Enzyme Overview and Functions

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Questions and Answers

What is the term for the catalytically active form of an enzyme?

  • Cofactor
  • Apoenzyme
  • Substrate
  • Holoenzyme (correct)

Which factor does not affect enzyme activity?

  • Enzyme concentration
  • Substrate shape (correct)
  • Temperature
  • pH

What is the unit of activity for an enzyme?

  • 1 mmol substrate converted in 1 minute
  • 1 µmol substrate converted in 1 hour
  • 1 µmol substrate converted in 1 minute (correct)
  • 1 nmol substrate converted in 1 minute

What does the Km value indicate in enzyme kinetics?

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

What defines the optimum temperature for an enzyme?

<p>The temperature where it exhibits maximum activity (C)</p> Signup and view all the answers

What type of inhibitor permanently alters enzyme activity?

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

Enzymes in humans typically show maximum activity at what temperature range?

<p>35-40 °C (B)</p> Signup and view all the answers

Which statement is true regarding enzyme concentration?

<p>Higher enzyme concentration increases the potential reaction rate. (A)</p> Signup and view all the answers

What is the primary role of enzymes in biochemical reactions?

<p>To decrease the activation energy (A)</p> Signup and view all the answers

Which type of enzyme is responsible for catalyzing oxidation-reduction reactions?

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

Which statement accurately describes the efficiency of enzyme-catalyzed reactions?

<p>They are highly efficient, proceeding from 10³ to 10⁸ times faster. (D)</p> Signup and view all the answers

What distinguishes enzymes in terms of specificity?

<p>They exhibit reaction specificity and substrate specificity. (C)</p> Signup and view all the answers

What is the relationship between enzyme activity and the Michaelis constant (Km)?

<p>Lower Km values suggest higher enzyme affinity for the substrate. (D)</p> Signup and view all the answers

Which of the following is NOT a classification of enzymes?

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

Which of the following characteristics is true for all enzymes?

<p>Most enzymes are proteins, albeit some are ribozymes. (D)</p> Signup and view all the answers

What defines a catalyst in the context of enzymatic reactions?

<p>A catalyst decreases the activation energy and is not consumed. (B)</p> Signup and view all the answers

Flashcards

Apoenzyme

The protein part of an enzyme.

Cofactor

The non-protein component of an enzyme that aids in catalytic activity.

Holoenzyme

The fully functional, catalytically active form of an enzyme, composed of both apoenzyme and cofactor.

Active site

The specific region on an enzyme where substrate binds and catalysis occurs.

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Enzyme Activity

The rate of substrate conversion to product, expressed as the amount of substrate transformed in a given time.

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Optimum temperature for an enzyme

The temperature at which an enzyme exhibits its maximum activity.

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Optimum pH for an enzyme

The pH at which an enzyme shows its highest activity.

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Inhibitor

Any substance that reduces the rate of an enzyme-catalyzed reaction.

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Enzymes

Biological catalysts that speed up chemical reactions within living organisms.

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Enzyme Composition

Enzymes are primarily proteins, but some are also made of RNA, known as ribozymes.

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Enzyme Function

Enzymes accelerate the rate of a chemical reaction without altering the reaction's equilibrium.

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Enzyme Specificity

Enzymes display specificity, meaning they only work on a specific type of molecule (the substrate) and catalyze a particular reaction type.

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Activation Energy and Enzymes

Enzymes accelerate reactions by lowering the activation energy, which is the energy required for a reaction to start.

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Enzyme Classification

Enzymes are categorized into six classes based on the type of reaction they catalyze: Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, and Ligases.

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Michaelis-Menten Constant (Km)

The Michaelis-Menten constant (Km) is a measure of the substrate concentration at which the enzyme's reaction rate is half its maximum velocity. A lower Km indicates higher affinity of the enzyme for its substrate.

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Enzyme Inhibition

Enzyme inhibition occurs when a molecule binds to an enzyme and decreases its activity. There are three main types: competitive, non-competitive, and uncompetitive.

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Study Notes

Enzyme Overview

  • Enzymes are biological catalysts
  • They increase the rate of biochemical reactions
  • They are highly specific for their substrate and reaction type
  • Enzymes are not consumed in the reaction
  • Most are proteins, some are ribozymes (RNA)
  • Lower activation energy by stabilizing the transition state

Learning Objectives for Enzymes

  • Describe enzymes and their properties
  • List enzyme classifications
  • Describe factors affecting enzyme activity
  • Explain the relationship between Km and enzyme activity
  • Explain enzyme inhibition and different types of inhibition

Metabolic Reactions and Enzymes

  • Enzymes facilitate metabolic reactions, including both anabolic (building up) and catabolic (breaking down) pathways
  • Enzymes increase the rate of these reactions, which are fundamental to life processes
  • Enzymes catalyze reactions by lowering activation energy
  • This speeds up reaction rates
  • Enzymes can modify molecules by binding temporarily for transport, degradation, or modifications within cells.
  • With some special molecules

Glycolysis Overview

  • Glycolysis is a metabolic process that breaks down glucose into pyruvate
  • Enzymes are crucial to facilitate these reactions (e.g., hexokinase, phosphofructokinase, etc.)
  • Each reaction step is catalyzed by specific enzymes

Enzyme Activity

  • Enzyme activity is the rate at which an enzyme catalyzes a reaction
  • Measured by the amount of substrate converted to product in a given time
  • One unit of enzyme activity converts 1 μmol of substrate to product in one minute under optimal conditions
  • Enzyme activity is influenced by several factors, including enzyme concentration, substrate concentration, temperature, pH, and inhibitors.
  • Enzyme activity can be measured and optimized according to these factors

Factors Affecting Enzyme Activity

  • Enzyme concentration: Higher concentration, faster reaction
  • Substrate concentration: More substrate, speeds reaction up until saturation
  • Temperature: Optimal temperature for max efficiency; high temp, denatures/slows reactions
  • pH: Affects enzyme structure and function (optimal pH for every enzyme)
  • Inhibitors: Substrates that reduce enzyme rate.

Enzyme Nomenclature

  • Enzymes are classified in an organized way
  • This is done according to their function (i.e. oxidoreductases, transferases, hydrolases, etc.)
  • Each enzyme is given a unique EC number for precise identification

Enzyme Kinetics and Km

  • Km reflects the enzyme's affinity for its substrate
  • Low Km means higher affinity (higher substrate concentration required to reach half V-max)
  • High Km means lower affinity (requires high substrate concentration to get half Vmax)
  • Vmax is the maximum reaction rate of an enzyme

Enzyme Regulation

  • Factors influencing enzyme activity
  • Enzymes can be regulated by changing the amount (synthesis/degradation), enzyme modification (e.g., phosphorylation / dephosphorylation), or the compartments in a cell.
  • These factors influence enzyme activity at different stages/steps

Isoenzymes

  • Enzymes that share the same catalytic function but have different structures(sequences) and different regulatory properties
  • Examples include lactate dehydrogenase and creatine kinase
  • Can be used to distinguish between different tissues or cellular conditions

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