Enzyme activity (Effect of temperature) Research Question How does temperature affect the activity Of the enzyme catalase? Hypothesis The higher temperature would increase Catalase activity leading to a faster reaction. Teme degrees 4 10 22 410 65+ Results Time to float disa Triall 5.85 3.06 4.00 1/29/24 Mini Lab #1 10.49 9.43 Trial a 5.70 2.86 5.26 7.86 11.36 Average 5.775 2.96 4.63 9.175 10.395 Rate Class average 5

Enzyme activity (Effect of temperature) Research Question How does temperature affect the activity Of the enzyme catalase? Hypothesis The higher temperature would increase Catalase activity leading to a faster reaction. Teme degrees 4 10 22 410 65+ Results Time to float disa Triall 5.85 3.06 4.00 1/29/24 Mini Lab #1 10.49 9.43 Trial a 5.70 2.86 5.26 7.86 11.36 Average 5.775 2.96 4.63 9.175 10.395 Rate Class average 5

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.22E

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Similar questions

Compare the lock-and-key and induced-fit models for substrate binding to an enzyme.
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With the enzyme activity results in Table 1, without plotting a graph, determine: a) b) c) Vmax (explain) Why is the velocity v constant at [S] greater than 2 x 10° M? What is the free [E] at [S] = 2 x 102 M? Table 1 [S] (mol/L) 2 x 10-1 2 x 10-2 2 x 10-3 2 x 10-4 1,5 x 10-4 1.3 x 10-5 v (umol/min) 60.00 60.00 60.00 48.00 45.00 12.00
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H20 -OH H30* (1) XS LIAIH4 (2) H2O HO, он (1) XS CH;MgBr (2) H20
The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics. Product formed (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 1000 The Km for this enzyme is approximately: 4 mM. 2 mM. 1 mM. 6 mM. 1000 mM.
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A research group discovers a neW version oI happyasee, which they nappyase", that catalyzes the chemical reaction HAPPY = SAD The researchers begin to characterize the enzyme. In the first experiment, with [E] at 4 nM, they find that the Vmax is 1.6 µM s-1. Based on this experiment, what is the kcat for happyase*? kcat 400 S In another experiment, with [E,] at 1 nM and [HAPPY] at 30 µM, the researchers find that Vo is equal to 300 nM s-1. What i the measured Km of happyase* for its substrate HAPPY? Km 10 x10–6 Incorrect Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax increases to 4.8 µM s-, and the measured Km is now 15 µM. S For the inhibitor ANGER, calculate the values of a' and a. a' 2 Incorrect 2
Find the specific Rate constant
The acid-catalyzed hydrolysis of sucrose, C12H22O11 + H₂O + H+ -> C6H12O6 + C6H12O6 + H+ is known as "inversion of sucrose" because the angle, a, by which the solution rotates polarized light changes from positive to negative as the reaction proceeds (data from 30 degree C): t/hr a 0 78 2 71 4 12 18 24 42 65.10 44.60 32.40 22.45 2.30 48 -1.96 61 -9 86 95 -15.80 -17.25 -21.15 ∞ Use this data to show that the reaction is first order and determine its rate coefficient (at 30 degree C).
An enzyme catalyzed the reaction: S -> P has a AG" value of +4.8 kJ/mol. If you start with a solution containing 500 mM substrate [S] prior to the addition of enzyme and initiating the catalyzed reaction, then what is the substrate concentration [S] after reaching equilibrium? [R = 8.315 J/ mol* K; T = 25 C] NOTE - Provide your numeric answer in mM units as a TWO digit significant figure, and do NOT include units in your answer (report the numeric answer ONLY).
What should be taken in consideration when designing an enzyme kinetics experiment so that the reaction will not be too slow or too fast? M - amount of substrate B - amount of enzyme |- temperature O - pH