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- . The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.1. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrationsPredict or describe the absorbance or enzyme activity at: pH = 2 pH = 14 Explain your predictions 2. Explain why the maximum initial reaction rate cannot be reached at low substrate concentrations.11. The most highly sensitive test in viral hepatitis is y-Glutamyl transpeptidase (Y-GT) increased activity in blood, which level riscs 10-15 times more than the norm (30-50 ME/L). What is the diagnostic value of this enzyme? For the answer: a) present the main properties of enzymes which activity determination in patient blood are widely uscd in enzyme diagnostics; b) explain the y-Glutamyl transpeptidase (y-GT) system and present an appropriate scheme; c) give examples of other enzymes which activity is determined in the liver disorders.
- Please ASAP. Thank you. Explain these results in short answer form. Why was the slope zero for blank solution? What was the optimal concentration for peroxidase activity? Do these values make sense?Pepsin, a peptidase that hydrolyzes proteins, functions in the stomach at an optimum pH of 1.5–2.0. How is the rate of a pepsin-catalyzed reaction affected by each of thefollowing conditions? increasing the concentration ofproteins changing the pH to0 running the reaction at 0°C using lesspepsin11) Using the data above, construct Lineweaver-Burk plots. First, graph the inverse of the reaction velocity (rate of reaction) data in column II versus the inverse of the methanol concentration in column I. Then, on the same graph, plot the inverse of the reaction velocity (rate of reaction) data in column III versus the inverse of the methanol concentration in column I
- i) Re-arrange the Michaelis Menten equation so it involves the ratio [S]. Show all steps beginning Km noting any assumptions or required conditions. Km ii) Calculate the ratio [lo for the case when the rate of product formation is 68% of Vmax and the substrate is in great excess. d[P] dt : k₂ with = [E],[S] Km+[S]' [S]o Km iii) Explain, in a few sentences, why the ratio determines the ratio V Vmax V Vmax Begin by explaining the meaning of stating simply "it's the ratio...." is not sufficient. Include in your explanation the factors that effect v and Vmax. Consider what factors make v different from or equal to Vmax. Consider what Km represents concerning processes involving ES. " iv) Calculate KM at 310K at given the following rate constant information: k₁ = 17 s-¹M-1 at 300K with A = 7300 s-¹M-1 K-1₁ 6 s¹ at 300K with A = 14500 s -1 k₂ = 31 s¹ at 300K with A = 600 s-¹at what substrate concentration is v= 5.0 mM s^-1 for the enzyme catalyzed hydrolysis of trehalose?32. Between the following 4 Km values, select the one that indicates binding of the enzyme to its substrate with the highest affinity: Group of answer choices 10 nM 1000 uM 1 mM 10 pM
- 5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop aSucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…Consider the enzyme pancreatic amylase, which has an optimum pH of 7.0. How is the rate of a pancreatic amylase-catalyzed reaction affected by each of the following changes: (a) lowering the pH from 7 to 4; (b) increasing the pH from 7 to 9; (c) decreasing the temperature from 37 °C to 28 °C; (d) increasing the temperature from 37 °C to 50 °C?