Enzymes Overview
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Questions and Answers

What is a characteristic of enzymes?

  • They do not require specific environmental conditions.
  • They are consumed in chemical reactions.
  • They decrease the speed of reactions.
  • They exhibit high specificity for substrates. (correct)

All enzymes are made up of proteins.

False (B)

Which enzyme catalyzes the hydrolysis of bonds?

  • Hydrolases (correct)
  • Lyases
  • Ligases
  • Oxidoreductases

What is the complete conjugated enzyme called?

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

Enzymes usually require specific __________ to function properly.

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

Enzymes can catalyze reactions with multiple substrates at the same time.

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

Match the type of enzyme with its description:

<p>Simple enzyme = Consists only of protein Conjugated enzyme = Contains both protein and non-protein portions Holoenzyme = Complete enzyme with both components Coenzymes = Organic molecules often derived from vitamins</p> Signup and view all the answers

What is the term used for the region where an enzyme binds to its substrate?

<p>active site</p> Signup and view all the answers

In __________ inhibition, the inhibitor binds to the enzyme at a site other than the active site.

<p>non-competitive</p> Signup and view all the answers

Which of the following is a reason why enzymes are important in medicine?

<p>Their presence in the bloodstream can indicate diseases. (A)</p> Signup and view all the answers

Enzyme concentration remains constant in all physiological conditions.

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

Match the enzyme with its function:

<p>Amylase = Breaks down starch Urease = Breaks down urea Lactase = Breaks down lactose Lipase = Breaks down fats</p> Signup and view all the answers

What suffix is commonly added to the names of enzymes?

<p>-ase</p> Signup and view all the answers

Which of the following is an example of competitive inhibition?

<p>An inhibitor outcompeting the substrate for the active site (B)</p> Signup and view all the answers

Ligases are enzymes that catalyze oxidation-reduction reactions.

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

The enzyme __________ is responsible for breaking down proteins in the stomach.

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

Flashcards

What are enzymes?

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

How are enzymes classified?

Enzymes are classified based on the specific type of chemical reaction they catalyze.

What is the active site of an enzyme?

The active site is a specific region on an enzyme where the substrate binds and the reaction takes place.

How do enzymes speed up reactions?

Enzymes lower the activation energy required for a reaction to proceed, making it easier and faster.

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Explain competitive inhibition.

Competitive inhibition is when an inhibitor molecule competes directly with the substrate for binding to the active site, preventing the enzyme from functioning.

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Explain non-competitive inhibition.

Non-competitive inhibition is when an inhibitor molecule binds to a site on the enzyme different from the active site, but this binding alters the active site's shape, preventing it from working properly.

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What is enzyme concentration?

Enzyme concentration is the amount of enzyme present in a given solution. Increasing enzyme concentration generally speeds up the reaction rate.

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How can enzyme concentration be decreased?

Enzyme concentration can be decreased if the enzyme is being inhibited.

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What is enzyme specificity?

Enzymes are highly specific, meaning they typically catalyze only one specific reaction or a small group of reactions.

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What factors affect enzyme activity?

The rate of an enzymatic reaction is influenced by factors such as temperature, pH, substrate concentration, and the presence of cofactors.

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Why are enzymes important for life?

Many enzymes are essential for life, as most reactions required to sustain life are not spontaneous and require enzymatic help.

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Where are enzymes found in the body?

Enzymes can be found in various locations within a cell, including the nucleus, cytoplasm, mitochondria, and even outside cells, like digestive enzymes.

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How are enzymes used in medicine?

A change in enzyme concentration in the bloodstream can indicate cell damage or disease. Enzymes are valuable tools in disease diagnosis and treatment.

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What are the types of enzymes based on their structure?

Simple enzymes consist only of protein, while conjugated enzymes contain both protein and non-protein components, such as cofactors, like vitamins or minerals.

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Study Notes

Enzymes

  • Enzymes are proteins, with a few exceptions being RNA.
  • They accelerate reactions significantly, enabling reactions to occur many millions of times faster than without the enzyme.
  • Each enzyme typically catalyzes a single reaction.
  • Enzymes often require cofactors or coenzymes to function.
  • Enzyme function is highly sensitive to environmental factors, including pH, temperature, and substrate concentration and the presence of cofactors.
  • Many enzymes are crucial for life, as most biological processes require enzyme assistance.
  • Enzymes are found in various cellular locations: nucleus, cytoplasm, mitochondria, and extracellularly.
  • Enzyme levels in the bloodstream can indicate cell damage or disease.
  • Enzymes play a vital role in both diagnosing and treating diseases.

Enzyme Properties

  • Most enzymes are proteins.
  • They are sensitive to changes in pH and temperature.
  • Enzymes act as catalysts, accelerating reactions without being consumed in the process.
  • Enzymes are highly efficient, often increasing reaction rates by several orders of magnitude.
  • Enzymes exhibit high specificity, typically working on a single substrate or a narrow group of related substrates.
  • Enzymes possess active sites for substrate binding and subsequent product formation.

Types of Enzymes

  • Simple enzymes are composed solely of protein.
  • Conjugated/Complex enzymes combine a protein portion (apoenzyme) with a non-protein component (cofactor).
    • The complete conjugated enzyme is referred to as a holoenzyme.
  • Cofactors include metals (iron, zinc, calcium, magnesium) and non-protein organic molecules called coenzymes (often vitamins or vitamin derivatives such as NAD+, FAD, and NADP+).

Naming Enzymes

  • Enzymes are named by adding the suffix "-ase" to the substrate's name or a description of the catalyzed reaction.
  • For example, pyruvate dehydrogenase catalyzes the decarboxylation of pyruvate.

Where Enzymes are Found

  • Some enzymes are found outside cells, such as digestive enzymes.
  • Others are located within cells, in the nucleus, mitochondria, or cytoplasm, depending on their specific function.

Enzyme Concentration

  • Enzyme concentration is not fixed, fluctuating based on individual bodily conditions.
  • Enzyme concentration may increase in response to higher substrate levels or increased demand.
  • Enzyme concentration can decrease due to inhibition mechanisms.

Enzyme Classification

  • Enzymes are categorized based on the type of reaction they catalyze.
  • Six major classes of enzymes:
    • Oxidoreductases: Catalyze oxidation-reduction reactions.
    • Transferases: Catalyze the transfer of functional groups.
    • Hydrolases: Catalyze hydrolysis reactions, breaking bonds with water.
    • Lyases: Catalyze the breaking of bonds without hydrolysis or oxidation.
    • Isomerases: Catalyze the rearrangement of atoms within a molecule.
    • Ligases: Catalyze the joining of two or more molecules.

Enzyme Specificity

  • Enzymes display specificity, catalyzing reactions with specific substrates.
  • Enzyme specificity categorizations:
    • Absolute specificity: The enzyme works only with a single substrate for a particular reaction.
    • Group specificity: The enzyme works with a particular functional group.
    • Linkage specificity: The enzyme works on a specific type of chemical bond.
    • Stereospecificity: The enzyme works on a specific stereoisomer.

How Enzymes Work

  • Enzymes bind substrates at specific active sites.
  • Active sites have unique shapes and chemical environments for substrate binding.
  • Once bound, enzymes facilitate reactions by:
    • Lowering the activation energy, facilitating reaction pathways.
    • Stabilizing the transition state, making reaction progress easier.

Enzyme Inhibition

  • Enzyme inhibition occurs when a molecule hinders enzyme activity.
  • Two major types of enzyme inhibition:
    • Competitive inhibition: The inhibitor competes with the substrate for the active site.
    • Non-competitive inhibition: The inhibitor binds to a site other than the active site, altering the enzyme's shape and hindering its function.

Examples of Important Enzymes

  • Urease: Breaks down urea.
  • Pepsin: Breaks down proteins in the stomach.
  • Trypsin: Breaks down proteins in the small intestine.
  • Chymotrypsin: Breaks down proteins in the small intestine.
  • Lactase: Breaks down lactose in the small intestine.
  • Amylase: Breaks down starches in the mouth and small intestine.
  • Lipase: Breaks down fats in the small intestine.
  • Pyruvate dehydrogenase: Involved in glucose breakdown.
  • Acetylcholinesterase: Breaks down the neurotransmitter acetylcholine.

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Description

Explore the fascinating world of enzymes, the specialized proteins that catalyze reactions at remarkable speeds. Learn about their sensitivity to environmental conditions, their roles in cellular functions, and their significance in diagnosing diseases. This quiz covers essential characteristics and properties of enzymes.

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