Enzyme kinetics uses math to quantify all of the following, except: a. An enzyme's substrate affinity b. None; all the other choices are correct O c. An enzyme's catalytic power Od. An enzyme's stability
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- A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme BGraph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.enzymes are naturally occurring catalysts responsible for various biochemical reactions. Give a modern and recent application of an enzyme used in a biochemical reaction a - the commercial or trade name of the catalyst and enzyme. b - the properties of the catalyst and enzyme (e.g., shape, size, colour, price). c - the advantages and the disadvantages of the chosen catalyst and enzyme d - catalytic reaction (e.g., the reactant, product, reaction equation, phase, selectivity, promoter, catalyst support, operating temperature & pressure).
- Explain all aspects of enzyme kinetics. You must explain all terms that relateto measuring and comparing enzyme velocity. What are the two enzyme"constants" you would teach to a senior level undergraduate course. Howwould you determine values of these under experimental conditions (i.e. invitro).Which one of the following statements is true of enzyme catalysts? a. Their catalytic activity is independent of pH. b. They are generally equally active on D and L isomers of a given substrate. c. They can increase the equilibrium constant for a given reaction by a thousand fold or more. d. They can increase the reaction rate for a given reaction by a thousand fold or more. e. To be effective, they must be present at the same concentration as their substrate.Which of the following is TRUE concerning the induced fit model of enzyme catalysis? * (One correct answer only) A. The active site can be influenced by molecules binding elsewhere on an enzyme B. The initial binding of enzyme and substrate is the most tightly bound conformation C. The induced fit must occur prior to the initial binding of enzyme and substrate in order for the reaction to proceed D. The binding of enzyme and substrate is weakest in the transition state
- Chemistry an enzyme binding equilibrium has a KD= 10 mm. What concentration of ligand (in mM) is required in order to bind 10% of the enzymeCharacterization of enzyme activity does not allow us to: a. determine how different variables affect the enzyme's ability to function b. determine the molecular composition of the enzyme c. determine the optimal environment for an enzyme to function d. determine the effect of inhibitors on the enzymeSuppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme?Select all that apply A.the active site of the enzyme must be rigid B.the active site of the enzyme must be flexible C.only one substrate could be converted to product by the enzyme D.the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures E.the entire enzyme must be rigid
- The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (uM) 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Km of the inhibited enzyme reaction?How does the average reaction rate differ from an instantaneous reaction rate? © A. The average reaction rate is how quickly the reaction proceeds over time. An instantaneous reaction rate is how quickly the reaction proceeds at a specific time. B. The average reaction rate is how quickly the reaction proceeds at a specific time. An instantaneous reaction rate is how quickly the reaction proceeds over time. C. The average reaction rate is how quickly the reaction proceeds over time considering the reactants. An instantaneous reaction rate is how quickly the reaction proceeds at a specific time considering the products. D. The average reaction rate is how quickly the reaction proceeds over time. An instantaneous reaction rate is how quickly the reaction proceeds compared to another reaction.What does the Michalis-Menten equation tell you? A. The velocity of an enzyme under physiological conditions B. The variation of enzyme activity as a function of [substrate] C. The quantity of reactant that disappears per unit time D. A and B E. B and C Vo = Vmax [S] KM + [S] Vo = Vmax® [S] KM + [S]