Enzymes in the Human Body
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Questions and Answers

What is the primary role of enzymes in the human body?

  • To provide structural support to cells
  • To transport nutrients across cell membranes
  • To release energy from food
  • To accelerate biological processes (correct)

Which of the following statements is true about ribozymes?

  • They do not catalyze chemical reactions
  • They can catalyze reactions among RNAs (correct)
  • They are found only in the liver
  • They are solely composed of protein

What happens to an enzyme's activity when its structure is denatured due to heat?

  • It loses its enzymatic activity (correct)
  • It remains functional but slows down
  • It changes its substrates
  • Its activity increases significantly

What determines the catalytic activity of an enzyme?

<p>The sequence of amino acids in its structure (A)</p> Signup and view all the answers

What type of molecules typically act as substrates for enzymes?

<p>Molecules that the enzymes interact with (B)</p> Signup and view all the answers

In which part of the body do intracellular enzymes primarily function?

<p>In all tissues and fluids (C)</p> Signup and view all the answers

Which of the following enzyme sizes is true based on provided information?

<p>Enzymes can vary from 62 to 2500 amino acid residues (A)</p> Signup and view all the answers

What role do enzymes in the circulatory system play?

<p>Regulating blood clotting (A)</p> Signup and view all the answers

What happens to enzyme activity once all enzyme molecules are occupied by substrate?

<p>The enzyme activity ceases. (A)</p> Signup and view all the answers

Which statement correctly describes a competitive inhibitor?

<p>It structurally resembles the specific substrate and competes for the active site. (C)</p> Signup and view all the answers

How does an increase in substrate concentration initially affect enzyme activity?

<p>Enzyme activity increases until a saturation point is reached. (C)</p> Signup and view all the answers

Which of the following factors does NOT affect enzyme activity?

<p>Pressure levels. (D)</p> Signup and view all the answers

What role do enzymes play in the human body?

<p>Enzymes facilitate various chemical reactions. (A)</p> Signup and view all the answers

What constitutes the active site of an enzyme?

<p>The catalytic site and binding site (B)</p> Signup and view all the answers

Which classification of enzymes catalyzes oxidation and reduction reactions?

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

What type of enzyme is pepsin?

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

Which enzyme catalyzes the joining of two fragments of DNA?

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

In the induced-fit model, what does the binding of the substrate induce?

<p>Weak interactions and conformational changes in the enzyme (B)</p> Signup and view all the answers

What is a cofactor?

<p>A non-protein, essential substance for enzyme activity (B)</p> Signup and view all the answers

What mechanism of catalysis involves the formation of a covalent bond between substrate and enzyme?

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

What role does activation energy play in enzyme-catalyzed reactions?

<p>It must be reduced by an enzyme to facilitate the reaction (A)</p> Signup and view all the answers

What is the primary function of transferases?

<p>To transfer chemical groups between compounds (A)</p> Signup and view all the answers

Which of the following is NOT a type of enzyme classification?

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

Which process demonstrates the effect of enzyme action in fermentation?

<p>Formation of carbon dioxide in bread rising (A)</p> Signup and view all the answers

What type of enzymes catalyzes the rearrangement of molecular structures?

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

The process in which alcohol is produced from fermentation largely depends on which factor?

<p>Plant species and applied enzymes (A)</p> Signup and view all the answers

What happens to substrate and enzyme during the transition state?

<p>They undergo weak interactions leading to strain (C)</p> Signup and view all the answers

What component of the enzymatic action is referred to as the transition state?

<p>The intermediate complex formed after substrate binding (B)</p> Signup and view all the answers

Which amino acids are primarily involved in enzyme active site catalysis?

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

How do enzymes affect the activation energy of reactions?

<p>They lower the activation energy required. (A)</p> Signup and view all the answers

What happens to enzyme activity at temperatures higher than the optimum level?

<p>Enzyme activity decreases due to denaturation. (C)</p> Signup and view all the answers

Which factor does not influence enzyme activity?

<p>Color of the substrate (B)</p> Signup and view all the answers

What is a key characteristic of biological catalysts?

<p>They remain unchanged after the reaction. (B)</p> Signup and view all the answers

What defines the specificity of an enzyme?

<p>The shape and structure of its active site. (A)</p> Signup and view all the answers

How does substrate concentration affect the rate of enzymatic reactions?

<p>At low concentrations, reaction rate increases with concentration. (C)</p> Signup and view all the answers

In which pH range do most enzymes exhibit optimal activity?

<p>Near neutrality, typically around 5 to 7 (B)</p> Signup and view all the answers

Which statement best describes the role of allosteric regulation in enzyme activity?

<p>It allows enzymes to respond to cellular conditions. (B)</p> Signup and view all the answers

What is the first step in the catalytic action of enzymes?

<p>Combining of enzyme and substrate. (D)</p> Signup and view all the answers

What is denaturation in the context of enzymes?

<p>The alteration of an enzyme's structure, leading to loss of function. (B)</p> Signup and view all the answers

Which process describes how enzymes lower activation energy?

<p>By stabilizing the transition state. (D)</p> Signup and view all the answers

What occurs during the disintegration of the enzyme-substrate complex?

<p>The product is released and the enzyme is regenerated. (B)</p> Signup and view all the answers

Flashcards

What are enzymes?

Enzymes are biological catalysts, mostly proteins, that speed up chemical reactions in living organisms without being consumed in the process.

What is a substrate?

The molecule that an enzyme acts upon is called a substrate. Enzymes bind to their specific substrates and convert them into different molecules called products.

What is the active site of an enzyme?

The shape of an enzyme determines its function. The active site is a specific region on the enzyme where the substrate binds and the reaction takes place.

What is denaturation?

The process of enzymes losing their shape and activity due to factors like heat or extreme pH is called denaturation. This disrupts the enzyme's active site, making it unable to bind to its substrate.

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What is the optimal temperature and pH for enzymes?

Enzymes work best at an optimal temperature and pH. Outside of this range, their activity may decrease or stop due to changes in their structure.

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What are ribozymes?

Ribozymes are catalytic RNA molecules that can act as enzymes. They are involved in various cellular processes, such as protein synthesis.

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What are intracellular enzymes?

Intracellular enzymes are found within cells and catalyze reactions within the cell's metabolic pathways.

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Why are enzymes important?

Enzymes are crucial for maintaining essential life processes. They play a vital role in various biological processes, including metabolism, digestion, and immunity.

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Active site

The site on an enzyme where the substrate binds and the chemical reaction takes place.

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Cofactor

A non-protein molecule that helps an enzyme function correctly.

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Apoenzyme

The protein part of an enzyme, without its cofactor.

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Holoenzyme

The complete, functional enzyme, including both the protein part (apoenzyme) and the non-protein part (cofactor).

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Oxidoreductases

A group of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons.

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Transferases

A group of enzymes that catalyze the transfer of functional groups, such as amino groups or phosphate groups, between molecules.

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Hydrolases

A group of enzymes that catalyze the breaking of bonds using water.

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Lyases

A group of enzymes that catalyze the breaking of bonds without using water.

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Isomerases

A group of enzymes that catalyze the rearrangement of atoms within a molecule, creating an isomer.

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Ligases

A group of enzymes that catalyze the joining of two molecules, often forming a new bond.

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Substrate

The molecule that an enzyme acts upon.

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Activation energy

The minimum amount of energy required for a chemical reaction to occur.

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Induced-fit model

A model describing how enzymes and substrates interact. The enzyme changes shape slightly to fit the substrate better.

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Catalysis by bond strain

A type of catalysis where the enzyme distorts the substrate's bonds, making it easier to break.

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Covalent catalysis

A type of catalysis where the enzyme forms a temporary covalent bond with the substrate.

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Enzyme Saturation Point

The point where adding more substrate doesn't increase the reaction speed. This is because all the active sites on enzymes are already occupied by substrate molecules.

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Enzyme Inhibitors

Chemicals that block an enzyme's active site, preventing it from binding to its specific substrate and carrying out its function.

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Competitive Inhibitor

A type of inhibitor that competes with the normal substrate for the same active site on the enzyme.

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Salt Concentration's Effect on Enzymes

Changes in the amount of salts in a solution can affect enzyme activity because they can alter the enzyme's shape and charge, potentially disrupting its active site.

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Enzymes increase reaction rates by...

They bring together reactants, orienting them correctly for the reaction to happen more efficiently.

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Denaturation

The process where an enzyme loses its shape and ability to function due to factors like extreme temperature or pH.

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Optimum Temperature

The temperature at which an enzyme exhibits its highest activity.

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Optimum pH

The pH at which an enzyme shows its highest activity.

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Enzyme-Substrate Complex

The temporary complex formed when a substrate binds to the active site of an enzyme.

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Specificity of Enzymes

Enzymes are highly specific, typically catalyzing a single or a limited set of reactions.

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How do enzymes speed up reactions?

By lowering the activation energy required for the reaction to occur.

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Binding of Enzyme and Substrate

The initial step in enzymatic catalysis where the enzyme forms a complex with the substrate.

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Transition State

The intermediate state between the substrate and the product, formed in the process of enzymatic catalysis.

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Product

The final molecule formed by the enzymatic reaction, resulting from the transformation of the substrate.

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Catalysis

The process by which a catalyst, including an enzyme, alters the rate of a chemical reaction without being consumed in the process.

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What are enzymes made of?

Enzymes are often made of proteins, but some are made of RNA molecules called ribozymes.

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Denaturation of Enzymes

The process where the original structure of the enzyme is disrupted, causing it to lose its activity.

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Study Notes

Enzymes: Biological Catalysts

  • Enzymes are protein molecules with catalytic activity, crucial for metabolic processes and chemical reactions in cells.
  • Enzymes react with a molecule (substrate) and convert it into a different molecule (product).
  • Enzyme regulation is vital for clinical diagnosis.
  • Ribozymes are RNA catalysts.
  • Enzymes are present in all tissues and fluids. Intracellular enzymes catalyze metabolic pathways; membrane-bound enzymes respond to cellular signals; circulatory enzymes regulate blood clotting, etc.

Enzyme Structure

  • Enzymes are linear chains of amino acids forming a 3D structure.
  • Amino acid sequence determines the enzyme's structure and catalytic activity.
  • Enzyme structure denatures, and activity is lost with heat.
  • Enzymes are large molecules, much larger than their substrates, ranging from 62 to 2,500+ amino acid residues.
  • Only a small part (active site) of the enzyme is involved in catalysis, consisting of the catalytic and binding sites.
  • Some ribozymes are RNA biological catalysts combined with proteins.

Enzyme Classification

  • Enzymes are classified into six functional classes according to the type of reaction they catalyze (International Union of Biochemists - IUB).
    • Oxidoreductases: Catalyze oxidation-reduction reactions (e.g., pyruvate dehydrogenase).
    • Transferases: Transfer chemical groups between molecules (e.g., transaminase).
    • Hydrolases: Catalyze hydrolysis reactions (e.g., pepsin hydrolyzes peptide bonds in proteins).
    • Lyases: Break bonds without the addition of water (e.g., aldolase).
    • Isomerases: Catalyze the formation of isomers (e.g., phosphoglucomutase).
    • Ligases: Join two molecules together (e.g., DNA ligase).

Cofactors

  • Cofactors are non-protein components essential for enzyme function.
  • The protein part of an enzyme is the apoenzyme.
  • Enzyme + cofactor = holoenzyme.
  • Cofactors can be metal ions or organic molecules (coenzymes).

Examples of Enzyme Action

  • Beverages: Fermentation varies depending on the plant product and enzyme used (e.g., grapes, honey, hops, etc. for wine, beer).
  • Food: Bread fermentation uses yeast and sugar to produce carbon dioxide gas, giving the bread its texture.
  • Drug action: Drugs can inhibit or promote enzyme activity by affecting the active site.

Mechanism of Enzyme Action

  • Collision theory: Molecules must collide with the correct orientation and sufficient energy (activation energy).
  • Active site: Enzymes have a specific shape and functional groups for substrate binding.
  • Enzyme-substrate complex: The enzyme and substrate bind weakly, but this interaction induces conformational changes.
  • Induced fit model: The binding between enzyme and substrate strengthens with changes, with the active site adapting to fit.
  • Catalysis Mechanisms: Enzymes use various mechanisms:
    • Bond strain: The enzyme strains substrate bonds.
    • Covalent catalysis: Covalent intermediates form between enzyme and substrate.
    • Acid/base catalysis: Enzymes use amino acid side chains as acid or base catalysts.
    • Orientation and proximity: Brings substrate groups together
  • Two-step process: -Enzyme + substrate → enzyme-substrate complex -enzyme-substrate complex → product + enzyme

Factors Affecting Enzyme Activity

  • Temperature: Optimal temperature increases activity, but extreme temperatures denature the enzyme.
  • pH: Most enzymes have an optimal pH near neutrality, but some function in more extreme conditions. pH changes can affect amino acid charges (and thus enzyme activity).
  • Substrate concentration: Low substrate concentration affects reaction rate, but high concentration leads to saturation, where reaction rate plateau.
  • Inhibitors: Inhibitors can bind to the active site blocking substrate binding (competitive inhibitors) affecting enzyme activity.
  • Salt concentration: Changes in salinity can affect protein folding and interactions, thus enzyme function.

Active Site

  • The active site's amino acid residues are crucial for catalysis and substrate binding.
  • Active site amino acids are not necessarily contiguous, but are properly positioned by 3D folding.
  • Common active site residues include polar amino acids, aspartate, cysteine, glutamate, histidine, serine, and lysine.

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Description

This quiz explores the essential roles enzymes play within the human body, including their catalytic activities and the effects of various factors on their performance. Test your knowledge on enzyme functionality, substrates, and inhibitors while learning about the significance of enzymes in biological processes.

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