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Questions and Answers
What is the main reason why enzymes greatly enhance the rate of a reaction?
In the lock and key mechanism of enzymes, what does the 'key' represent?
Which model of enzyme-substrate interactions states that the enzyme's active site becomes complementary to the substrate only when it is bound in place?
What type of bonds typically hold together an enzyme-substrate complex?
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Which of the following is a property of enzymes?
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Enzymes are specific in their action because they...
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What happens to an enzyme when the temperature is raised too high?
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Which of the following disrupts the structure and function of enzymes by breaking ionic bonds?
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In which pH range do most enzymes function best?
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Which classification of enzymes involves the oxidation of one substrate with the simultaneous reduction of another substrate or coenzyme?
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Which type of enzyme transfers one group (other than hydrogen) from the substrate to another substrate?
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What do hydrolases catalyze in a chemical bond using water?
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Which type of enzyme rearranges the internal structure of a molecule or changes one isomer to another?
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Which type of enzyme catalyzes the joining of two substrates together using energy from ATP?
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What is the function of activators in enzyme activity?
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What is the role of coenzymes in enzyme function?
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Study Notes
Enzyme Functionality and Mechanisms
- Enzymes enhance reaction rates significantly by lowering activation energy, allowing reactions to proceed faster.
- In the lock and key mechanism, the 'key' represents the specific substrate that fits perfectly into the enzyme's active site, demonstrating enzyme specificity.
- The induced fit model explains that the enzyme's active site adapts to become complementary to the substrate only upon binding, facilitating a more dynamic interaction.
Enzyme-Substrate Complex
- Enzyme-substrate complexes are typically held together by weak interactions such as hydrogen bonds, ionic bonds, and van der Waals forces, promoting reversible binding.
Characteristics of Enzymes
- Enzymes exhibit specificity in their action because they are tailored to catalyze particular reactions, often determined by the shape and chemical properties of the substrate.
- When temperatures are raised excessively, enzymes can denature, losing their functional shape and thus their ability to catalyze reactions efficiently.
Factors Affecting Enzyme Structure
- Disruption of ionic bonds, crucial for maintaining enzyme structure, can occur due to changes in pH or exposure to certain chemicals, leading to loss of function.
- Most enzymes function optimally within a pH range of 6-8, although some require more acidic or basic environments for optimal performance.
Enzyme Classifications
- Oxidoreductases are enzymes that facilitate the oxidation of one substrate while simultaneously reducing another substrate or coenzyme.
- Transferases are enzymes that transfer functional groups (other than hydrogen) from one substrate to another, playing a crucial role in metabolism.
- Hydrolases catalyze the cleavage of chemical bonds using water, often involved in digestion processes.
- Isomerases rearrange the internal structures of molecules, converting one isomer to another, essential in metabolic pathways.
- Ligases are enzymes that join two substrates together, often using energy derived from ATP, crucial for biosynthesis.
Enzyme Regulation
- Activators enhance enzyme activity by increasing the rate of catalysis or stabilizing the active form of the enzyme.
- Coenzymes, which are organic molecules, assist enzymes by donating or accepting specific atoms, or by serving as carriers for chemical groups in enzymatic reactions.
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Description
Test your knowledge on the classification of enzymes based on their functions. Learn about examples of different types of enzymes such as hydrolases, lyases, isomerases, and more.
