The enzyme carbonic anhydrase can catalyze CO2 hydration according to the reactionbelow:CO2 + H2OThe initial rates for the hydration reactionlisted in the table to the right were obtainedusing an initial enzyme concentration of 2.3nM and a temperature of 0.5 °C. Use aLineweaver-Burk plot to find Km, theMichaelis constant, and k2, the turnover rate,for carbonic anhydrase in this reaction.HCO3 + H+Rate (M s¹)[CO2] mM2.78×10-55.00×10-51.252.58.33×10-51.67×10-45.020.0

Answered: The enzyme carbonic anhydrase can…

Physical Chemistry

2nd Edition

ISBN:9781133958437

Author:Ball, David W. (david Warren), BAER, Tomas

Publisher:Ball, David W. (david Warren), BAER, Tomas

Chapter20: Kinetics

Section: Chapter Questions

Problem 20.38E: List at least four experimentally determined parameters that you, an experimenter, can define when...

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Are the following processes examples of homogeneous or heterogeneous catalysis? a Hydrolysis of immiscible ethyl acetate (l) in an aqueous basic solution. b Conversion of NOX gases to N2 and O2 by platinum metal. c Decomposition of atmospheric ozone by NO gas. d Oxidation of ethyl alcohol, C2H5OH, by the enzyme alcohol dehydrogenase, ADH, to acetaldehyde in the body. e Solid-state conversion of C graphite to C diamond by transition metal additives at high pressure.
What are the rate laws of mechanisms 1 and 2 for oscillating reactions if the second reactions were the rate-determining steps?
List two ways that enzyme catalysis of a reaction is superior to normal conditions.
384 Enzyme Reactions and Kinetics Q6.3: What kinetic parameter reveals the most information about how well an enzyme works? Describe this kinetic parameter in terms of the turnover number and the Michaelis constant and provide an explanation for why triosephosphate isomerase is considered to be ~16,000 better than pepsin when this kinetic parameter is used to compare these two enzymes.
The protein catalase catalyzes the reaction 2H,0,(aq) – 2 H,0O(0) + 0,(g) and has a Michaelis–Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s-1. The total enzyme concentration is 0.016 µM and the initial substrate concentration is 6.58 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax ) for this enzyme. Rmax mM-s- Calculate the initial rate, R (often written as Vo), of this reaction. R = mM-s-
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For the gas phase decomposition of t-butyl propionate,C2H5COOC(CH3)3(CH3)2C=CH2 + C2H5COOHthe rate constant in s-1 has been determined at several temperatures. When ln k is plotted against the reciprocal of the Kelvin temperature, the resulting linear plot has a slope of -1.97×104 K and a y-intercept of 29.5. The value of the rate constant for the gas phase decomposition of t-butyl propionate at 530 K is _______s-1. (Enter your answer to one significant figure.)
An enzyme catalyzes a reaction with a KmKm of 7.507.50 mM and a VmaxVmax of 3.00 mM⋅s−1.3.00 mM⋅s−1. Calculate the reaction velocity, v0,v0, for each substrate concentration. a. [S]=4.00mM*s^-1 b. [S]=7.5mM*s^-1
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An enzyme kinetics experiment is carried out by adding 1.00mg of a 50.0kDa enzyme into a total volume of 50uL of buffer, and measuring the initial rates while adding increasing amounts of substrate (1 Da = 1 g/mol). The calculated Vmax from this series of experiments was 30.5mM/s. Calculate the turnover number for the enzyme.
For the gas phase isomerization of cyclobutene,(CH2)2(CH)2CH2=CHCH=CH2the rate constant has been determined at several temperatures. When ln k in s-1 is plotted against the reciprocal of the Kelvin temperature, the resulting linear plot has a slope of -1.64×104 K and a y-intercept of 30.1. The activation energy for the gas phase isomerization of cyclobutene is __________kJ/mol.
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