EFFECT OF pH ON ENZYME ACTIVITY Results: Tube 1 Tube 2 Tube 3 Time in Minutes Iodine Benedict's Iodine Benedict's Iodine Benedict's (+) (orange-red precipitate) 30 + (+) + 15 (orange-red precipitate) + (+) + 15 (brick-red precipitate) (+) + 15 + (brick-red precipitate) Note: Mark (+) if the blue color appears and (-) if no blue color appears in iodine test. (+) if precipitate is formed and note the color of the ppt. and (-) if no precipitate is
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- Studies at diff erent pH’s show that an enzyme has two catalytically important residues whose pKs are ∼4 and ∼10. Chemical modifi cation experiments indicate that a Glu and a Lys residue are essential for activity. Match the residues to their pKs and explain whether they are likely to act as acid or base catalysts.A histidine side chain is known to play an import-ant role in the catalytic mechanism of an enzyme; how-ever, it is not clear whether histidine is required in its pro-tonated (charged) or unprotonated (uncharged) state. Toanswer this question you measure enzyme activity over arange of pH, with the results shown in Figure Q2–1. Whichform of histidine is required for enzyme activity?Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
- Sodium fluoroacetate (FH2CCOO- Na+) is highly toxic. Patients with fluoroacetate poisoning accumulate citrate and fluorocitrate in their cells. Which enzyme is inhibited by fluoroacetate for this to occur? Explain.The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow.
- Many enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax [S]/([S] + Km)where Vmax = maximum velocity, [S] = concentration ofsubstrate, and Km = the Michaelis constant.It is instructive to plug a few values of [S] into theequation to see how rate is affected. What are the rates for[S] equal to zero, equal to Km, and equal to infinite concen-tration?The activity of an enzyme requires a glutamic acid to display its -COOHfunctional group in the protonated state. Suppose the pKa of the -COOHgroup is 4.07.(a) Will the enzyme be more active at pH 3.5 or 4.5? Explain.(b) What fraction of the enzymes will be active at pH = 4.07? Explain.(c) At what pH will the enzyme show 78% of maximal activity?Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
- a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?Why is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!Trend observed in graph and conclusion about the effect of temperature on enzyme activity. i) include a concise description of the trend observed in the graph shown in question 3 above, and explain this trend using the language presented in this unit and your biochemical knowledge of enzymes and reactions. In your conclusion, provide a logical argument supported by molecular theory that would explain any change observed in enzyme activity.