### Determining the Biochemically Relevant Substrate for an EnzymeA given enzyme is able to utilize five different substrates. The KM values have been measured for each substrate. Which substrate is most likely the biochemically relevant one in the cell? In other words, which one is most likely the predominant in vivo substrate for this enzyme? (Choose the one best answer).- **Substrate 1 with KM = 4.7 × 10^-1 M**- **Substrate 2 with KM = 1.5 × 10^-2 M**- **Substrate 3 with KM = 1.5 × 10^-8 M**- **Substrate 4 with KM = 4.7 × 10^-3 M**- **Substrate 5 with KM = 4.7 × 10^-5 M**### ExplanationThe Michaelis constant (KM) is a crucial parameter in enzyme kinetics that provides insight into the enzyme's affinity for a particular substrate. A lower KM value indicates a higher affinity, suggesting that the enzyme binds more readily to the substrate at lower concentrations. Therefore, the substrate with the lowest KM value would typically be the predominant in vivo substrate, as the enzyme will preferentially utilize this substrate at physiological concentrations. ### True Statements About the Citric Acid (TCA) Cycle:*(Choose all correct answers)*- ☐ Decarboxylation reactions are part of the citric acid cycle.- ☐ Reduced coenzymes NADH and FADH2 are produced as products of the citric acid cycle.- ☐ This is an aerobic pathway.- ☐ The major products of the citric acid cycle are NAD+, FAD, and ATP.- ☐ The pathway occurs in the cytosol of eukaryotic cells.- ☐ The pathway occurs in the mitochondrial matrix of eukaryotic cells.When explaining the citric acid cycle or Tricarboxylic Acid (TCA) cycle, it may be essential to note the importance of each statement. This would include elaborating on key concepts such as:1. **Decarboxylation Reactions:** Types of reactions involved in the cycle.2. **Reduced Coenzymes:** The role and importance of NADH and FADH2.3. **Aerobic Pathway:** Why oxygen is necessary for the process.4. **Major Products:** Understanding all the molecules produced and their significance.5. **Cellular Location:** Differentiating where in the cell this process occurs, especially between eukaryotic and prokaryotic cells.Any student studying cellular respiration or related topics would benefit from a deeper dive into each of these aspects to thoroughly comprehend the complexity and functionality of the TCA cycle.

The KM of an enzyme describes the substrate concentration at which half the enzyme's active sites…

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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on When testing the effect of substrate concentration on the reaction rate, there comes a point at which increasing the substrate concentration has no effect on the reaction rate. That is, the reaction rate remains the same and no longer increases. Which of the statements below would explain this? Select one: O A. The enzyme is denatured OB. The substrate is denatured OC. All available enzymes are saturated or full with substrates. OD. The enzyme concentration is too high
In the same kinetics experiment above without the inhibitor, what is the fraction of occupied enzyme at substrate concentration 1microM ? How about when it's 1mM ?
Enzyme X has a Km of 2 µM and a kcat of 104 s1. In the presence of an inhibitor, Km increases to 4 µM but kcat doesn't change. Is the inhibitor competitive, uncompetitive, or mixed? And what are the value(s) of a and/or a'? Choose N/A if not applicable. Inhibitor = [ Select ] [ Select ] a = a'? = [ Select]
200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.
I need help with parts d-g a.) For Ado: catalytic efficiency = 4.18 x 106 M-1s-1 For ATP: catalytic efficiency = 12.1 x 107 M-1s-1 b.) Both specificity constants are below the diffusion limit so neither substrate is limiting the reaction rate due to diffusion c.) Line weaver Burk equation for AdoK enzyme with Ado substrate: y = 0.68x + (2.04 x 104), where y = 1/vo and x = 1/[Ado]
An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
.When saturated with substrate, an enzyme has a maximum initial rate of 110 umoles of substrate converted to product per second. At a substrate concentration of 100 µM, the same enzyme converts substrate to product at a rate of 0.010 mmoles/sec. Assuming that Michaelis- Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2 x 10 M.
An enzyme catalyzes the reaction M↽−−⇀N M ↽ − − ⇀ N . The enzyme is present at a concentration of 2.0 nM 2.0 nM , and the ?max V max is 2.1 μM s−1 2.1 μM s − 1 . The ?m K m for substrate M M is 6.3 μM 6.3 μM . Calculate ?cat k cat .What values of ?max and ?m would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an α′ of 1.9?
for the table below make a graph call it Factors vs Rate of Enzyme Activity rules: data points must be an x or circled dot, must be on grid papaer and half the page minimum size, the independant variable on the x axis and dependant variable on the y axis, must include titles
-Inhibitor +Inhibitor [S] (mM) V0&νβσπ;(μmol/sec). νο&νβσπ: &ν βσπ (μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Vmax of this enzyme WITH iinhibitor?
2. The enzymatic reaction rate r is given by equation 2 below as a function of substrate concentration Cs and kinetics parameters KM and rmax. Using linear and nonlinear regression in excel, evaluate the kinetic parameter constants of a biosystem given the gathered data from a series of batch runs
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.

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