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Questions and Answers
What is the primary function of a catalyst in a chemical reaction?
What is the primary function of a catalyst in a chemical reaction?
- To decrease the reaction rate by binding to the substrate.
- To be consumed in the reaction and become part of the product.
- To increase the reaction rate without being permanently altered. (correct)
- To shift the reaction's equilibrium towards the products.
In the context of an enzymatic reaction, what does the symbol ⇌ typically signify?
In the context of an enzymatic reaction, what does the symbol ⇌ typically signify?
- The reaction is reversible. (correct)
- The reactants and products exist in equal concentrations.
- The reaction only proceeds towards the products.
- The reaction is irreversible.
Which of the following statements is true regarding the effect of enzymes on reaction equilibrium?
Which of the following statements is true regarding the effect of enzymes on reaction equilibrium?
- Enzymes shift the equilibrium to favor substrate formation.
- Enzymes have no effect on the equilibrium position. (correct)
- Enzymes increase the concentrations of both products and substrate.
- Enzymes shift the equilibrium to favor product formation.
What does the term 'activation energy' refer to in the context of chemical reactions?
What does the term 'activation energy' refer to in the context of chemical reactions?
How do enzymes affect the activation energy of a reaction?
How do enzymes affect the activation energy of a reaction?
What is a 'substrate' in the context of an enzymatic reaction?
What is a 'substrate' in the context of an enzymatic reaction?
Which of the following best describes the transition state in an enzymatic reaction?
Which of the following best describes the transition state in an enzymatic reaction?
What is the typical optimal pH environment in which most human enzymes function?
What is the typical optimal pH environment in which most human enzymes function?
According to the content, what is the typical optimum temperature at which most human enzymes function?
According to the content, what is the typical optimum temperature at which most human enzymes function?
What are the catalytic RNA molecules called?
What are the catalytic RNA molecules called?
What is the primary role of an enzyme in a chemical reaction?
What is the primary role of an enzyme in a chemical reaction?
Which of the following best describes a coenzyme?
Which of the following best describes a coenzyme?
What is a holoenzyme?
What is a holoenzyme?
Which enzyme class is responsible for catalyzing the joining of two molecules?
Which enzyme class is responsible for catalyzing the joining of two molecules?
Which of the following enzymes has the largest rate enhancement between its catalysed and uncatalysed rate?
Which of the following enzymes has the largest rate enhancement between its catalysed and uncatalysed rate?
An enzyme that facilitates the conversion of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P) belongs to which class?
An enzyme that facilitates the conversion of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P) belongs to which class?
Which of these would be considered a cofactor?
Which of these would be considered a cofactor?
A reaction involving the breaking of a peptide bond in a protein is most likely catalyzed by which class of enzyme?
A reaction involving the breaking of a peptide bond in a protein is most likely catalyzed by which class of enzyme?
Which of the following describes what happens to the equilibrium of a reaction when an enzyme is added?
Which of the following describes what happens to the equilibrium of a reaction when an enzyme is added?
The reaction alcohols ⇌ aldehydes is likely catalyzed by which class of enzyme?
The reaction alcohols ⇌ aldehydes is likely catalyzed by which class of enzyme?
Flashcards
Activation Energy
Activation Energy
The minimum amount of energy required for a chemical reaction to occur. Enzymes lower this energy barrier, speeding up reactions.
Coenzyme
Coenzyme
A compound derived from a vitamin that assists an enzyme in catalyzing a reaction.
Cofactor
Cofactor
An inorganic ion that assists an enzyme in catalyzing a reaction.
Apoenzyme
Apoenzyme
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Holoenzyme
Holoenzyme
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Enzyme
Enzyme
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Reaction Rate
Reaction Rate
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Half-life
Half-life
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Oxidoreductase
Oxidoreductase
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Ligase
Ligase
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Catalyst
Catalyst
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Substrate
Substrate
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Product
Product
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Lowering Activation Energy
Lowering Activation Energy
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Transition State
Transition State
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Equilibrium
Equilibrium
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Enzyme Effect on Equilibrium
Enzyme Effect on Equilibrium
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Study Notes
Copyright Information
- La Trobe University reproduced the material under the Copyright Act 1968 (part VB).
- Any further reproduction is subject to copyright protection.
- Do not remove the copyright notice.
Enzyme Features and Classes
- Enzymes are biological catalysts that increase reaction rates without being consumed.
- They accelerate reactions by lowering the activation energy.
- Enzymes are primarily proteins, although some are catalytic RNA molecules called ribozymes.
- Enzymes operate optimally at pH 7.4 and 37°C (for most human enzymes).
Intended Learning Outcomes
- Students will understand enzymes as catalysts in biochemical reactions.
- Students will identify basic enzyme features.
- Students will describe the major enzyme classes.
- Students will grasp that enzymes reduce activation energy but do not alter equilibrium.
Enzymatic Equation
- Enzymatic reactions follow the general equation: E + S ⇌ ES ⇌ EP ⇌ E + P,
- Where E = enzyme, S = substrate, and P = product.
- Substrate is the molecule the enzyme acts on.
- Product is the molecule formed from the reaction.
Reaction Rate vs. Equilibrium
- Reaction rate measures substrate and product concentration change.
- Equilibrium is where these concentrations no longer change in a closed system.
- Equilibrium does not necessitate equal substrate and product concentrations.
- Enzymatic equations usually use the reversible sign to signify reversibility of the reaction.
Equilibrium in Simple Terms
- At equilibrium, the system balances; no net change in substrate or product quantities.
- Reactions still occur in both directions but their rates are equal.
- Equilibrium denotes a dynamic state where reaction rates are equal in both directions.
Enzymes Increase Reaction Rate
- Enzymes do not change the amount of product formed at equilibrium.
- Enzymes simply accelerate the time to reach equilibrium.
Enzymes Lower Activation Energy
- Enzymes lower activation energy in reactions using alternative routes.
- This alternate route is represented by a lower activation energy peak on a reaction progress diagram.
Changes in Transition State
- Transition state without enzyme is highly unstable requiring high activation energy.
- Transition state with enzyme is more stable, requiring less activation energy, through intermediate formation.
Enzyme Rates
- Enzymes dramatically increase reaction rates from billions to quadrillions of times faster in some cases.
What Enzymes Need To Work
- Some enzymes function without other compounds .
- Some enzymes require coenzymes generated from vitamins (e.g. NADH) or cofactors to function.
- Cofactors can alter enzyme conformation (shape) for better function (e.g. metal ions like Mg2+, Fe2+, Zn2+).
Definitions
- An enzyme acts as a catalyst, speeding up biochemical reactions.
- Coenzymes are vitamin-derived molecules helping enzymes.
- Cofactors are non-protein molecules (i.e. ions) aiding enzymes.
- Apoenzyme is the protein component of an enzyme requiring coenzymes to finalize functionality.
- Holoenzyme is the combination of apoenzyme and coenzyme for an active enzyme.
Enzyme Classifications
- There are six major enzyme classes based on the reaction they catalyze.
- Examples of classes include oxidoreductases (alcohol dehydrogenase), transferases (kinases), hydrolases (lipases), lyases (decarboxylases), isomerases (isomerase), and ligases (DNA ligase).
Summary
- Enzymes increase reaction rates by decreasing activation energy.
- Enzymes do not alter the equilibrium of the reaction.
- Some need cofactors/coenzymes.
- Enzymes are categorized into six classes.
Resources
- Lehninger Principles of Biochemistry (Seventh Edition, 2017) by Freeman and Company, specifically Chapter 6.
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