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 which is normally 13 units. The enzyme activity data are presented below. Does this treatment affect enzyme activity? TREATED – 35, 45, 36, 11, 41, 29, 38
Q: Select all the intermediates that would be isolated if the enzyme malate dehydrogenase was inhibited
A: Introduction : A decrease in enzyme-related processes, enzyme production or activity of the enzyme…
Q: 1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of…
A: Background information Km is that substrate concentration at which velocity is half of the maximum.…
Q: The KM for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8 × 10−2 M, and the KM…
A: The Michaelis-Menten equation, at some unique substrate concentration, defines the rate of catalysis…
Q: Aldolase enzymes have the following rate constants. k₁ = 10³M ¹s¹, k-₁ = 4.4x10 s ¹, k₂ = 10's-¹ -1…
A: Consider the following single substrate (S) enzyme (E) catalyzed reaction mechanism given below E +…
Q: what is the Km for the following enzyme michael menten
A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…
Q: The turnover number of the enzyme fumarase that catalyzes the reaction,
A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…
Q: 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: The general depiction of an enzyme catalyzed reaction is as follows; Enzyme kinetics is given by…
Q: An enzyme-catalyzed reaction is allowed to proceed for 3.4 minutes under steady-state conditions…
A: Ans- Concentration of Product = 6.3uM Time for which the reaction has been…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: Enzymes are biological catalysts that help chemical processes occur faster. Enzymes are proteins…
Q: The following experimental data were obtained for the kinetics of the enzyme reaction Glucose + ATP…
A: Enzyme kinetics are explained by Michaelis Menten equation shown below: V=VmaxSKm+S Here, V is…
Q: Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at…
A: Enzymes catalyse the biochemical reactions by decreasing the activation energy. Enzyme kinetics are…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: Asked : Type of inhibitor PQR
Q: what each term means and why it applies to either anabolism or catabolism. a) endergonic b)…
A: Anabolism is the formation of large molecules from the smaller one through biological reactions,…
Q: If you wanted to figure out what the optimum temperature is for catalase, how would you set up your…
A: Hi! Thank you for the questions. As you have posted multiple questions, I will be answering the…
Q: Calculate the Km of the above enzyme.
A: This is the concept of enzyme-catalyzed reaction which is given by Michaelis-Menten. The equation…
Q: Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach).…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…
Q: In an enzyme experiment, when the enzyme is added only to the substrate, the Vmax value is 0.828 and…
A: Enzymes are proteins with catalytic function. They are sensitive to temperature, the potential of…
Q: concentration of each enzyme and with [X] = 1 µM. Which curve corresponds to which enzyme? Explain.
A: Given, the substrate concentration is [X] =1 μM Km of enzyme A = 2.0 μM Km of enzyme B = 0.5 μM
Q: Q is an analog of substrate A that binds to enzyme X and produces the following kinetics: [A] V0…
A: The mathematical equation for Lineweaver-Burk plot: 1V=KmVmax[S]+1Vmax
Q: Catechol, a substance found in plants, reacts with oxygen to produce benzoquinone and water. The…
A: Enzymes are proteins that act on specific molecules called substrates, and result in formation of…
Q: If the enzyme lactase has a Vo of 0.40 mM per minute when [S] = 1.25 mM, and a Vo of 1.0 mM per…
A: If an enzyme follows Michaelis-Menten Kinetics, a plot of the reciprocal of the reaction velocity…
Q: For the following calculations, please provide your answers in whole numbers (no decimals). A…
A: Enzymes are biocatalysts which increase the rate of chemical reaction by decreasing the activation…
Q: H2O2 + catalase = 2 H2O2 + O2, is an example of what enzyme specificity? * A. Stereochemical B.…
A: Catalase is an enzyme seen in all living organisms and they are responsible for the neutralization…
Q: Which of the following explains why the Benedict’s test was negative for tube 2 (amylase and starch…
A: Amylase is a type of enzyme that helps to digest the food consumed by an organism. It is found…
Q: An attempt was made to inhibit Enzyme X by adding compounds M and L. The results are summarized in…
A: Inhibitors are substances that inhibit the enzyme and decrease enzyme activity. Inhibitors are…
Q: Assume that in a certain cell, the ratio of products/reactants or Keq - 809.5 (Keq is dimensionless)…
A: Enzymatic reactions usually follow the Michaelis-Menten kinetics except for the allosteric enzymes.…
Q: A research group discovers a new version of happyase, which they call happyase*, that catalyzes the…
A: Enzyme catalyzed reactions can be characterized using the Michaelis-Menten equation. The initial…
Q: Catalase is the enzyme. experiment with h2O2 3. What is the marker for the enzyme’s optimum…
A: Enzymes are proteins which accelerate the rate of a biochemical reaction. Optimum activity of an…
Q: the RHR, OHR, and the balanced overall reaction of the voltaic cell
A:
Q: Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of…
A: Proteins that catalyze all the biochemical reactions in the body are called enzymes. They decrease…
Q: J. C. Servaites, in Plant Physiol. (1985) 78:839–843, observed that Rubisco from tobacco leaves…
A: Rubisco stands for Ribulose 1,5-bisphosphate carboxylase-oxygenase. It is an enzyme that helps in…
Q: hat is the initial velocity measurement for the hydrolysis of 50 μM amoxicillin by the enzyme
A: Generally, the initial velocity is the velocity of the object before the effect of acceleration that…
Q: effect of the temperature and ph on amylase temperature explain what is the purpose of this lab,
A: Starch Plants perform photosynthesis in the presence of sunlight using water and carbon dioxide to…
Q: The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried…
A: Enzymes are proteins. They are biological catalysts. Tertiary and quaternary structures are crucial…
Q: What is the minimum and maximum pH in which Enzyme X will work? What is the optimal (best) pH? Rate…
A: The enzymes are proteinaceous molecules that helps in accelerating the rate of the reaction that is…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: Vmax km Competitive remains same increases Non Competitive Decreases remains same…
Q: Use the plot (below) to estimate values of KM and Vmax for an enzyme-catalyzed reaction. Use 1…
A: Michaelis Menten (MM) kinetics was developed by Canadian physician Maud Menten and German biochemist…
Q: Write a series of balanced equations and a summary equation for the reactions of the glucose–alanine…
A: Glucose-alanine cycle: It is the series of reaction in which amino groups and carbons from muscle…
Q: In Lineweaver Burk plot: O a. The slope of the plot is the Vmax/Km O b. The intercept on X-axis is…
A: The study of the rates of enzyme-catalyzed chemical reactions is known as enzyme kinetics. The…
Q: Assume that in a certain cell, the ratio of products/reactants or Keq = 745.4 (Keq is dimensionless)…
A: The Reaction quotient or Q is given as the Q = (Product of concentrations of products)/(Product of…
Q: The initial rate for an enzyme-catalyzed reaction has been determined at several substrate…
A: The substrate concentration and velocity is put into the following chart:
Q: Consider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence…
A: The reciprocal of the given data is as follows: 1/S (Mol-1) 1/V (min/micromol) Uninhibited 1/V…
Q: As a result of an experiment following measurements were obtained from a cell: ATP concentration of…
A: Gibbs energy: ∆G = ∆G°' + 2.303 RTlogQ∆G = Actual free energy∆G°' = standard energyR = Ideal gas…
Q: give the properties of the enzyme (e.g., shape, size, colour, price). a) amylase b) invertase
A: Enzymes are generally considered biological catalysts. This is because in presence of them a…
Q: What is the percent change for the enzyme active at 40 C compared to 25 C* 220 200 180 160 e…
A: Enzymes are proteins that act as a catalyst to speed up chemical reactions. A catalyst is a…
Q: The following are the negative regulators of phosphofructokinase except Select one: a. AMP +b. H…
A: Introduction: The series of chemical reaction that covert glucose into pyruvate and ATP is known as…
Q: Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten…
A: Enzymes serve as biological catalysts that speed up reactions and increase the reaction rate by…
Q: If 10 µM enzyme was used to obtain the data in the summary plot below, k-cat = ________________…
A: An enzyme is a type of biological catalyst that aids in the acceleration of chemical reactions.…
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 which is normally 13 units. The enzyme activity data are presented below. Does this treatment affect enzyme activity?
TREATED –
35, 45, 36, 11, 41, 29, 38
Trending now
This is a popular solution!
Step by step
Solved in 2 steps
- 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 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 . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
- The 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.The 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 1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…The 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.
- For an experiment that uses different concentrations of avocado catalase to determine how it affects the rate of the reaction with hydrogen peroxide, what type of graph would be appropriate for the results?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 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:
- What is the rate of the reaction at 20 sec for each of the enzyme concentration. Show calculationThe 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?what is the Km for the following enzyme michael menten