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Questions and Answers
What is the structure where the substrate binds in an enzyme?
Which of the following is a common co-factor for many enzymes?
What is the term for the point at which the substrate runs out and the enzyme reaction reaches equilibrium?
What is the method that allows measurement of enzyme activity live and in real time?
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What factor can affect the rate of reaction in an enzyme?
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What type of RNA exhibits enzymatic activity and catalyzes splicing reactions?
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What is the structure where the enzyme reaction is measured at the initial rate of reaction?
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What is the purpose of the Beer-Lambert law in discontinuous assay?
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What does Km represent in the Michaelis-Menten equation?
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What is the Vmax in enzyme kinetics?
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Which method can be used to determine Km and Vmax?
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What happens to enzymes at extreme pH or temperature?
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Why do some enzymes exhibit a 'bell-shaped' pH profile?
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What does the Beer-Lambert law help determine in spectrophotometry?
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In enzyme kinetics, what does a higher Km value indicate?
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What is the Michaelis-Menten equation used to describe enzyme kinetics?
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True or false: The Michaelis-Menten equation can be derived using assumptions and rate equations?
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True or false: Km is the substrate concentration that gives a rate equal to half of Vmax?
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True or false: Enzymes from thermophilic bacteria are exceptions to the general effect of temperature on enzyme activity?
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True or false: The pH optimum of an enzyme is the highest point on the bell-shaped pH curve due to the ionization of two specific amino acid residues?
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Study Notes
Enzyme Structure and Function
- Enzymes are biological catalysts, and most are proteins.
- Enzyme structures include: substrate active site where substrate binds, and the enzyme-substrate complex (ESC) formed when substrate binds to the active site.
- Many enzymes have co-factors, such as metal ions (e.g., Fe2+, Cu+) or coenzymes/prosthetic groups (e.g., FAD).
Exception to the Rule
- Catalytic RNA, known as ribozyme, exhibits enzymatic activity and catalyzes splicing reactions to produce mature mRNA, making it an exception to the rule that most enzymes are proteins.
Enzyme Kinetics and Activity
- The initial rate of reaction is measured to understand enzyme kinetics.
- Plateau formation occurs when substrate runs out or the enzyme reaction is reversible and reaches equilibrium.
- Factors affecting the rate of reaction include: substrate concentration, temperature, and pH.
Methods to Measure Enzyme Activity
- Continuous assay: allows measuring enzyme activity live and in real-time as the reaction proceeds.
- Discontinuous assay: involves stopping the reaction at various points to measure the activity of products formed.
- Spectroscopy is commonly used to measure enzyme activity, requiring either the substrate or product to absorb light or UV at a specific wavelength.
- Coupled reactions: when neither the enzyme-substrate nor the product absorbs light.
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Description
Test your knowledge of enzymes and catalysts with this quiz. Explore topics such as enzyme structures, co-factors, and the exceptional case of catalytic RNA. Challenge yourself with questions about the active site, substrate binding, and more.
