Seven tomato plants were treated with chlorogenic acid (and seven control plants were not treated) to determine if this acid influences the activity of the enzyme o-diphenol oxidase in their leaves. The enzyme activity data are presented below. Does this treatment affect enzyme activity? TREATED – 35, 45, 36, 11, 41, 29, 38 NOT TREATED – 10, 18, 82, 91, 78, 11
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Seven tomato plants were treated with chlorogenic acid (and seven control plants were not treated) to determine if this acid influences the activity of the enzyme o-diphenol oxidase in their leaves. The enzyme activity data are presented below. Does this treatment affect enzyme activity?
TREATED – 35, 45, 36, 11, 41, 29, 38
NOT TREATED – 10, 18, 82, 91, 78, 11
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- J. C. Servaites, in Plant Physiol. (1985) 78:839–843, observed that Rubisco from tobacco leaves collected before dawn had a much lower specific activity than the enzyme collected at noon. This difference persisted despite extensive dialysis, gel filtration, or heat treatment. However, precipitation of the predawn enzyme by 50% (NH4)2SO4 restored the specific activity to the level of the noon-collected enzyme. Suggest an explanation.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 BlueThe enzyme hexokinase catalyzes the first step/reaction of glycolysis. If equal amounts of an inhibitor of hexokinase are added to flasks Y and Z below, and the volume of their respective balloons is calculated 60 minutes later, explain the results you would expect if the inhibitor is A) a competitive inhibitor and B) and allosteric inhibitor? Flask Y: 100mL H2O, 3g glucose, 6.5 g yeast Flask Z: 100mL H2O, 6g glucose, 6.5 g yeast A) Competitive inhibitor added to Y and Z, expected results and explanation: B) Allosteric inhibitor added to Y and Z, expected results and explanation:
- A scientist is studying the enzyme X which is an important point of regulation in the metabolism of the inhabitants of Sumeru. He developed four Akademiyan-derived compounds which may possibly work against this enzyme, and tested using an eudiometer the metabolic rate of the sample cell lines. Data are below. Time for each compound (min) Eudiometer volume reading (mL) A B C D 0 83.1 62.6 89.0 66.4 5 83.2 100.6 90.2 71.4 10 83.2 83.6 95.0 77.2 15 83.2 83.6 100 84.6 20 83.3 110.8 104.6 88.2 Show the properly labeled volume versus time plot for each eudiometer, with the equation of the line and R2. What is the most effective inhibitor among the four compounds? It was found that the most effective inhibitor exhibits uncompetitive inhibition. Illustrate the Lineweaver-Burk plots of uninhibited and inhibited enzyme X with properly labeled axes.One mg of enzyme has a Km of 5 x 10-5 M and a Vmax of 700 µmoles/liter/sec. The observed velocity in a cell extract containing one mg of enzyme and 2 x 10-4 M substrate was found to be 200 µmoles/liter/sec. This observation indicated that an inhibitor was present in this cell extract. True or FalseThe following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. Morphine is a non-competitive inhibitor of carbonic anhydrase. Draw on the same Lineweaver-Burke plot as above a graph showing the effect of a concentration of morphine that inhibits the first enzyme such that it reduces the Vmax to ½ its maximal value. Make sure to put in sample data points. Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.
- I have successfully extracted crude enzymes from the cocoa pod husk, an agriculture waste. The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.An enzyme catalyzes the conversion of mannose to glucose. The KM of the enzyme is 0.135 μM and the vmáx is 65 μmol/min. What is the rate of the reaction when theconcentration of mannose is 2.0 μM? a. 30.4 μM/min b. 60.9 μmol/min c. 65 μmol/min d. 60.9 μM/minThe optimal temperature for human amylase is very different than that from plants such as barley. What would you predict is the optimal temperature for human amylase in Celsius?
- An enzyme “happyase” catalyzes the reaction: sad to happy. For total enzyme concentration of 4 nM, the measured Vmax was 3.2 μM/S. What is the kcat for happyase ______ and what is its unit _____ (shown in fraction format, eg. M/S)A catalyst like lactase that assists in the metabolism od milk is best described as Group of answer choices homogeneous heterogeneous enzymatic non-truseable 7, What graph will demonstrate that experimental concentration data fit a second-order reaction? Group of answer choices ln[reactant] vs. time ln(k) vs. 1/T 1/[reactant] vs. time [reactant] vs. time ln(k) vs. EaThe following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.