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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enzyme-inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displays kinetics somehow similar to non-competitive inhibition, does this is inhibitor good to use to inhibit toxanthine oxidase in the case of hyperuricemia and gout?
For lactate dehydrogenase reaction if km for NADH is 2×10^-4 M . What concentration of it would be appropriate for determining Km for pyruvate?
Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions
Could you help propose a reasonable mechanism for the following biochemical transformation?
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?
Pyruvate carboxylase catalyzes the first step of gluconeogenesis. ATP + HCO3─ + pyruvate → oxaloacetate + ADP + Pi ∆G0’ = ─2.1 kJ mol-1 a) Calculate ΔG for this reaction under the following physiological conditions: 370C, pH 7 [pyruvate] = [HCO3─] = 4.0 mM [oxaloacetate]= 2.0 mM [ATP] = 3.5 mM [Pi] = 5.0 mM [ADP] = 1.8 mM
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
Recall that phosphonacetyl L - aspartate (PALA) is a potent inhibitor of ATCase because it mimics the two physiological substrates. However, in the presence of substrates, low concentrations of this unreactive bisubstrate analog increase the reaction velocity. On the addition of PALA, the reaction rate increases until an average of three molecules of PALA are bound per molecule of enzyme. This maximal velocity is 17-fold greater than it is in the absence of PALA. The reaction rate then decreases to nearly zero on the addition of three more molecules of PALA per molecule of enzyme. Why do low concentrations of PALA activate ATCase?
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
Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme’s catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a general-base and a general-acid catalyst, respectively. Propose a mechanism for the reaction.
make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.
Pleas draw the Fischer projection and Haworth's projection

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