Understanding Enzyme Structure

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Questions and Answers

How do enzymes increase the rate of a biochemical reaction?

  • By providing additional reactants to the system.
  • By lowering the activation energy of the reaction. (correct)
  • By changing the equilibrium constant of the reaction.
  • By increasing the activation energy of the reaction.

Which of the following is an example of a coenzyme?

  • Zn2+
  • Mg2+
  • H2O
  • NAD+ (correct)

How does a competitive inhibitor affect enzyme activity?

  • It stabilizes the transition state of the reaction.
  • It binds to an allosteric site, changing the enzyme's shape.
  • It binds to the enzyme's active site, blocking the substrate. (correct)
  • It increases the enzyme's affinity for the substrate.

What is the primary effect of increasing temperature on enzyme activity, up to a certain point?

<p>It increases the reaction rate up to an optimal temperature. (A)</p> Signup and view all the answers

Which of the following statements accurately describes the first law of thermodynamics?

<p>Energy cannot be created or destroyed, only transferred. (B)</p> Signup and view all the answers

What is the role of ATP in cellular processes?

<p>To provide the energy currency for the cell. (C)</p> Signup and view all the answers

Which of the following best describes an exergonic reaction?

<p>A reaction that releases energy and has a negative $\Delta G$. (A)</p> Signup and view all the answers

What is the main purpose of the Calvin Cycle in photosynthesis?

<p>To fix CO2 into glucose using ATP and NADPH. (A)</p> Signup and view all the answers

During cellular respiration, where does glycolysis take place?

<p>Cytoplasm (C)</p> Signup and view all the answers

How does anaerobic respiration differ from aerobic respiration in terms of ATP production?

<p>Anaerobic respiration produces significantly less ATP than aerobic respiration. (D)</p> Signup and view all the answers

Flashcards

Enzymes

Biological catalysts that speed up chemical reactions by lowering the activation energy.

Active site

The location on an enzyme where the substrate binds.

Enzyme-substrate complex

The complex formed when an enzyme binds to its substrate.

Cofactors

Inorganic molecules that assist enzyme function (e.g., metal ions).

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Coenzymes

Organic molecules that aid enzymes (e.g., vitamins).

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Activation energy

The energy needed to initiate a chemical reaction.

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Competitive inhibitors

Bind to the active site, blocking the substrate.

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Noncompetitive inhibitors

Bind to an allosteric site, changing the enzyme's shape.

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Exergonic reaction

Releases energy (cellular respiration, ΔG < 0).

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Endergonic reaction

Requires energy (photosynthesis, ΔG > 0).

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Study Notes

Enzyme Structure

  • Enzymes are biological catalysts that speed up chemical reactions by lowering the activation energy
  • Enzymes are proteins, but some can be RNA-based ribozymes
  • Enzymes have an active site, which is where the substrate binds
  • An active site's shape determines enzyme specificity (lock-and-key vs. induced fit)
  • Enzyme-substrate complex forms when an enzyme binds to the substrate to form an unstable intermediate
  • Enzymes convert a substrate into a product, but they are not consumed in the reaction and can be reused
  • Cofactors are inorganic molecules (e.g., metal ions like Mg2+, Zn2+)
  • Coenzymes are organic molecules (e.g., vitamins like NAD+, FAD)

Enzyme Catalysis

  • Activation energy describes the energy required to start a reaction
  • Enzymes accelerate reactions via stabilizing the transition state and reducing activation energy
  • Proximity and orientation: Enzymes bring substrates together in the correct position
  • Microenvironment: The active site provides an optimal environment (pH, polarity)
  • Induced fit: Enzyme changes shape slightly to better fit the substrate

Environmental Impacts on Enzyme Function

  • As temperature increases, the reaction rate increases up to an optimal temperature
  • High temperatures denature enzymes by breaking hydrogen bonds
  • Low temperatures slow down reactions but do not denature the enzyme
  • Enzymes have an optimal pH (e.g., pepsin in the stomach: pH 2; trypsin in the intestine: pH 8)
  • Extreme pH levels can disrupt ionic bonds and denature enzymes
  • More substrate increases enzyme activity up to saturation point, where all active sites are occupied
  • Competitive inhibitors bind to the active site, blocking the substrate
  • Noncompetitive inhibitors bind to an allosteric site, changing the enzyme's shape
  • Feedback inhibition describes when the product of a reaction inhibits the enzyme that produces it

Cellular Energy

  • Energy transfer describes how energy cannot be created or destroyed, only transferred, as described via the First Law of Thermodynamics
  • The Second Law of Thermodynamics describes how energy transfer increases entropy (disorder)
  • Exergonic reactions release energy (e.g., cellular respiration, ΔG < 0)
  • Endergonic reactions require energy (e.g., photosynthesis, ΔG > 0)
  • ATP (Adenosine Triphosphate) is the main energy currency of the cell
  • Hydrolysis of ATP (ATP → ADP + Pi) releases energy used for cellular work
  • Phosphorylation occurs when transferring a phosphate group to another molecule to activate it

Photosynthesis

  • Photosynthesis converts light energy into chemical energy (glucose)
  • 6CO_2 + 6H_2O + light → C_6H_{12}O_6 + 6O_2
  • Photosynthesis occurs in the chloroplasts of plant cells
  • Light-dependent reactions occur in the thylakoid membrane and convert light energy into ATP and NADPH
  • Photosystem II (PSII) absorbs light, exciting electrons
  • Water is split to replace lost electrons, producing O2
  • The Electron Transport Chain (ETC) pumps H⁺ into the thylakoid lumen, creating a proton gradient
  • ATP Synthase produces ATP by chemiosmosis
  • Photosystem I (PSI) absorbs more light, re-energizing electrons
  • Electrons reduce NADP+ to NADPH for the Calvin cycle
  • The Calvin Cycle occurs in the stroma
  • The Calvin Cycle uses ATP and NADPH from light reactions to fix CO2 into glucose
  • Carbon fixation: Rubisco enzyme fixes CO2 to RuBP
  • Reduction: ATP and NADPH convert 3-PGA to G3P
  • Regeneration: Some G3P is used to regenerate RuBP

Cellular Respiration

  • Produces: Glucose (after two cycles)
  • Cellular respiration converts glucose into ATP
  • C_6H_{12}O_6 + 6O_2 → 6CO_2 + 6H_2O + 36-38 ATP
  • Occurs in mitochondria (except glycolysis)
  • Glycolysis (cytoplasm): Glucose → 2 Pyruvate + 2 ATP + 2 NADH
  • Anaerobic process (does not require O2)
  • Pyruvate oxidation (mitochondrial matrix): Pyruvate → Acetyl-CoA + CO2 + NADH
  • Krebs Cycle (Citric Acid Cycle) (mitochondrial matrix): Acetyl-CoA → 2 CO2 + 3 NADH + FADH2 + ATP
  • Electron Transport Chain (ETC) and Oxidative Phosphorylation (inner mitochondrial membrane)
  • NADH and FADH2 donate electrons to ETC
  • Electrons travel through protein complexes, pumping H+ into the intermembrane space
  • O2 is the final electron acceptor, forming H2O
  • ATP Synthase produces ~34 ATP via chemiosmosis

Fitness and Energy Flow

  • Efficiency of cellular respiration
  • Aerobic respiration = 36-38 ATP per glucose
  • Anaerobic respiration (fermentation) = 2 ATP per glucose
  • Fermentation (Anaerobic respiration) occurs when O2 is absent
  • Lactic acid fermentation (muscles, bacteria): Pyruvate → Lactic acid + NAD+
  • Alcohol fermentation (yeast, some bacteria): Pyruvate → Ethanol + CO2 + NAD+
  • Energy flow in ecosystems:
  • Producers (autotrophs) perform photosynthesis
  • Consumers (heterotrophs) perform cellular respiration
  • Energy is lost as heat at each trophic level (10% rule)

Key Takeaways

  • Enzymes lower activation energy and have specific conditions for optimal function
  • Photosynthesis stores energy in glucose, while cellular respiration releases energy as ATP
  • Aerobic respiration is much more efficient than fermentation
  • ATP is the universal energy molecule used by all cells

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