Subjects

Biology

Biological molecules

Proteins

Factors affecting enzyme activity

How Enzymes Work: From Activation Energy to Cool Temperature Tricks

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Darragh Mccooe

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Subject Expert

27/04/2023

108

Structure & Function
Enzymes
biological catalysts
They speed up metabolic reactiong
They
are not changed by the reaction
be seused
They
Cene

Page 2: Enzyme Action Mechanism

This page details how enzymes interact with their substrates to form complexes. The mechanism involves precise molecular interactions at the active site.

Vocabulary: The enzyme-substrate complex (ES complex) forms when the substrate binds to the enzyme's active site.

Definition: The active site is the specific region of an enzyme where the substrate binds and the reaction occurs.

Highlight: The formation of bonds between the enzyme's amino acids and the substrate is crucial for catalysis.

View

Page 3: Enzyme Specificity

This page explores the specific nature of enzyme-substrate interactions through the lock-and-key model.

Definition: Enzyme specificity refers to an enzyme's ability to catalyze only specific reactions with particular substrates.

Vocabulary: Catabolism refers to breakdown reactions, while anabolism involves building larger molecules.

Highlight: The three-dimensional shape of the enzyme's active site precisely matches its specific substrate.

View

Page 4: Induced Fit Model and Cofactors

This page describes the induced fit model and the role of cofactors in enzyme function.

Definition: The induced fit model suggests that the active site molds itself around the substrate during binding.

Vocabulary: Cofactors are non-protein substances required by some enzymes for proper function.

Example: Metal ions like Mg2+ and Fe3+ serve as cofactors by helping to shape the active site.

View

Page 5: Prosthetic Groups and Coenzymes

This page covers additional non-protein components necessary for enzyme function.

Definition: Prosthetic groups are permanently attached non-protein molecules required for enzyme function.

Example: NAD and FAD are coenzymes that act as hydrogen acceptors in metabolic reactions.

Highlight: Enzyme activity increases with substrate concentration until all active sites are occupied.

View

Page 6: Enzyme Kinetics

This page explains how substrate concentration affects enzyme activity rates.

Definition: The limiting factor is the component that restricts the rate of reaction when present in minimal amounts.

Highlight: Reaction rates level off when either all active sites are occupied or substrate becomes limiting.

View

Page 7: Temperature Effects

This page discusses how temperature influences enzyme activity.

Highlight: Temperature increases initially speed up reactions by providing more kinetic energy.

Definition: Denaturation occurs when excessive temperature causes the enzyme's structure to break down.

Example: Optimal temperature provides maximum reaction rate before denaturation begins.

View

Page 8: pH Effects and Immobilization

This page covers pH influence on enzymes and introduces immobilization techniques.

Definition: Immobilized enzymes are physically confined within a defined space while maintaining their catalytic activity.

Highlight: Each enzyme has an optimal pH range for maximum activity.

View

Page 9: Enzyme Immobilization Methods

This page details various methods for immobilizing enzymes.

Vocabulary: Adsorption, encapsulation, entrapment, and cross-linkage are different immobilization techniques.

Example: Alginate beads can be used to entrap enzymes while maintaining their function.

View

Page 10: Advantages of Immobilization

This page discusses the benefits and drawbacks of enzyme immobilization.

Highlight: Immobilized enzymes can be reused and show improved stability.

Definition: Competitive inhibition occurs when inhibitors compete with substrates for the active site.

View

Page 11: Enzyme Inhibition

This page explains different types of enzyme inhibition.

Definition: Non-competitive inhibition occurs when the inhibitor binds away from the active site.

Highlight: The effect of competitive inhibition depends on relative concentrations of substrate and inhibitor.

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Subjects

Biology

Biological molecules

Proteins

Factors affecting enzyme activity

How Enzymes Work: From Activation Energy to Cool Temperature Tricks

Darragh Mccooe

@darraghmccooe_xfcu

2 Followers

Enzymes are essential biological catalysts that accelerate metabolic reactions without being consumed. They work by lowering the enzyme reaction activation energy required for chemical processes.

Key points:

Enzymes form an enzyme substrate active site complex through specific binding mechanisms
The lock-and-key and induced fit models explain enzyme-substrate interactions
Temperature effect on enzyme activity shows optimal function at specific temperatures before denaturation
Enzymes can be immobilized through various methods for industrial applications
Enzyme inhibition can occur through competitive and non-competitive mechanisms

27/04/2023

108

Biology

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Page 2: Enzyme Action Mechanism

This page details how enzymes interact with their substrates to form complexes. The mechanism involves precise molecular interactions at the active site.

Vocabulary: The enzyme-substrate complex (ES complex) forms when the substrate binds to the enzyme's active site.

Definition: The active site is the specific region of an enzyme where the substrate binds and the reaction occurs.

Highlight: The formation of bonds between the enzyme's amino acids and the substrate is crucial for catalysis.

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By signing up you accept Terms of Service and Privacy Policy

Page 3: Enzyme Specificity

This page explores the specific nature of enzyme-substrate interactions through the lock-and-key model.

Definition: Enzyme specificity refers to an enzyme's ability to catalyze only specific reactions with particular substrates.

Vocabulary: Catabolism refers to breakdown reactions, while anabolism involves building larger molecules.

Highlight: The three-dimensional shape of the enzyme's active site precisely matches its specific substrate.

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Page 4: Induced Fit Model and Cofactors

This page describes the induced fit model and the role of cofactors in enzyme function.

Definition: The induced fit model suggests that the active site molds itself around the substrate during binding.

Vocabulary: Cofactors are non-protein substances required by some enzymes for proper function.

Example: Metal ions like Mg2+ and Fe3+ serve as cofactors by helping to shape the active site.

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Page 5: Prosthetic Groups and Coenzymes

This page covers additional non-protein components necessary for enzyme function.

Definition: Prosthetic groups are permanently attached non-protein molecules required for enzyme function.

Example: NAD and FAD are coenzymes that act as hydrogen acceptors in metabolic reactions.

Highlight: Enzyme activity increases with substrate concentration until all active sites are occupied.

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Page 6: Enzyme Kinetics

This page explains how substrate concentration affects enzyme activity rates.

Definition: The limiting factor is the component that restricts the rate of reaction when present in minimal amounts.

Highlight: Reaction rates level off when either all active sites are occupied or substrate becomes limiting.

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Page 7: Temperature Effects

This page discusses how temperature influences enzyme activity.

Highlight: Temperature increases initially speed up reactions by providing more kinetic energy.

Definition: Denaturation occurs when excessive temperature causes the enzyme's structure to break down.

Example: Optimal temperature provides maximum reaction rate before denaturation begins.

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Page 8: pH Effects and Immobilization

This page covers pH influence on enzymes and introduces immobilization techniques.

Definition: Immobilized enzymes are physically confined within a defined space while maintaining their catalytic activity.

Highlight: Each enzyme has an optimal pH range for maximum activity.

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Page 9: Enzyme Immobilization Methods

This page details various methods for immobilizing enzymes.

Vocabulary: Adsorption, encapsulation, entrapment, and cross-linkage are different immobilization techniques.

Example: Alginate beads can be used to entrap enzymes while maintaining their function.

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Page 10: Advantages of Immobilization

This page discusses the benefits and drawbacks of enzyme immobilization.

Highlight: Immobilized enzymes can be reused and show improved stability.

Definition: Competitive inhibition occurs when inhibitors compete with substrates for the active site.

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Page 11: Enzyme Inhibition

This page explains different types of enzyme inhibition.

Definition: Non-competitive inhibition occurs when the inhibitor binds away from the active site.

Highlight: The effect of competitive inhibition depends on relative concentrations of substrate and inhibitor.

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Knowunity is the #1 education app in five European countries

Knowunity has been named a featured story on Apple and has regularly topped the app store charts in the education category in Germany, Italy, Poland, Switzerland, and the United Kingdom. Join Knowunity today and help millions of students around the world.

Download in

Google Play

Download in

App Store

4.9+

Average app rating

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Pupils love Knowunity

#1

In education app charts in 12 countries

950 K+

Students have uploaded notes

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iOS User

I love this app so much, I also use it daily. I recommend Knowunity to everyone!!! I went from a D to an A with it :D

Philip, iOS User

The app is very simple and well designed. So far I have always found everything I was looking for :D

Lena, iOS user

How Enzymes Work: From Activation Energy to Cool Temperature Tricks

Page 2: Enzyme Action Mechanism

Page 3: Enzyme Specificity

Page 4: Induced Fit Model and Cofactors

Page 5: Prosthetic Groups and Coenzymes

Page 6: Enzyme Kinetics

Page 7: Temperature Effects

Page 8: pH Effects and Immobilization

Page 9: Enzyme Immobilization Methods

Page 10: Advantages of Immobilization

Page 11: Enzyme Inhibition

Similar content

Can't find what you're looking for? Explore other subjects.

Knowunity is the #1 education app in five European countries

Knowunity has been named a featured story on Apple and has regularly topped the app store charts in the education category in Germany, Italy, Poland, Switzerland, and the United Kingdom. Join Knowunity today and help millions of students around the world.

4.9+

15 M

#1

950 K+

Still not convinced? See what other students are saying...

I love this app so much, I also use it daily. I recommend Knowunity to everyone!!! I went from a D to an A with it :D

The app is very simple and well designed. So far I have always found everything I was looking for :D

I love this app ❤️ I actually use it every time I study.

How Enzymes Work: From Activation Energy to Cool Temperature Tricks

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Page 2: Enzyme Action Mechanism

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Page 3: Enzyme Specificity

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Page 4: Induced Fit Model and Cofactors

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Page 5: Prosthetic Groups and Coenzymes

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Page 6: Enzyme Kinetics

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Page 7: Temperature Effects

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Page 8: pH Effects and Immobilization

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Page 9: Enzyme Immobilization Methods

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Page 10: Advantages of Immobilization

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Page 11: Enzyme Inhibition

Similar content

Can't find what you're looking for? Explore other subjects.

Knowunity is the #1 education app in five European countries

Knowunity has been named a featured story on Apple and has regularly topped the app store charts in the education category in Germany, Italy, Poland, Switzerland, and the United Kingdom. Join Knowunity today and help millions of students around the world.

4.9+

15 M

#1

950 K+

Still not convinced? See what other students are saying...

I love this app so much, I also use it daily. I recommend Knowunity to everyone!!! I went from a D to an A with it :D

The app is very simple and well designed. So far I have always found everything I was looking for :D

I love this app ❤️ I actually use it every time I study.