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- 33333333333333333333333 Using the table below, differentiate the effect of two varying pH levels (as indicated by by the color) to the amylase enzyme. How does pH level affects the enzymatic reaction (enzyme-substrate complex)? Tube 1 Tube 2 Tube 3 Tube 4 Ingredients StarchAmylaseBuffer pH 7 StarchAmylaseBuffer pH 2 MaltoseWaterBuffer pH 7 StarchWaterBuffer pH 7 Color (1) (2) Orange Blue(nmol/min) 30 31 32 33 34 35 A student performed a lactate dehydrogenase (LDH) assay multiple times with varying amounts of substrate added to the reaction mixture. All other conditions were kept the same. This graph shows the results observed: 100 75 10 20 30 40 Lactate concentration (nmol/ml) Why is this student not detecting a linear increase in reaction rate at higher substrate concentrations? T TTArial v 3 (12pt) * T.=,三, 日iu 4:03 PM to search 5/6/2021National Board of Medical Examiners Biochemistry Mark 36. In the presence of a metabolite (X), 6-phosphofructokinase is assayed at a fixed concentration of ATP and varying concentrations of fructose 6-phosphate. The resulting data are shown in the table. Fructose 6-phosphate (pM) 5 10 20 40 75 100 200 Velocity umoles/min 0.05 0.15 0.25 0.70 1.7 2.2 3.1 3.1 Velocity (+X) umoles/min 0.006 0.025 0. 10 0.35 1.03 16 2.9 3.1 400 Metabolite (X) is most likely which of the following substances? O A) ADP O B) AMP OC) CAMP D) Citric acid O E) Fructose-2,6-bisphosphate
- 41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax Velocity (mM.sec-) 0 024 0 036 0 053 0 060 0 061 0 062 Substrate Concentration (mM) 25 50 10 0 15 0 200 25 0 42 If the KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases, what can be said about the mode of inhibition and why? 43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the concentration of the enzyme used is 0 002 M Why is it useful to know this? 44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues Make use of relevant graphs and diagrams to explain your answerSucrase 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…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.
- 13-2. The oxidation of sugar molecules (carbohydrates) by the cell occurs according to the following reaction:C6H12O6 + 6O2 6CO2 + 6H2O + Energy GlucoseWhich or which of the following statements are true or false? Justify the false ones.A. All the energy produced by the cell is in the form of heat. B. None of the energy the cell produces is in the form of heat. C. Cellular energy is produced by a process that involves the oxidation of carbon atoms. D. The reaction supplies the cell with the essential nutrient water. E. In cells the reaction given above takes place in more than one stage. F. Many of the stages in carbohydrate oxidation involve reaction with oxygen gas. G. Some organisms carry out the reaction (above) in reverse. H. Some cells that grow in the absence of O2 produce CO2. 13.3 A highly sensitive instrument (which has not yet been invented) detects that one of the carbon atoms exhaled in Darwin's last breath when he died now resides in his blood where it is part of…The rate constant for the uncatalyzed reaction of two molecules of glycine ethyl ester to form glycylglycine ethyl ester is 0.6 M- 1s - 1. In the presence ofCo2 +, the rate constant is 1.5 x 106 M- 1s - 1. What rate enhancement does the catalyst provide?A synthetic substrate, the para-nitrophenylacetate (PNPA), is used to monitor enzyme activity of protein P. The product of the hydrolysis reaction absorbs at 410 nm with a molar extinction coefficient of 4 000 M-¹.cm-¹. 1- Write the reaction catalyzed by the protease P using the pNPA substrate. 2- The enzyme extract is too concentrated and a 1/300 dilution is needed for enzyme tests. Considering that you would need at least 600 µL of diluted enzyme extract for activity tests, indicate which volume of buffer and enzyme extract you must use for the dilution.
- 16) The graph at right shows the results of reaction rate vs. substrate concentration for a Michaelis-Menten type enzyme a. True b. False 17) The equilibrium constant for the conversion of the disaccharide sucrose to the simple sugars glucose and fructose is 140.000 reaction rate->4. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. (8) mg V₂ μmol s1 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00 0 100 200 300 [s], mM 400 500 WT (a) Estimate the KM and Vmax for the wild-type and mutant enzyme from the graph. V105A (b) Calculate the keat and keat/KM for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.Please note the following Lineweaver-Burk plot for the enzyme Virbraniumase reacting with a substrate: -0.4 . 1/V 5 4 3 2 -0.2 0 0.2 y = 5.2781x + 1.3338 R² = 0.9967 0.4 0.6 0.8 1/[S] 1 Based on the information provided, what is the Vmax for this reaction?