1. An enzyme catalyzes a reaction at a velocity of 20 µmol/min when the concentration of substrate (S) is 0.01 M.The Km for this substrate is 1 x 10-5 M. Assuming that Michaelis-Menten kinetics are followed, what will thereaction velocity be when the concentration of S is (a) 1 x 10-5 M and (b) 1 x 10-6 M?

First we need to convert the unit of velocity to mol/min.Now let's find Vmax using the…

Answered: An enzyme catalyzes a reaction at a…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 4P

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Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
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.
Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
Based on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.
Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?

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