Use this graph to draw new curves that reflect enzyme activity foreach of the conditions in parts a-c. (Label the curves E + Act, E+Inh, and E-mut.) Then answer part d.a. The enzyme in the presence of a heterotropic allostericactivator (E + Act).b. The enzyme in the presence of a heterotropic allostericinhibitor (E + Inh).c. A mutant enzyme (E-mut) in which the predominant structurein solution consists of monomers that have a higher affinity forthe substrate than that of the tetrameric enzyme.d. Show on the plot how to determine the Km of E-mut. 28. The following graph shows the activity of an enzyme thatfunctions as a homotetramer in which substrate concentration isplotted versus vo/Vmax (ratio of the initial velocity relative to themaximum velocity).Voхешл10.80.60.40.20[Substrate] (mM)

a. The enzyme in the presence of a heterotropic allosteric activator (E + Act).An allosteric…

Answered: Use this graph to draw new curves that…

Biomedical Instrumentation Systems

1st Edition

ISBN:9781133478294

Author:Chatterjee

Publisher:Chatterjee

Chapter6: Biomedical Electrodes, Sensors, And Transducers

Section: Chapter Questions

Problem 2P

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Similar questions

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.
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?
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the 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.
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.
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.
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?
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.
Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.
Characterizing Glycolysis List the reactions of glycolysis that a. are energy consuming (under standard-stale conditions), b. are energy yielding (under standard-state conditions), c. consume ATP. d. yield ATP e. are strongly influenced by changes in concentration of substrate and product because of their molecularity. f. are at or near equilibrium in the erythrocyte (see Table 18.2).
Study Figure 19.18 and decide which of the following statements is false. Pyruvate dehydrogenase is inhibited byÂ· NIADH. Pyruvate dehydrogenase is inhibited by AÎ¤Î¡. Citrate synthase is inhibited by NADH. Succinyl-CoA activates citrate synthase. Acetyl-CoA activates pyruvate carboxylase.
Which of the following comparisons or contrasts between endergonic and exergonic reactions is false? Endergonic reactions have a positive ?G and exergonic reactions have a negative ?G Endergonic reactions consume energy and exergonic reactions release energy Both endergonic and exergonic reactions require a small amount of energy to overcome an activation barrier Endergonic reactions take place slowly and exergonic reactions take place quickly.

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