Questions and Answers
What is a substrate?
The specific reactant that an enzyme binds to.
What is an enzyme/substrate complex?
A complex that forms when an enzyme binds to its specific substrate.
What is the active site of an enzyme?
A restricted region on the enzyme molecule that binds to the substrate.
What does induced fit refer to?
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How does an enzyme's active site lower activation energy? One way is by _____ substrates correctly.
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Each enzyme has an optimal _____ and pH.
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What are cofactors?
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What are coenzymes?
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What are competitive inhibitors?
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What are noncompetitive inhibitors?
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What is an allosteric site?
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What is allosteric regulation?
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What is an allosteric activator?
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What is an allosteric inhibitor?
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What is allosteric activation?
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What is allosteric inhibition?
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What is cooperativity?
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What is enzyme feedback inhibition?
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Study Notes
Enzymatic Concepts
- Substrate: The specific reactant that binds to an enzyme for a biochemical reaction.
- Enzyme/Substrate Complex: The temporary structure formed when an enzyme and substrate interact.
- Active Site: A specialized region on an enzyme where substrate binding occurs, crucial for catalytic activity.
- Induced Fit: A model explaining how the active site of an enzyme adapts upon substrate binding to enhance catalysis.
Mechanism of Enzyme Action
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Activation Energy Reduction: Enzymes lower activation energy through:
- Correct substrate orientation
- Strain on substrate bonds
- Creating a favorable microenvironment
- Covalent interactions with substrates
Environmental Effects on Enzymes
- Temperature and pH Sensitivity: Each enzyme has optimal conditions; for humans, it's approximately 37°C and pH 7.
Enzyme Helpers
- Cofactors: Non-protein chemical compounds that assist enzyme function; can be organic (coenzymes) or inorganic; often derived from vitamins.
- Coenzymes: Organic cofactors that play a role in enzyme activity, necessary for catalysis.
Inhibition Mechanisms
- Competitive Inhibitors: Molecules that compete with substrates by binding to an enzyme's active site.
- Noncompetitive Inhibitors: Bind to a different site on the enzyme, altering its shape and function, making the active site less effective.
Regulatory Sites and Mechanisms
- Allosteric Site: A distinct site on an enzyme, separate from the active site, where regulatory molecules can bind.
- Allosteric Regulation: Modulation of enzyme activity through the binding of effector molecules at allosteric sites.
Types of Allosteric Modulation
- Allosteric Activator: A molecule that binds to an allosteric site, enhancing enzyme activity.
- Allosteric Inhibitor: Binds to an allosteric site, leading to enzyme inactivity by changing active site shape.
Specialized Allosteric Functions
- Allosteric Activation: Increase in enzyme activity upon activator binding to its regulatory site.
- Allosteric Inhibition: Conformational changes in the enzyme prevent substrate binding due to inhibitor binding at the allosteric site.
- Cooperativity: A phenomenon where substrate binding at one active site increases the likelihood of substrate binding at other active sites, amplifying overall enzyme activity.
Metabolic Control
- Enzyme Feedback Inhibition: A regulatory mechanism where the end product of a metabolic pathway inhibits an upstream process, preventing overproduction and conserving resources.
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Description
Test your knowledge on key concepts related to allosteric enzymes and their inhibition. This quiz covers important terms like substrate, enzyme/substrate complex, active site, and induced fit. Expand your understanding of enzymatic functions and mechanisms.