Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excessuses gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A studentsearcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XOhich uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct theneweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on TableTable 1. Enzyme Kinetic DataVelocity, mM/sKmp0.0351[S], mMChaХan0.4920.06780.06150.2110.05310.02610.04510.0870.02980.01570.02110.0480.01950.00910.01420.0290.01270.00670.0081Enzyme Kinetic Parameter:ParametersVmax|Ku| Type of InhibitionMode of BindingXanthineKaempferolChlorogenic acidNANALine Weaver Burk Plot:

Kaemferol inhibitory effect on Xanthine oxidase: Enzymatic assays have shown that kaempferol…

Answered: Xanthine oxidase (XO) is the enzyme…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter25: Nitrogen Acquisition And Amino Acid Metabolism

Section: Chapter Questions

Problem 22P

See similar textbooks

Similar questions

The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
Studies were carried out to investigate some kinetic properties of alkaline phosphatase (ALP) extracted from Lepus townsendii liver. Incubation of ALP extract with 4- nitrophenylphosphate (4-NPP) formed the basis for determination of enzyme activity. Spectrophotometric method was used to assay the enzyme activity, and the kinetic constants- maximum enzyme velocity (Vmax) and Michealis-Menten constant (Km) were evaluated. Figure 2 shows the Lineweaver-Burk plot of ALP assay in the presence of inhibitor NaH;PO4 (0) and the control (+) analysis. [I]: concentration of inhibitor = 0.67 mM. 1/V, uM*min x 104 40- 30 20 y-Intercept 10 x-intercept -1/K. (1+ [1]/K)/ 12 1/[S)x 102 (M) Figure2 (i) Estimate Km and Vmax in the absence and presence of the inhibitor. (ii) What is the type of inhibition illustrated by the inhibitor? Explain.
Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1
Derive the rate law for the following enzyme reaction chain. Linear the equation you have derived as a Lineweaver-Burk type equation.
The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.
The Lineweaver-Burk plot, which illustrates the reciprocal of the reaction rate (1/v) versus the reciprocal of the substrate concentration (1/[S]), is a graphical representation of enzyme kinetics. This plot is typically used to determine the maximum rate, Vmax, and the Michaelis constant, Km, which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants Vmax and Km. What term is represented by C? Linewegver-Burk Pt 1/Vmax O A. В. -1/Km Km/Vmax C.
Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] [ES| k-1 + kz km Assume that k is negligible compared to the other rate constants. If the k is very small, it suggests that the enzyme has a Select an option affinity for its substrate, while if the if the km is very large, it suggests that the enzyme has a Select an option. affinity for its substrate. Select an option Submit You have used 0 of high Sav low moderate
Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate  delta delta G〒 on your sketch: Chemical step is rate limiting
An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Michaelis–Menten kinetics Lineweaver–Burk plot Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
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 kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table. Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1 is much larger than ?2, which of the following statements are correct? The mutant version has a higher affinity for the substrate. The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax. Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product. Based on the data table and your initial…

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS