6. An enzyme catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM/s. What is the reaction velocity when the substrate concentration is (a) 0.25 mM (b) 1.5 mM, and (c) 10 mM?
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Solved in 2 steps
- 1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? ExplainEnzyme A catalyzes the reaction S → P and has a KM of 50 μM and a Vmax of 100 nM ∙ s−1. Enzyme B catalyzes the reaction S → Q and has a KM of 5 mM and a Vmax of 120 nM ∙ s−1. When 100 μM of S is added to a mixture containing equivalent amounts of enzymes A and B, after 1 minute which reaction product will be more abundant: P or Q?Enzyme A catalyzes the reaction S → P and has a KM of 50 μM and a Vmax of 100 nM s–1. EnzymeB catalyzes the reaction S → Q and has a KM of 5 mM and a Vmax of 120 nM s–1. When 100 μM ofS is added to a mixture containing equal amounts of enzymes A and B, which reaction product (Por Q) will be more abundant after 1 minute of reaction?
- An enzyme catalysed reaction has a Km of 8 mM and a Vmax of 13 nM.s-1. Use the Michaelis-Menten equation to calculate the reaction velocity when the substrate concentration is 18 mM.1. Can you describe how electrostatic and steric considerations may lead to preferential stabilization of the transition state at an enzyme active site? 2. What factors are involved in “transition-state complementarity”?In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
- An enzyme is discovered that catalyzes the chemical reaction A team of motivated researchers sets out to study the enzyme, which they callhappyase. They find that the kcat for happyase is 600 s−1 and carry out several additional experiments.When [Et] = 20 nM and [SAD] = 40 μM, the reaction velocity, V0, is 9.6μM s−1. Calculate Km for the substrate SAD.1. As seen in the picture: - What kind of inhibition (competitive, uncompetitive, mixed) is involved? - Calculate Vmax and Kmax in the absence and presence of inhibitor A Show complete solution.An enzyme is found that catalyzes the reaction X ⇌ Y. Researchers find that the Km for the substrate X is 4 μM, and the kcat is 20 min−1.(a) In an experiment, [X] = 6 mM, and V0 = 480 nM min−1. What was the [Et] used in the experiment?(b) In another experiment, [Et] = 0.5 μM, and the measured V0 = 5 μM min−1. What was the [X] used in the experiment?(c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an α of 10. In an experiment with the same [Et] as in (a), but a different [X], an amount of Z is added that reduces V0 to 240 nM min−1. What is the [X] in this experiment?(d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.
- For some Enzyme, the Vmax is 18 micromols/min, Km is 400 microM. If the substrate concentration is 100 microM, what is the velocity of the reaction?Assume you have an enzyme that catalyzes a reaction that breaks down dopachrome. At t = 0 s, the absorbance at 475 nm is 0.2 when you add the enzyme. At t = 30 s, would you expect the absorbance to be less than or greater than 0.2?5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?