Enzyme Structure and Function

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Questions and Answers

What is the primary function of enzymes in biological systems?

  • To store genetic information
  • To slow down chemical reactions
  • To speed up chemical reactions (correct)
  • To provide structural support

Enzymes are always made of only one polypeptide chain.

False (B)

What is the specific region on an enzyme where the substrate binds?

active site

The _____ model describes how the enzyme and substrate change shape upon binding.

<p>induced-fit</p> Signup and view all the answers

Match the following terms with their corresponding descriptions:

<p>Enzyme = A globular protein that catalyzes a specific reaction Substrate = The molecule that binds to the enzyme's active site Active Site = The specific region on an enzyme where the substrate binds Induced-fit model = A model explaining enzyme-substrate interactions and conformational changes</p> Signup and view all the answers

What happens to an enzyme when it undergoes denaturation?

<p>The enzyme's active site is altered, and it is no longer able to bind to its substrate. (C)</p> Signup and view all the answers

Enzymes are primarily composed of globular proteins.

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

What is the bare minimum of energy required for a chemical reaction to occur?

<p>Activation energy</p> Signup and view all the answers

Enzymes ______ the activation energy of biochemical reactions.

<p>lower</p> Signup and view all the answers

What is the primary factor determining the rate of enzyme activity?

<p>The frequency of collisions between the enzyme and its substrate. (D)</p> Signup and view all the answers

A higher substrate concentration always leads to a faster reaction rate for an enzyme.

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

Match the following terms with their definitions:

<p>Activation energy = The energy required for reactant molecules to collide and break/form bonds during a reaction. Denaturation = Disruption of an enzyme's structure due to factors like heat or pH changes. Globular protein = A protein folded into a rounded shape, often found in enzymes. Enzyme-substrate complex = The temporary association of an enzyme with its substrate, facilitating the catalytic reaction.</p> Signup and view all the answers

Explain how enzymes facilitate chemical reactions.

<p>Enzymes lower the activation energy of reactions by providing an alternate pathway with a lower energy requirement. This allows reactions to occur more readily at a faster rate.</p> Signup and view all the answers

The collision frequency always increases as substrate concentration increases.

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

What happens to the reaction rate when the enzyme's active sites are saturated with substrate molecules?

<p>The reaction rate reaches its maximum capacity and does not increase further.</p> Signup and view all the answers

The ______ of an enzyme is the specific condition (temperature or pH) where it functions most effectively.

<p>optimum</p> Signup and view all the answers

Which of the following factors influences enzyme activity?

<p>Substrate concentration (A), Temperature (B), pH (C)</p> Signup and view all the answers

According to collision theory, why is it necessary for substrate molecules to collide with enzyme active sites?

<p>Collisions allow for the substrate to bind with the active site, forming an enzyme-substrate complex. This binding facilitates the chemical reaction that the enzyme catalyzes.</p> Signup and view all the answers

Adding more enzyme to a reaction mixture always increases the reaction rate.

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

What is the most likely outcome of increasing the temperature significantly above an enzyme's optimum temperature?

<p>Denaturation of the enzyme (D)</p> Signup and view all the answers

Proteins are polymers made by joining amino acids through peptide bonds, which are formed through a hydrolysis reaction.

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

What is the primary structure of a protein determined by?

<p>The order of amino acids in the polypeptide chain (D)</p> Signup and view all the answers

The process of breaking down large molecules into smaller ones is called ______.

<p>catabolism</p> Signup and view all the answers

Explain how temperature can affect the structure and function of a protein.

<p>High temperatures can disrupt the weak bonds (like hydrogen bonds) that help maintain the protein's structure. This disruption, called denaturation, causes the protein to lose its shape and ability to function properly.</p> Signup and view all the answers

What is the primary role of enzymes in metabolic reactions?

<p>They increase the rate of reactions by lowering the activation energy. (D)</p> Signup and view all the answers

Increasing the temperature always increases the rate of an enzyme-catalyzed reaction.

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

Describe the relationship between substrate concentration and the rate of an enzyme-catalyzed reaction.

<p>As substrate concentration increases, the rate of the reaction also increases until all active sites on the enzyme are occupied. At this point, the enzyme is saturated, and the reaction rate plateaus even with further increases in substrate concentration.</p> Signup and view all the answers

The process of breaking down complex molecules into simpler ones with the addition of water is called ______.

<p>hydrolysis</p> Signup and view all the answers

Match the following enzyme types with their respective roles in metabolic processes:

<p>Synthase = Catalyzes the breakdown of complex molecules into smaller ones. Hydrolase = Catalyzes the synthesis of complex molecules from simpler ones.</p> Signup and view all the answers

Anabolic reactions are energy-releasing processes.

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

Which of the following is an example of an anabolic process?

<p>Protein synthesis (A)</p> Signup and view all the answers

Which of the following is NOT a type of interaction that contributes to the tertiary structure of a protein?

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

The optimum pH for most enzymes is 7, which is a neutral pH.

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

What are the two main types of secondary protein structures?

<p>Alpha helices and beta sheets</p> Signup and view all the answers

The process of unfolding or breaking down a protein is called ______.

<p>denaturation</p> Signup and view all the answers

Match the level of protein structure with its corresponding description:

<p>Primary Structure = The three-dimensional folding of a single polypeptide chain Secondary Structure = The linear sequence of amino acids joined by peptide bonds Tertiary Structure = Regular structures formed by hydrogen bonds between backbone atoms Quaternary Structure = The arrangement of multiple polypeptide chains in a functional protein complex</p> Signup and view all the answers

Which level of protein structure is primarily responsible for the overall shape and stability of the protein?

<p>Secondary Structure (A)</p> Signup and view all the answers

Disulfide bridges are a type of ionic bond that contributes to the tertiary structure of proteins.

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

What is the significance of the primary structure of a protein?

<p>The sequence of amino acids in the primary structure determines the higher levels of protein structure, including its shape and function.</p> Signup and view all the answers

Flashcards

Denaturation

The disruption of an enzyme's structure due to external factors like heat or pH.

Active Site

The specific region of an enzyme where substrate binding occurs.

Globular Protein

Proteins that are folded into a rounded shape, important for enzyme function.

Enzyme Function

Enzymes lower the activation energy needed for biochemical reactions.

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Activation Energy

The minimum energy required for a chemical reaction to occur.

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Enzyme-Substrate Complex

The temporary complex formed when an enzyme binds to its substrate.

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Collision Frequency

The rate at which enzyme and substrate molecules collide, affecting enzyme activity.

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Reaction Rate

The speed at which reactants are converted to products in a chemical reaction.

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Enzymes

Globular proteins that serve as catalysts speeding up reactions.

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Induced-Fit Model

Theory describing how enzyme shape changes to fit the substrate.

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Substrate Specificity

An enzyme's ability to act on a specific substrate.

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Catalytic Bonds

Bonds within the active site that react with substrates to form products.

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Polypeptide Chains

Amino acids linked together forming the structure of enzymes.

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Chemical Reaction Speed

Enzymes increase the rate at which reactions occur in the body.

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Enzyme Saturation

A state where all active sites of an enzyme are occupied by substrate, maximizing activity.

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Optimal Temperature

The temperature at which an enzyme's activity is at its peak, ensuring maximum reaction rate.

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Optimal pH

The pH level at which an enzyme performs best, with a suitable shape for catalyzing reactions.

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Catalyst

A substance that increases the rate of a chemical reaction without being consumed.

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Collision Theory

The theory that particles must collide to react, affecting reaction rates.

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Anabolism

A metabolic process where simple molecules combine to form complex molecules.

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Catabolism

Metabolic processes that break down large molecules into smaller ones.

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Condensation

A reaction where monomers join to form polymers, releasing water.

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Hydrolysis

A chemical reaction where water breaks bonds in large molecules.

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Amino Acids

The building blocks (monomers) of proteins, there are 20 types.

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Peptide Bond

A covalent bond formed between the amine and carboxyl groups of amino acids.

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Protein Denaturation

The loss of protein structure due to environmental factors like temperature and pH.

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Protein Structure Levels

Proteins have primary, secondary, tertiary, and quaternary structures affecting function.

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Primary Structure

The linear sequence of amino acids in a protein, held by peptide bonds.

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Secondary Structure

Folding of polypeptide chains into alpha helices and beta sheets due to hydrogen bonds.

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Tertiary Structure

The 3D folding of a single polypeptide chain influenced by side chain interactions.

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Quaternary Structure

Formed when two or more polypeptide chains join to create a functional protein complex.

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Enzyme stability

The ability of an enzyme to maintain its activity under various conditions.

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Molecular Motion

Movement of particles that can be vibrational, translational, or rotational.

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Substrate Concentration

The amount of substrate available for enzyme reactions.

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Saturation

When all enzyme active sites are occupied, preventing further reaction rate increases.

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Condensation Reaction

A reaction where smaller molecules combine to form a larger molecule, releasing water.

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Study Notes

Enzyme Structure and Function

  • Enzymes are globular proteins that act as catalysts, speeding up chemical reactions in living organisms.
  • The active site of an enzyme binds specifically to its substrate.
  • The induced-fit model shows how the enzyme and substrate change shape upon binding for better function
  • Enzyme activity can be affected or destroyed by factors like heat and pH changes, resulting in denaturation and loss of function.
  • Enzymes are proteins made of amino acids joined by peptide bonds forming polypeptide chains that fold into complex three-dimensional shapes.
  • Enzymes help accelerate reactions by lowering the activation energy
  • Enzymes are involved in every metabolic process in living organisms.
  • Each enzyme has a unique active site with a specific shape and chemical properties that facilitate precise binding with its substrate.
  • The active site of an enzyme can be compared to a lock (enzyme) and key (substrate).
  • Enzymes work efficiently at specific temperature and pH ranges.

Enzyme Activity and Catalysis

  • Enzymes lower the activation energy for chemical reactions.
  • Activation energy is the minimum energy required to initiate a reaction.
  • Enzymes speed up reactions by providing an alternative reaction pathway with a lower activation energy.
  • The rate of enzyme activity is influenced by the frequency of collisions between the enzyme and substrate molecules.
  • Enzyme activity increases as substrate concentration increases, up to the point maximum capacity is reached, where the enzyme is saturated causing no further increase in reaction rate.
  • Enzymes work optimally at specific temperature and pH ranges.

Enzyme Roles in Metabolism

  • Metabolism is the web of all enzyme-catalyzed reactions in a cell or organism.
  • Anabolism involves synthesizing complex molecules from simpler molecules requiring energy.
  • Catabolism involves breaking down complex molecules into simpler molecules, releasing energy.
  • Enzymes play a critical role in both anabolic and catabolic pathways such as glycolysis and photosynthesis.

Protein Structure and Environmental Factors

  • Proteins are made from amino acids linked by peptide bonds.
  • The primary structure of a protein is its linear sequence of amino acids.
  • Secondary structure involves folding of the polypeptide chain into structures like alpha-helices and beta-sheets.
  • Tertiary structure is the three-dimensional shape of the protein.
  • Quaternary structure refers to the arrangement of multiple polypeptide chains in proteins with multiple subunits.
  • Factors affecting protein structure include pH, temperature, and other environmental conditions, such as high salt concentrations.
  • Extreme changes in conditions like high temperature and changes in pH can cause a disruption in protein shape (denaturation) leading to a loss of function.
  • Enzymes operate optimally at certain temperature and pH ranges.

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