11.Quantitative Relationships between Rate Constants to Calculate Km, KineticEfficiency (kcat/Km) and Vmax - II Triose phosphate isomerase catalyzes theconversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate.Glyceraldehyde-3-P dihydroxyacetone-PThe Km of this enzyme for its substrate glyceraldehyde-3-phosphate is 1.8 x 10-5 MWhen [glyceraldehydes-3-phosphate] = 30 μM, the rate of the reaction, v, was82.5 μmol mL-1 s-1.a. What is Vmax for this enzyme?b. Assuming 3 nm/mL of enzyme was used in this experiment (E total = 3nm/mL)for this enzyme?c. What is the catalytic efficiency (kcat/km) for triose phosphate isomerase?d. Does this enzyme reach catalytic perfection?

Kinetic parameters are Km and Vmax. They are used to determine the efficiency of an enzyme. Km is…

Answered: 11. Quantitative Relationships between…

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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KINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?
Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions
Conversion of F1,6BP to GA3P and DHAP by aldolase is striking in that it is strongly unfavorable when all species are at 1 M (∆G°’ = +22.8 kJ/mol) but favorable when the species are at their physiological conditions (∆G = -5.9 kJ/mol). Based on ∆G°’ and ∆G of aldolase and TIM, and using a reasonable physiological value of 15 mM for the concentration of F1,6BP, calculate the concentrations of GA3P and DHAP under physiological conditions (use T = 37°C). Why is the reaction so much more favorable under these conditions than when all species are at 1 M?
Select the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the above
Case Study: Enzyme Kinetics Data for new statin drug (inhibits HMG CoA reductase): ● ● I Substrate (UM) 0.5 1.0 1.5 2.5 3.5 || Rate of reaction (mm/min) 23.5 32.2 36.9 41.8 44 What are the Kms of the uninhibited and inhibited reactions? Rate of reaction in presence of 5.0 nM statin Using the above date, create a double-reciprocal (Lineweaver Burk) plot. What type of inhibition is shown by the new statin? What are the Vmax of the uninhibited and inhibited reactions? 16.67 25.25 30.49 37.04 38.91
What ion or ions are required for PYC activity? What ion or ions inhibit PYC activity? Remember, Mg2+ is the control substance, and not expected to have any effect on the enzyme’s activity.
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Many years later, in 1989, Wild, et al. revisited the idea of allosteric control of ATCase by CTP. They noted that CTP did indeed inhibit ATCase, but that the inhibition was always incomplete, even at high concentrations of CTP. They hypothesized that perhaps CTP did not act alone, but in combination with some other nucleotide. They tested the activity of ATCase in the presence of several nucleotide combinations. The results are shown in Table 3. a. What combination gives the most effective inhibition? b. What is the physiological significance of this combination? c. Revise Figure 1 to include this new information. d. Redraw Figure 2 to include this new information. How does the combination compare with the values for the nucleotides alone? Table 3: Relative specific activities for combinations of nucleotide effectors. A value greater than one indicates stimulation, a value less than one indicates inhibition. Nucleotide Effector ATP CTP GTP UTP ATP/CTP ATP/GTP ATP/UTP CTP/GTP CTP/UTP…

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