notes

Metabolism Overview

  • Metabolism encompasses all biochemical processes involved in synthesis (anabolism), breakdown (catabolism), and conversion of constituents within cells and organisms.
  • It's crucial for understanding bodily functions, societal issues like obesity, and medical discoveries.

Why Study Metabolism?

  • Understanding how our bodies function is essential, including the socioeconomic implications of obesity and diabetes.
  • Medical discoveries, including genetic diseases affecting metabolic processes, are vital research areas.

Metabolic Pathways

  • Biochemical processes use electron carriers for energy generation.
  • Catabolism breaks down energy-containing nutrients (carbs, fats, proteins) into simpler, low-energy molecules, generating energy (e.g., ATP).
  • Anabolism synthesizes complex molecules (e.g., proteins, polysaccharides, lipids) from simpler precursors, utilizing energy (e.g., ATP).

Control Measures of Metabolism

  • Metabolic pathways are compartmentalized within cells and tissues. This compartmentalization allows for regulated metabolic activity.
  • Thermodynamics governs the energy changes in metabolic processes, with favorable reactions releasing energy (exergonic) and unfavorable reactions requiring energy input (endergonic).

Energy-Currency

  • Energy is absorbed to break a bond, energy is released when a bond is formed. Stronger bonds generally have higher energy.
  • ATP is a crucial energy carrier in metabolic reactions.

Cell-to-Cell Communication

  • Cells communicate and regulate metabolism through various methods including metabolite sensing.
  • Segregation and selective transport of metabolites between cells control various metabolic processes.

Inhibition and Control

  • Enzymes catalyze metabolic reactions, lowering the activation energy to enable these reactions to occur efficiently.
  • Inhibition mechanisms, both competitive and non-competitive (allosteric), are key for controlling metabolic activity.

Enzyme Turnover

  • Enzymes are not constantly present in a cell. Enzyme activity can depend on the enzyme half-life, which can be regulated.
  • The appropriate duration of activity or enzyme presence is crucial for regulating biological processes and maintaining homeostasis.

Carbohydrates and Glycolysis

  • Carbohydrates are a primary energy source in non-photosynthetic cells.
  • Monosaccharides are single sugar units (e.g., glucose).
  • Disaccharides are two sugars joined together.
  • Polysaccharides are complex carbohydrates (e.g., glycogen).
  • Glycolysis is the process of breaking down glucose to produce energy.

Aerobic and Anerobic Glycolysis

  • Glycolysis can occur aerobically (with oxygen) or anaerobically (without oxygen).
  • Aerobic glycolysis produces a higher yield of energy (ATP).
  • Anaerobic glycolysis produces lactic acid (in humans) as a byproduct.

Gluconeogenesis

  • Gluconeogenesis is the process of synthesizing glucose from non-carbohydrate precursors (e.g., lactate, amino acids).
  • It's the reverse of glycolysis and is vital for maintaining blood glucose levels when carbohydrate intake is insufficient.

Glycogen Metabolism

  • Glycogen is a storage form of glucose in animals.
  • Glycogenesis is the process of glycogen synthesis.
  • Glycogenolysis is the process of glycogen breakdown.

Regulation of Metabolism

  • Metabolic processes are carefully regulated by various factors, including hormonal control via signals like glucagon and insulin.
  • The control of metabolic rate is essential for maintaining blood glucose levels and regulating bodily functions.
  • Cells must control the amounts of enzymes present and/or the activity of enzymes to adjust their metabolic activity.

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